                         SEQUENCE LISTING

<110>  Syngenta Participations AG
       Nichols, Jason David
       Oeller, Paul William
       Ember, Brian Nelson
       Kim, Myoung Kug
 
<120>  POTENTIATION OF ENZYMATIC SACCHARIFICATION

<130>  9848-10WO

<150>  US 61/445,616
<151>  2011-02-23

<160>  5     

<170>  PatentIn version 3.5

<210>  1
<211>  529
<212>  PRT
<213>  Artificial

<220>
<223>  Synthetic construct comprising CBH I

<400>  1

Met Ser Ala Leu Asn Ser Phe Asn Met Tyr Lys Ser Ala Leu Ile Leu 
1               5                   10                  15      


Gly Ser Leu Leu Ala Thr Ala Gly Ala Gln Gln Ile Gly Thr Tyr Thr 
            20                  25                  30          


Ala Glu Thr His Pro Ser Leu Ser Trp Ser Thr Cys Lys Ser Gly Gly 
        35                  40                  45              


Ser Cys Thr Thr Asn Ser Gly Ala Ile Thr Leu Asp Ala Asn Trp Arg 
    50                  55                  60                  


Trp Val His Gly Val Asn Thr Ser Thr Asn Cys Tyr Thr Gly Asn Thr 
65                  70                  75                  80  


Trp Asn Thr Ala Ile Cys Asp Thr Asp Ala Ser Cys Ala Gln Asp Cys 
                85                  90                  95      


Ala Leu Asp Gly Ala Asp Tyr Ser Gly Thr Tyr Gly Ile Thr Thr Ser 
            100                 105                 110         


Gly Asn Ser Leu Arg Leu Asn Phe Val Thr Gly Ser Asn Val Gly Ser 
        115                 120                 125             


Arg Thr Tyr Leu Met Ala Asp Asn Thr His Tyr Gln Ile Phe Asp Leu 
    130                 135                 140                 


Leu Asn Gln Glu Phe Thr Phe Thr Val Asp Val Ser His Leu Pro Cys 
145                 150                 155                 160 


Gly Leu Asn Gly Ala Leu Tyr Phe Val Thr Met Asp Ala Asp Gly Gly 
                165                 170                 175     


Val Ser Lys Tyr Pro Asn Asn Lys Ala Gly Ala Gln Tyr Gly Val Gly 
            180                 185                 190         


Tyr Cys Asp Ser Gln Cys Pro Arg Asp Leu Lys Phe Ile Ala Gly Gln 
        195                 200                 205             


Ala Asn Val Glu Gly Trp Thr Pro Ser Ser Asn Asn Ala Asn Thr Gly 
    210                 215                 220                 


Leu Gly Asn His Gly Ala Cys Cys Ala Glu Leu Asp Ile Trp Glu Ala 
225                 230                 235                 240 


Asn Ser Ile Ser Glu Ala Leu Thr Pro His Pro Cys Asp Thr Pro Gly 
                245                 250                 255     


Leu Ser Val Cys Thr Thr Asp Ala Cys Gly Gly Thr Tyr Ser Ser Asp 
            260                 265                 270         


Arg Tyr Ala Gly Thr Cys Asp Pro Asp Gly Cys Asp Phe Asn Pro Tyr 
        275                 280                 285             


Arg Leu Gly Val Thr Asp Phe Tyr Gly Ser Gly Lys Thr Val Asp Thr 
    290                 295                 300                 


Thr Lys Pro Ile Thr Val Val Thr Gln Phe Val Thr Asp Asp Gly Thr 
305                 310                 315                 320 


Ser Thr Gly Thr Leu Ser Glu Ile Arg Arg Tyr Tyr Val Gln Asn Gly 
                325                 330                 335     


Val Val Ile Pro Gln Pro Ser Ser Lys Ile Ser Gly Val Ser Gly Asn 
            340                 345                 350         


Val Ile Asn Ser Asp Phe Cys Asp Ala Glu Ile Ser Thr Phe Gly Glu 
        355                 360                 365             


Thr Ala Ser Phe Ser Lys His Gly Gly Leu Ala Lys Met Gly Ala Gly 
    370                 375                 380                 


