ID Q184Q9_CLOD6 Unreviewed; 692 AA.
AC Q184Q9;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:CAJ69963.1};
DE EC=3.2.1.- {ECO:0000313|EMBL:CAJ69963.1};
GN OrderedLocusNames=CD630_30710 {ECO:0000313|EMBL:CAJ69963.1};
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563 {ECO:0000313|EMBL:CAJ69963.1, ECO:0000313|Proteomes:UP000001978};
RN [1] {ECO:0000313|EMBL:CAJ69963.1, ECO:0000313|Proteomes:UP000001978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630 {ECO:0000313|EMBL:CAJ69963.1,
RC ECO:0000313|Proteomes:UP000001978};
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch R., Sharp S., Simmonds M., Steven K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B.and.Parkhill.J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR EMBL; AM180355; CAJ69963.1; -; Genomic_DNA.
DR RefSeq; WP_003439934.1; NZ_JAUPES010000008.1.
DR RefSeq; YP_001089585.1; NC_009089.1.
DR AlphaFoldDB; Q184Q9; -.
DR STRING; 272563.CD630_30710; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR EnsemblBacteria; CAJ69963; CAJ69963; CD630_30710.
DR GeneID; 66355468; -.
DR KEGG; cdf:CD630_30710; -.
DR KEGG; pdc:CDIF630_03354; -.
DR PATRIC; fig|272563.120.peg.3237; -.
DR eggNOG; COG1501; Bacteria.
DR OrthoDB; 176168at2; -.
DR PhylomeDB; Q184Q9; -.
DR BioCyc; PDIF272563:G12WB-3232-MONOMER; -.
DR Proteomes; UP000001978; 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:InterPro.
DR CDD; cd14752; GH31_N; 1.
DR CDD; cd06591; GH31_xylosidase_XylS; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43863; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 1.
DR PANTHER; PTHR43863:SF2; MALTASE-GLUCOAMYLASE, INTESTINAL-LIKE; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:CAJ69963.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:CAJ69963.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001978}.
FT DOMAIN 18..200
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 246..580
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 591..676
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
SQ SEQUENCE 692 AA; 80416 MW; 32B352F1B37F5544 CRC64;
MIKISEDYIE KRFDNELLRI EAWGKNSLRI RSFVDQNFVD ENYALNEKPK LNKDDITINK
NEDGSAIIKN GKIKAVLDHR DRITFYNDKN EILLKEYIRL RAVKHDDGGE DVGTIEITKD
FNSTLKLKSR EYRPSYSGEF EVTTRFESEP SEKIFGMGQY QHKFLDLKNT VLELAQRNSQ
ISVPFYISSL GYGLLWNNPG IGKVSFAKNM TEWKMFSTNF IDYWITCGES PKELNKNYSQ
VTGTVPMMPE NLLGLWQSKL RYRTSEEVLD VVKEYSKRGI KLSSIAIDYF HWPKQGEYKF
DLDYWKNPKE LVKKLKEEYS VEPIVSVWPT VQSDAENYND YLENGYLVNV NRGVRMTMQI
QGNTVFVDMT NENAREYVWD RIDKNYKQLG IDYYWLDVAE PGYSVYDFDN YRYKKGNVLS
CGNIYPIDYL KMIYDGLHND IESVVTLVRG AWAGAQKYGA LVWSGDIDSS FEAFNNQVNT
GLNMGLAGIP WWTTDIGGFH GGNPKDPEFR ELMVRWFQYA TFSPILRMHG DRLPHSKPLS
NKGGGSMVTG APNEIWSYGE EVEVILTKFI KIRESLKTYL KKLMKEAHED GTPVMRTLFY
EFPEDDKTWE VDNTYMLGDE ILVAPIMNYK DRSRKVYLPK GHTWENIFSG VSYEGGKTYE
VECPLEEIPI FLKQDSSYNF KELKNILGEV KS
//
