G1091_BACFR
ID G1091_BACFR Reviewed; 464 AA.
AC P0C863; Q64XU4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Glycosyl hydrolase family 109 protein 1;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN OrderedLocusNames=BF0931;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
CC -!- FUNCTION: Glycosidase. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC Note=Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.
CC {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109
CC subfamily. {ECO:0000305}.
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DR EMBL; AP006841; BAD47682.1; -; Genomic_DNA.
DR RefSeq; WP_005785179.1; NZ_UYXF01000001.1.
DR RefSeq; YP_098216.1; NC_006347.1.
DR AlphaFoldDB; P0C863; -.
DR SMR; P0C863; -.
DR CAZy; GH109; Glycoside Hydrolase Family 109.
DR EnsemblBacteria; BAD47682; BAD47682; BF0931.
DR GeneID; 66330087; -.
DR KEGG; bfr:BF0931; -.
DR PATRIC; fig|295405.11.peg.934; -.
DR HOGENOM; CLU_046965_0_0_10; -.
DR OMA; MESGKHA; -.
DR Proteomes; UP000002197; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycosidase; Hydrolase; Lipoprotein; Membrane; NAD;
KW Palmitate; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 17..464
FT /note="Glycosyl hydrolase family 109 protein 1"
FT /id="PRO_0000348549"
FT BINDING 63..64
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 134..137
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 154..155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 240..243
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT LIPID 17
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 17
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 464 AA; 52117 MW; 9F0AEE5438727396 CRC64;
MFKHLNALFI GLALFACTSG AVAQTIKPIE TPVPVRPAGQ KDVVGLTTPK LDVVRVGFIG
LGMRGPGAVE RFTHIPGTQI VALCDLIPER VAGAQKILTK ANLPEAASYS GSEDAWKKLC
ERKDIDLVYI ATDWKHHAQM AIYAMEHGKH VAIEVPSAMT LDEIWALINT SEKTRKHCMQ
LENCVYDFFE LTTLNMAQQG VFGEVLHTEG AYIHNLEDFW PYYWNNWRMD YNQNHRGDVY
ATHGMGPACQ LLDIHRGDKM NYLVSMDTKA VNGPAYIKKT TGKEVKDFQN GDQTSTLIRT
EKGKTILIQH NVMTPRPYSR MYQVVGADGY ASKYPIEEYC MRPTQIASND VPNHEKLNAH
GSVPADVKKA LMDKYKHPIH KELEETAKKV GGHGGMDYIM DYRLVYCLRN GLPLDMDVYD
LAEWCCMADL TKLSIENSSA PVAIPDFTRG AWNKVKGYRH AFAK