Met Glu Ala Gly Met Val Leu Val Met Ser Leu Trp Asp Asp Tyr Ser 
385                 390                 395                 400 


Val Asn Met Leu Trp Leu Asp Ser Thr Tyr Pro Thr Asn Ala Thr Gly 
                405                 410                 415     


Thr Pro Gly Ala Ala Arg Gly Ser Cys Pro Thr Thr Ser Gly Asp Pro 
            420                 425                 430         


Lys Thr Val Glu Ser Gln Ser Gly Ser Ser Tyr Val Thr Phe Ser Asp 
        435                 440                 445             


Ile Arg Val Gly Pro Phe Asn Ser Thr Phe Ser Gly Gly Ser Ser Thr 
    450                 455                 460                 


Gly Gly Ser Ser Thr Thr Thr Ala Ser Gly Thr Thr Thr Thr Lys Ala 
465                 470                 475                 480 


Ser Ser Thr Ser Thr Ser Ser Thr Ser Thr Gly Thr Gly Val Ala Ala 
                485                 490                 495     


His Trp Gly Gln Cys Gly Gly Gln Gly Trp Thr Gly Pro Thr Thr Cys 
            500                 505                 510         


Ala Ser Gly Thr Thr Cys Thr Val Val Asn Pro Tyr Tyr Ser Gln Cys 
        515                 520                 525             


Leu 
    


<210>  2
<211>  472
<212>  PRT
<213>  Artificial

<220>
<223>  Synthetic construct comprising CBH II

<400>  2

Met Val Val Gly Ile Leu Ala Thr Leu Ala Thr Leu Ala Thr Leu Ala 
1               5                   10                  15      


Ala Ser Val Pro Leu Glu Glu Arg Gln Ser Cys Ser Ser Val Trp Gly 
            20                  25                  30          


Gln Cys Gly Gly Gln Asn Trp Ala Gly Pro Phe Cys Cys Ala Ser Gly 
        35                  40                  45              


Ser Thr Cys Val Tyr Ser Asn Asp Tyr Tyr Ser Gln Cys Leu Pro Gly 
    50                  55                  60                  


Thr Ala Ser Ser Ser Ser Ser Thr Arg Ala Ser Ser Thr Thr Ser Arg 
65                  70                  75                  80  


Val Ser Ser Ala Thr Ser Thr Arg Ser Ser Ser Ser Thr Pro Pro Pro 
                85                  90                  95      


Ala Ser Ser Thr Thr Pro Ala Pro Pro Val Gly Ser Gly Thr Ala Thr 
            100                 105                 110         


Tyr Ser Gly Asn Pro Phe Ala Gly Val Thr Pro Trp Ala Asn Ser Phe 
        115                 120                 125             


Tyr Ala Ser Glu Val Ser Thr Leu Ala Ile Pro Ser Leu Thr Gly Ala 
    130                 135                 140                 


Met Ala Thr Ala Ala Ala Ala Val Ala Lys Val Pro Ser Phe Met Trp 
145                 150                 155                 160 


Leu Asp Thr Leu Asp Lys Thr Pro Leu Met Ser Ser Thr Leu Ser Asp 
                165                 170                 175     


Ile Arg Ala Ala Asn Lys Ala Gly Gly Asn Tyr Ala Gly Gln Phe Val 
            180                 185                 190         


Val Tyr Asp Leu Pro Asp Arg Asp Cys Ala Ala Ala Ala Ser Asn Gly 
        195                 200                 205             


Glu Tyr Ser Ile Ala Asp Gly Gly Val Ala Lys Tyr Lys Asn Tyr Ile 
    210                 215                 220                 


Asp Thr Ile Arg Gly Ile Val Thr Thr Phe Ser Asp Val Arg Ile Leu 
225                 230                 235                 240 


Leu Val Ile Glu Pro Asp Ser Leu Ala Asn Leu Val Thr Asn Leu Ala 
                245                 250                 255     


Thr Pro Lys Cys Ser Asn Ala Gln Ser Ala Tyr Leu Glu Cys Ile Asn 
            260                 265                 270         


Tyr Ala Ile Thr Gln Leu Asn Leu Pro Asn Val Ala Met Tyr Leu Asp 
        275                 280                 285             


