ID D5BHY7_ZUNPS Unreviewed; 445 AA.
AC D5BHY7;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:ADF51375.1};
GN OrderedLocusNames=ZPR_1030 {ECO:0000313|EMBL:ADF51375.1};
OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS profunda).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zunongwangia.
OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF51375.1, ECO:0000313|Proteomes:UP000001654};
RN [1] {ECO:0000313|EMBL:ADF51375.1, ECO:0000313|Proteomes:UP000001654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC {ECO:0000313|Proteomes:UP000001654};
RX PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA Zhou B.C., Yu J., Zhang Y.Z.;
RT "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT to the deep-sea environment and ecological role in sedimentary organic
RT nitrogen degradation.";
RL BMC Genomics 11:247-247(2010).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP001650; ADF51375.1; -; Genomic_DNA.
DR AlphaFoldDB; D5BHY7; -.
DR STRING; 655815.ZPR_1030; -.
DR CAZy; CBM6; Carbohydrate-Binding Module Family 6.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR KEGG; zpr:ZPR_1030; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_11_2_10; -.
DR OrthoDB; 9763933at2; -.
DR Proteomes; UP000001654; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd18618; GH43_Xsa43E-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF6; -; 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51175; CBM6; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT DOMAIN 318..444
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT ACT_SITE 44
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 140
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 445 AA; 50000 MW; 51FD788F22D39BC3 CRC64;
MLCSVLGTSF LNAQNPIIQT SYTADPAPMV HDDKLYLYTS HDEDNSTWFT MDDWRLYTTE
DMVNWTDHGA VLEYTDFDWS LKNAWAPAAI QRDGKFYIYV PITDRSNQNG IGVAVSDSPY
GPFIDPLGKP LVSESNADID PAVFIDDDGQ AYMFWGNPEC YFVKLNEDMI STKGDIQKIP
NTIEAFGKRK GEKNERRPTT YEEGPWVYKR NDIYYLFFAA GPIPEHIGYS TSKSVTGPWK
YQGELMPNQG GSFTNHPGIV DYKGKTYFFY HNAGLPGGSG FTRSVCVQEL KFNSDGTIEQ
MNMTSGIKEA LKKLNPYRKT EAETIAWSEG FKAQSNDVVG NFVTAMKDGA YIKVKAVDFG
KTSPKSVTAR IGSIHNNNVS MEIHIDSKDG KLLATLDVPL TGGNDRWKLV TADVEELTGV
HDLFFVVKGK APTQLMYFDY WMFSK
//
