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Database: UniProt
Entry: A0A125MHC2_9BACE
LinkDB: A0A125MHC2_9BACE
Original site: A0A125MHC2_9BACE 
ID   A0A125MHC2_9BACE        Unreviewed;       770 AA.
AC   A0A125MHC2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Family 65 glycosyl hydrolase {ECO:0000313|EMBL:KAA5418439.1};
GN   ORFNames=F2Y81_11550 {ECO:0000313|EMBL:KAA5418439.1};
OS   Bacteroides cellulosilyticus.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=246787 {ECO:0000313|EMBL:KAA5418439.1, ECO:0000313|Proteomes:UP000448877};
RN   [1] {ECO:0000313|EMBL:KAA5418439.1, ECO:0000313|Proteomes:UP000448877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BIOML-A6 {ECO:0000313|EMBL:KAA5418439.1,
RC   ECO:0000313|Proteomes:UP000448877};
RX   PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA   Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA   Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA   Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA   Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA   Xavier R.J., Alm E.J.;
RT   "A library of human gut bacterial isolates paired with longitudinal
RT   multiomics data enables mechanistic microbiome research.";
RL   Nat. Med. 25:1442-1452(2019).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC       {ECO:0000256|ARBA:ARBA00006768}.
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:KAA5418439.1}.
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DR   EMBL; VVYV01000017; KAA5418439.1; -; Genomic_DNA.
DR   RefSeq; WP_007217409.1; NZ_VVYV01000017.1.
DR   AlphaFoldDB; A0A125MHC2; -.
DR   STRING; 246787.BcellWH2_01302; -.
DR   eggNOG; COG1554; Bacteria.
DR   Proteomes; UP000448877; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR   Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR005194; Glyco_hydro_65_C.
DR   InterPro; IPR005195; Glyco_hydro_65_M.
DR   InterPro; IPR005196; Glyco_hydro_65_N.
DR   InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR   InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR   PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR   PANTHER; PTHR11051:SF14; MALTOSE PHOSPHORYLASE; 1.
DR   Pfam; PF03633; Glyco_hydro_65C; 1.
DR   Pfam; PF03632; Glyco_hydro_65m; 1.
DR   Pfam; PF03636; Glyco_hydro_65N; 1.
DR   PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KAA5418439.1}.
FT   DOMAIN          14..265
FT                   /note="Glycoside hydrolase family 65 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03636"
FT   DOMAIN          322..688
FT                   /note="Glycoside hydrolase family 65 central catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03632"
FT   DOMAIN          698..758
FT                   /note="Glycoside hydrolase family 65 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03633"
FT   ACT_SITE        488
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
SQ   SEQUENCE   770 AA;  89611 MW;  C30C00CC3D27903C CRC64;
     MKRYLKTDEW NIIEDNFHAD NLRMSESIFS LGNGRFGQRG NFEEPYSSDS YRGSFVAGIT
     FLDKTRVGWW KNGFPHFYTR IPNAADWSRV SLRLIDEELD LAQWDVNSFS RRLDMKAGIS
     YRDFEITSPK GHQIRVHVEH INNMAHPDLC LIKYSVTSIN YTGRISLIPS LDAIIVNKDD
     DPNEKIWNIL RSGVTKDCAY LWTQTRREDA QVCYAMTYQF FKNGKEATSN PIRIEKEKQT
     GFSIGADVKP GDNVMLIKYT VISSSLYDER QELIEHSIAK ARQTKIDGWD KLGNDHQQAW
     TNIWKEMDVV IEGDPEAQQG IRYNIFQLCQ TYRGDDPRLN IGPKGFTGEK YGGNTYWNTE
     LCCVPFFLLS TPREIVKNLL IYRYNQLPKA IENARKLGFK EGAALFPQVT YSGEECHSEW
     EITFEEIHRN NIIVYAIAQH AAITGSKDYV AKYGLEVMIA VSRFWSQRVS FSKPKQKYVI
     LGVTGPDEYE NNVDNNWYTN YSCVQCLRMT LNYLEIIAGE YPDEYARVRR VTNLRQQEEA
     ERWRDIINHM YLPEDKELGI FVQNDGFLDK ELNSTDAIPP EERPINQHWS WDRILRSCYI
     KQSDVLLGLY LYYFNFDKET VRRNFDFYET MTVHESSLSP HIHSILAARI GEVEKAYQLF
     LHATRLDLDD YNNETHQGLH ITSMPGSWLA IVRGFAGMQI LEGILSFFPV IPEKWNSYSF
     QINYQGRTLH MHVGKEINIS LIAGEELNIQ VYKNVYKLKL GTDLLLRIEE
//
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