Ala Gly His Ala Gly Trp Leu Gly Trp Pro Ala Asn Gln Asp Pro Ala 
    290                 295                 300                 


Ala Gln Leu Phe Ala Asn Val Tyr Lys Asn Ala Ser Ser Pro Arg Ala 
305                 310                 315                 320 


Val Arg Gly Leu Ala Thr Asn Val Ala Asn Tyr Asn Ala Trp Asn Ile 
                325                 330                 335     


Thr Thr Pro Pro Ser Tyr Thr Gln Gly Asn Ala Val Tyr Asn Glu Lys 
            340                 345                 350         


Leu Tyr Ile His Ala Leu Gly Pro Leu Leu Ala Asn His Gly Trp Ser 
        355                 360                 365             


Asn Ala Phe Phe Ile Thr Asp Gln Gly Arg Ser Gly Lys Gln Pro Thr 
    370                 375                 380                 


Gly Gln Leu Glu Trp Gly Asn Trp Cys Asn Ala Val Gly Thr Gly Phe 
385                 390                 395                 400 


Gly Ile Arg Pro Ser Ala Asn Thr Gly Asp Ser Leu Leu Asp Ser Phe 
                405                 410                 415     


Val Trp Ile Lys Pro Gly Gly Glu Cys Asp Gly Thr Ser Asn Ser Ser 
            420                 425                 430         


Ala Pro Arg Phe Asp Tyr His Cys Ala Ser Ala Asp Ala Leu Gln Pro 
        435                 440                 445             


Ala Pro Gln Ala Gly Ser Trp Phe Gln Ala Tyr Phe Val Gln Leu Leu 
    450                 455                 460                 


Thr Asn Ala Asn Pro Ser Phe Leu 
465                 470         


<210>  3
<211>  715
<212>  PRT
<213>  Artificial

<220>
<223>  Synthetic construct comprising EG

<400>  3

Met Ala Thr Gln Gly Ala Leu Asp Ser Ala Val Thr Ala Leu Gln Ser 
1               5                   10                  15      


Ala Ile Thr Thr Phe Ser Gly Ala Arg Gln Asp Gly Ala Lys Thr Ser 
            20                  25                  30          


Gly Phe Thr Ser Ala Gln Val Thr Ala Leu Ile Asn Ser Ala Lys Ala 
        35                  40                  45              


Asp Lys Glu Gly Val Arg Thr Ser Ala Asn Gly Asp Asp Val Ser Pro 
    50                  55                  60                  


Val Glu Tyr Trp Val Asn Ser Ser Val Leu Gly Ala Phe Asn Ala Ala 
65                  70                  75                  80  


Ile Thr Ala Leu Glu Asn Ala Ser Gly Gln Ser Ala Ile Asp Ala Ala 
                85                  90                  95      


Tyr Leu Ala Leu Ile Gln Ala Gly Lys Thr Phe Asn Asp Ala Lys Arg 
            100                 105                 110         


His Gly Thr Thr Pro Asp Arg Thr Ala Leu Asn Asn Ala Ile Thr Ala 
        115                 120                 125             


Ala Val Asn Ala Lys Asn Gly Val Gln Thr Ala Ala Asp Lys Asp Gln 
    130                 135                 140                 


Ala Ser Leu Gly Ser Ser Trp Ala Thr Gly Ala Gln Phe Asn Ala Leu 
145                 150                 155                 160 


Asn Thr Ala Ile Asp Ser Ala Thr Ala Val Lys Asn Asn Ala Asn Ala 
                165                 170                 175     


Thr Lys Ala Ser Val Asp Thr Ala Ala Ala Ser Leu Asn Ala Ala Ile 
            180                 185                 190         


Ala Thr Phe Thr Thr Ala Val Thr Asn Asn Gly Pro Gly Thr Gln Thr 
        195                 200                 205             


Phe Arg Asp Ile Thr Ala Ala Gln Leu Val Ala Glu Ile Lys Ile Gly 
    210                 215                 220                 


Trp Asn Leu Gly Asn Ser Leu Asp Ala His Asn Gly Phe Pro Ala Asn 
225                 230                 235                 240 


