ID D4ZGP8_SHEVD Unreviewed; 736 AA.
AC D4ZGP8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Glucanase {ECO:0000256|RuleBase:RU361186};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361186};
GN OrderedLocusNames=SVI_0876 {ECO:0000313|EMBL:BAJ00847.1};
OS Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ00847.1, ECO:0000313|Proteomes:UP000002350};
RN [1] {ECO:0000313|Proteomes:UP000002350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12
RC {ECO:0000313|Proteomes:UP000002350};
RX PubMed=20458400; DOI=10.1039/c000396d;
RA Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H.,
RA Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T.,
RA Nakasone K., Mori H.;
RT "Complete genome sequence and comparative analysis of Shewanella violacea,
RT a psychrophilic and piezophilic bacterium from deep sea floor sediments.";
RL Mol. Biosyst. 6:1216-1226(2010).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase family 6.
CC {ECO:0000256|RuleBase:RU361186}.
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DR EMBL; AP011177; BAJ00847.1; -; Genomic_DNA.
DR RefSeq; WP_013050158.1; NC_014012.1.
DR AlphaFoldDB; D4ZGP8; -.
DR STRING; 637905.SVI_0876; -.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
DR KEGG; svo:SVI_0876; -.
DR eggNOG; COG3291; Bacteria.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_015488_3_1_6; -.
DR OrthoDB; 9793816at2; -.
DR Proteomes; UP000002350; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00146; PKD; 2.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.40; 1, 4-beta cellobiohydrolase; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR34876; -; 1.
DR PANTHER; PTHR34876:SF4; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE C-RELATED; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR Pfam; PF18911; PKD_4; 2.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00637; CBD_II; 1.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 1.
DR SUPFAM; SSF49299; PKD domain; 2.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
DR PROSITE; PS50093; PKD; 2.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU361186};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001,
KW ECO:0000256|RuleBase:RU361186};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361186};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361186};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW ECO:0000256|RuleBase:RU361186};
KW Reference proteome {ECO:0000313|Proteomes:UP000002350};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361186}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT CHAIN 24..736
FT /note="Glucanase"
FT /evidence="ECO:0000256|RuleBase:RU361186"
FT /id="PRO_5005126545"
FT DOMAIN 18..127
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT DOMAIN 133..196
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 214..295
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 669..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 399
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10056"
FT ACT_SITE 448
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10057"
SQ SEQUENCE 736 AA; 79402 MW; A1DE8E59F00DF439 CRC64;
MRSGLIKGVT LTSMLLATLQ ANAAVKCDYS IENEWETGFV GAIQLKNTGE TLIDGWQVSW
QYLDGSTVSS AWNSTFSGNS PYLASNLVWN NLIQPGETIT FGIQGEKGIP NKAASTPKIS
GEICTREANN SAPMTSFTII ESGLDISFDA SATRDADGDE LTYSWDFGDE TLGEGVNTEH
SFSSLGSYIV TLTVSDGLVI DEHSIELNIK SLVPNQAPLA SFNTIHDGLA LSFNASNSSD
PEGDALSYLW SFGDGTSQSG INTYHQYAAH GLYTVTLNVS DGSSNTQIRT ELLVTYDGAT
GQHVANPFLG TTSYINPDYA KFVDASMALE SAPHLQAKMA QVKQQATAVW LDRIDAIYGG
EINSGRLSLE QHFDNALAQK RVGVPITVSI VVYNLPDRDC AALASNGTLN AAEGGLEIYK
HDYIDTIANI AAAPRFEDLR IIAVIEPDSL PNLVTNTRVL KCGIVNSNGT YVEGVQYALS
RFSRLDNVYS YLDIAHSGWL GWDTNMRGAI DLYTSVVAGV ADGDMSVLDG FISNVANYTP
AEEIFLPDPE FDFDGDFMGI KSSSYYEWNP VFDEKDFAQS LHAEFVAKGF PTSLAMLIDT
SRNGWGASDR PTSPNEDASN EDQYVMDSKL DRRAHRGNWC NSSGAGIGAR PETLPFGSTS
VIQAYVWIKP PGESDGTSDA SQTTPDEEGK SFDPMCSPEF TTSGGVLTGA MNGAPSAGAW
FHEQFKMLVE NAHPEL
//
