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Unreviewed, UniProtKB/TrEMBL Q59316 (Q59316_CLOSR)

Last modified April 14, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · Ontologies · Sequences · References · Cross-references · Entry information

Names and origin

Protein namesSubmitted name:
    Cellobiose-phosphorylase EMBL AAC45510.1
    EC=2.4.1.20
Gene names
Name: cepA EMBL AAC45510.1
OrganismClostridium stercorarium EMBL AAC45510.1
Taxonomic identifier1510 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length811 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existencePredicted.

Sequences

Sequence LengthMass (Da)Tools
Q59316-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2DE204AA2817972E

FASTA81192,714
        10         20         30         40         50         60 
MKFGYFDDVN REYVITTPAT PYPWINYLGC QDFFSLISNT SGGYCFYRDA RLRRITRYRY 

        70         80         90        100        110        120 
NNVPIDSGGR YFYIYDSGDY WTPGWMPVKR ELDRYECRHG LGYTRITGER NGVEVSQLAF 

       130        140        150        160        170        180 
VPLNYNGEVN QVVITNKSGS EKEIALFSFV EFCLWNAMDD MTNFQRNFST GEVEVEGSAI 

       190        200        210        220        230        240 
YHKTEYRERR NHYAFFWVNS PIDGFDTDRE SFLGLYNGFD SPKNVAAGKP TNSIASGWSP 

       250        260        270        280        290        300 
IASHYIKMSL KPGEKRSYIF VLGYVENPPE EKWERKGVIN KKRAREMQQK FIDDTCVEKA 

       310        320        330        340        350        360 
FQELKDYWAD LCSKFALESH DEKLNRMVNI WNPYQCMVTF NMSRSASYFE SGISRGMGFR 

       370        380        390        400        410        420 
DSAQDLLGFV HQVPERARQR ILDLASTQFE DGSAYHQYQP LTKKGNSDIG SGFNDDPLWL 

       430        440        450        460        470        480 
ILATAQYIKE TGDFGILDEM VPFDCDENKK DTLFEHLKRS FYHVVNNLGP HGLPLIGRAD 

       490        500        510        520        530        540 
WNDCLNLNCF STQPMNPFTP ADKFEGRVAE SVFIAGMFVL IGPEYVELCK RRGLSEEAAE 

       550        560        570        580        590        600 
AEKHIQNMVN AVLTHGYDGE WFLRAYDHFG NKIGSKECSE GQIFIEPQGI CVMAGIGVKE 

       610        620        630        640        650        660 
GLAQKALDSV MKRLDTKYGI VLHTPAYTEY YLNLGEISSY PPGYKENAGI FCHNNPWIAI 

       670        680        690        700        710        720 
AETVIGRGDR AFEVYSKIAP AYIEDISDIH RTEPYVYSQM IAGRTRWSFG EAKNSWLTGT 

       730        740        750        760        770        780 
AAWNFVAITQ YILGVRPVYD GLMVDPCIPA SWDGFTVTRE FRGSKYRIRV ENPEHICKGV 

       790        800        810 
NKVIMDGKEI EGQVLPVSPK ESEHEVIVIM G 

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References

[1]"Purification and properties of a cellobiose phosphorylase (CepA) and a cellodextrin phosphorylase (CepB) from the cellulolytic thermophile Clostridium stercorarium."
Reichenbecher M., Lottspeich F., Bronnenmeier K.
Eur. J. Biochem. 247:262-267(1997) [PubMed: 9249035] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: NCIB 11754 EMBL AAC45510.1.

Cross-references

Sequence databases

U56424 Genomic DNA. Translation: AAC45510.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyGH94. Glycoside Hydrolase Family 94.

Enzyme and pathway databases

BRENDA2.4.1.20. 16695.

Family and domain databases

InterProIPR009342. Carb_bd_put.
IPR010383. Glyco_transf_36.
IPR010403. GT36_AF.
[Graphical view]
PfamPF06204. CBM_X. 1 hit.
PF06165. Glyco_transf_36. 1 hit.
PF06205. GT36_AF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ59316_CLOSR
AccessionPrimary (citable) accession number: Q59316
Entry history
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: April 14, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
Names and origin · Protein attributes · Ontologies · Sequences · References · Cross-references · Entry information