Pro Thr Val Asp Gln Met Glu Arg Gly Trp Gly Asn Pro Ala Thr Thr 
                245                 250                 255     


Lys Ala Asn Ile Thr Ala Leu Lys Asn Ala Gly Phe Asn Ala Ile Arg 
            260                 265                 270         


Ile Pro Val Ser Trp Thr Lys Ala Ala Ser Gly Ala Pro Asn Tyr Thr 
        275                 280                 285             


Ile Arg Thr Asp Trp Met Thr Arg Val Lys Glu Ile Val Asn Tyr Ala 
    290                 295                 300                 


Val Asp Asn Asp Met Tyr Ile Ile Leu Asn Thr His His Asp Glu Asp 
305                 310                 315                 320 


Val Leu Thr Phe Met Asn Ser Asn Ala Ala Ala Gly Lys Ala Ala Phe 
                325                 330                 335     


Gln Lys Leu Trp Glu Gln Ile Ala Ala Ala Phe Lys Asp Tyr Asn Glu 
            340                 345                 350         


Lys Leu Ile Phe Glu Gly Leu Asn Glu Pro Arg Thr Pro Gly Ser Ser 
        355                 360                 365             


Asn Glu Trp Asn Gly Gly Thr Asp Glu Glu Arg Asn Asn Leu Asn Ser 
    370                 375                 380                 


Tyr Tyr Pro Ile Phe Val Asn Thr Val Arg Ser Ser Gly Gly Asn Asn 
385                 390                 395                 400 


Gly Lys Arg Ile Leu Met Ile Asn Pro Tyr Ala Ala Ser Met Glu Ala 
                405                 410                 415     


Val Ala Met Asn Ala Leu Thr Leu Pro Ala Asp Ser Ala Ala Asn Lys 
            420                 425                 430         


Leu Ile Val Ser Phe His Ser Tyr Gln Pro Tyr Asn Phe Ala Leu Asn 
        435                 440                 445             


Lys Asp Ser Ser Ile Asn Thr Trp Ser Ser Ser Ser Ser Gly Asp Thr 
    450                 455                 460                 


Ser Pro Ile Thr Gly Pro Ile Asp Arg Tyr Tyr Asn Lys Phe Val Ser 
465                 470                 475                 480 


Gln Gly Ile Pro Val Ile Ile Gly Glu Phe Gly Ala Met Asn Lys Asn 
                485                 490                 495     


Asn Glu Ala Val Arg Ala Gln Trp Ala Glu Tyr Tyr Val Ser Tyr Ala 
            500                 505                 510         


Gln Ser Lys Gly Ile Lys Cys Phe Trp Trp Asp Asn Gly Val Thr Ser 
        515                 520                 525             


Gly Ser Gly Glu Leu Phe Gly Leu Leu Asn Arg Thr Asn Asn Thr Phe 
    530                 535                 540                 


Thr Tyr Asn Ala Leu Leu Asn Gly Met Met Ser Gly Thr Gly Gly Thr 
545                 550                 555                 560 


Val Pro Thr Pro Pro Thr Pro Pro Ala Thr Pro Thr Pro Pro Thr Thr 
                565                 570                 575     


Ile Thr Gly Asn Leu Gly Thr Tyr Gln Phe Gly Thr Gln Glu Asp Gly 
            580                 585                 590         


Val Ser Pro Asn Tyr Thr Gln Ala Val Trp Glu Leu Ser Gly Thr Asn 
        595                 600                 605             


Leu Thr Thr Ala Lys Thr Thr Gly Ala Lys Leu Val Leu Val Phe Thr 
    610                 615                 620                 


Thr Ala Pro Asn Ala Ser Met His Phe Val Trp Gln Gly Pro Ala Asn 
625                 630                 635                 640 


Ser Leu Trp Trp Asn Glu Lys Glu Ile Leu Gly Asn Thr Gly Asn Pro 
                645                 650                 655     


Ser Ala Thr Gly Val Thr Trp Asn Ser Gly Thr Lys Thr Leu Thr Ile 
            660                 665                 670         


Pro Leu Thr Ala Asn Ser Val Lys Asp Tyr Ser Val Phe Thr Ala Gln 
        675                 680                 685             


