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GUNA_NOVHA
ID   GUNA_NOVHA              Reviewed;         342 AA.
AC   P37696;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Probable endoglucanase;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   Flags: Precursor;
GN   Name=cmcAX;
OS   Novacetimonas hansenii (Komagataeibacter hansenii).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Novacetimonas.
OX   NCBI_TaxID=436;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 21-34.
RC   STRAIN=ATCC 23769 / NCIMB 8246;
RX   PubMed=8300521; DOI=10.1128/jb.176.3.665-672.1994;
RA   Standal R., Iversen T.-G., Coucheron D.H., Fjaervik E., Blatny J.M.,
RA   Valla S.;
RT   "A new gene required for cellulose production and a gene encoding
RT   cellulolytic activity in Acetobacter xylinum are colocalized with the bcs
RT   operon.";
RL   J. Bacteriol. 176:665-672(1994).
CC   -!- FUNCTION: Enzyme capable of hydrolyzing carboxy-methyl-cellulose (CMC).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 8 (cellulase D) family.
CC       {ECO:0000305}.
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DR   EMBL; M96060; AAA16969.1; -; Unassigned_DNA.
DR   PIR; A36963; A36963.
DR   PDB; 1WZZ; X-ray; 1.65 A; A=21-342.
DR   PDBsum; 1WZZ; -.
DR   AlphaFoldDB; P37696; -.
DR   SMR; P37696; -.
DR   CAZy; GH8; Glycoside Hydrolase Family 8.
DR   EvolutionaryTrace; P37696; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR002037; Glyco_hydro_8.
DR   InterPro; IPR019834; Glyco_hydro_8_CS.
DR   Pfam; PF01270; Glyco_hydro_8; 1.
DR   PRINTS; PR00735; GLHYDRLASE8.
DR   SUPFAM; SSF48208; SSF48208; 1.
DR   PROSITE; PS00812; GLYCOSYL_HYDROL_F8; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW   Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:8300521"
FT   CHAIN           21..342
FT                   /note="Probable endoglucanase"
FT                   /id="PRO_0000007930"
FT   ACT_SITE        57
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        114
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10058"
FT   HELIX           26..38
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   STRAND          48..51
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   HELIX           56..69
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   HELIX           72..85
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   STRAND          89..92
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   STRAND          96..99
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   STRAND          102..106
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   HELIX           113..130
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   HELIX           133..150
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   STRAND          151..154
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   STRAND          157..160
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   STRAND          170..175
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   HELIX           177..179
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   HELIX           182..192
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   HELIX           196..210
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   TURN            214..217
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   STRAND          221..226
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   TURN            227..229
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   STRAND          232..234
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   STRAND          240..242
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   TURN            244..247
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   HELIX           248..255
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   HELIX           261..274
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   TURN            285..287
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   STRAND          292..294
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   HELIX           297..305
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   HELIX           317..319
FT                   /evidence="ECO:0007829|PDB:1WZZ"
FT   HELIX           323..339
FT                   /evidence="ECO:0007829|PDB:1WZZ"
SQ   SEQUENCE   342 AA;  37443 MW;  85FF9BDF8B979F81 CRC64;
     MSVMAAMGGA QVLSSTGAFA DPAPDAVAQQ WAIFRAKYLR PSGRVVDTGN GGESHSEGQG
     YGMLFAASAG DLASFQSMWM WARTNLQHTN DKLFSWRFLK GHQPPVPDKN NATDGDLLIA
     LALGRAGKRF QRPDYIQDAM AIYGDVLNLM TMKAGPYVVL MPGAVGFTKK DSVILNLSYY
     VMPSLLQAFD LTADPRWRQV MEDGIRLVSA GRFGQWRLPP DWLAVNRATG ALSIASGWPP
     RFSYDAIRVP LYFYWAHMLA PNVLADFTRF WNNFGANALP GWVDLTTGAR SPYNAPPGYL
     AVAECTGLDS AGELPTLDHA PDYYSAALTL LVYIARAEET IK
 
 
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