ID G5SN50_9BACT Unreviewed; 429 AA.
AC G5SN50;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Glycosyl hydrolase, family 43 {ECO:0000313|EMBL:EHH01335.1};
GN ORFNames=HMPREF9441_00778 {ECO:0000313|EMBL:EHH01335.1};
OS Paraprevotella clara YIT 11840.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Paraprevotella.
OX NCBI_TaxID=762968 {ECO:0000313|EMBL:EHH01335.1, ECO:0000313|Proteomes:UP000003598};
RN [1] {ECO:0000313|EMBL:EHH01335.1, ECO:0000313|Proteomes:UP000003598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11840 {ECO:0000313|EMBL:EHH01335.1,
RC ECO:0000313|Proteomes:UP000003598};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHH01335.1}.
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DR EMBL; AFFY01000014; EHH01335.1; -; Genomic_DNA.
DR RefSeq; WP_008618021.1; NZ_JH376590.1.
DR AlphaFoldDB; G5SN50; -.
DR STRING; 762968.HMPREF9441_00778; -.
DR GeneID; 78581982; -.
DR PATRIC; fig|762968.3.peg.696; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_11_2_10; -.
DR OrthoDB; 9763933at2; -.
DR Proteomes; UP000003598; Unassembled WGS sequence.
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 305..429
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT SITE 138
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 429 AA; 48471 MW; E716276BB7EA6EE7 CRC64;
MWLCGGATLR AQDPIIQTKY TADPAPMVYN DTVFLYTGHD EDDAYSFKMF DWQLYTSTDM
VNWTDHGTVA TTKTFPWREE QNGAWAMQVV ERNGKFYMYC TVQGNGIGVL VSDSPYGPFK
DPIGQPLVWQ KGIGDDIDPT VFIDDDGQAY MYWGNPNLYY VKLNEDMISY SGGIVKIGKL
KTYQEGPWFY KRNGHYYLAF ASTCCPEGIG YAMSGSPTGP WDVKGYIMRP TERTRGNHPG
IIDYKGKTYV FGQNNDLLFL DMKEHRERRS VSVAEMHYNP DGTIQEVPYF KDVKVEQIEH
FNPYRRVEAE TMAWGHGLKT ARLDDGGIYV TAVDDGDSLV VRGVDFGKRG AKRFRACIAS
EQGCAVEMHL DSAGGPLVGT LEVKATGGMQ TYKEMECRVK GAKGVHDLVF LFKGSVGKDL
MNWDYWCFN
//