Pro Ser Leu Arg Ile Ile Ile Ala Tyr Tyr Asn Gly Gly Asn Val Asn 
    690                 695                 700                 


Asp Leu Gly Ile Val Ser Ala Asn Leu Thr Gln 
705                 710                 715 


<210>  4
<211>  382
<212>  PRT
<213>  Artificial

<220>
<223>  Synthetic construct comprising EG

<400>  4

Met Lys Ser Leu Phe Ala Leu Ser Leu Phe Ala Gly Leu Ser Val Ala 
1               5                   10                  15      


Gln Asn Ala Ala Trp Ala Gln Cys Gly Gly Asn Gly Trp Thr Gly Ser 
            20                  25                  30          


Lys Thr Cys Val Ser Gly Tyr Lys Cys Thr Val Val Asn Glu Trp Tyr 
        35                  40                  45              


Ser Gln Cys Ile Pro Gly Thr Ala Glu Glu Pro Thr Thr Thr Leu Lys 
    50                  55                  60                  


Thr Thr Thr Gly Gly Gly Ser Thr Pro Thr Gly Thr Pro Gly Asn Gly 
65                  70                  75                  80  


Lys Phe Leu Trp Val Gly Thr Asn Glu Ala Gly Gly Glu Phe Gly Glu 
                85                  90                  95      


Gly Ser Leu Pro Gly Thr Trp Gly Lys His Phe Ile Phe Pro Asp Pro 
            100                 105                 110         


Ala Ala Val Asp Thr Leu Ile Ser Gln Gly Tyr Asn Ala Phe Arg Val 
        115                 120                 125             


Gln Leu Arg Met Glu Arg Thr Asn Pro Ser Ser Met Thr Gly Pro Phe 
    130                 135                 140                 


Asp Thr Ala Tyr Leu Lys Asn Leu Thr Thr Ile Val Asp His Ile Thr 
145                 150                 155                 160 


Gly Lys Gly Ala Asn Val Ile Leu Asp Pro His Asn Tyr Gly Arg Tyr 
                165                 170                 175     


Phe Asp Lys Ile Ile Thr Ser Thr Ser Asp Phe Gln Thr Trp Trp Lys 
            180                 185                 190         


Asn Phe Ala Thr Gln Phe Lys Ser Asn Ser Lys Val Ile Phe Asp Thr 
        195                 200                 205             


Asn Asn Glu Tyr Asn Thr Met Asp Gln Thr Leu Val Leu Asn Leu Asn 
    210                 215                 220                 


Gln Ala Ala Ile Asn Gly Ile Arg Ala Ala Gly Ala Thr Gln Thr Ile 
225                 230                 235                 240 


Phe Val Glu Gly Asn Gln Trp Ser Gly Ala Trp Ser Trp Pro Asp Val 
                245                 250                 255     


Asn Asp Asn Met Lys Ala Leu Thr Asp Pro Leu Asp Lys Ile Val Tyr 
            260                 265                 270         


Glu Met His Gln Tyr Leu Asp Ser Asp Ser Ser Gly Thr Ser Pro Asn 
        275                 280                 285             


Cys Val Ser Thr Thr Ile Gly Val Glu Arg Val Lys Ala Ala Thr Glu 
    290                 295                 300                 


Trp Leu Arg Lys Asn Lys Lys Ile Gly Met Ile Gly Glu Leu Ala Gly 
305                 310                 315                 320 


Gly Pro Asn Asp Thr Cys Lys Thr Ala Val Lys Asn Met Leu Asp Tyr 
                325                 330                 335     


Leu Lys Glu Asn Ser Asp Val Trp Lys Gly Val Thr Trp Trp Ala Ala 
            340                 345                 350         


Gly Pro Trp Trp Ala Asp Tyr Met Phe Ser Phe Glu Pro Pro Ser Gly 
        355                 360                 365             


Thr Gly Tyr Gln Tyr Tyr Asn Ser Leu Leu Lys Thr Tyr Ile 
    370                 375                 380         


<210>  5
<211>  6
<212>  PRT
<213>  Artificial

<220>
<223>  Endoplasmic reticulum targeting sequence

<400>  5

Ser Glu Lys Asp Glu Leu 
1               5       


