G1091_BACFN
ID G1091_BACFN Reviewed; 464 AA.
AC Q5LGZ0; Q64XU4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Glycosyl hydrolase family 109 protein 1;
DE EC=3.2.1.-;
DE Flags: Precursor;
GN OrderedLocusNames=BF0853;
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND LACK OF FUNCTION AS
RP ALPHA-N-ACETYLGALACTOSAMINIDASE.
RX PubMed=17401360; DOI=10.1038/nbt1298;
RA Liu Q.P., Sulzenbacher G., Yuan H., Bennett E.P., Pietz G., Saunders K.,
RA Spence J., Nudelman E., Levery S.B., White T., Neveu J.M., Lane W.S.,
RA Bourne Y., Olsson M.L., Henrissat B., Clausen H.;
RT "Bacterial glycosidases for the production of universal red blood cells.";
RL Nat. Biotechnol. 25:454-464(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
CC -!- FUNCTION: Glycosidase (By similarity). Has no alpha-N-
CC acetylgalactosaminidase activity. {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; AM039446; CAJ01378.1; -; Genomic_DNA.
DR EMBL; CR626927; CAH06596.1; -; Genomic_DNA.
DR RefSeq; WP_005785179.1; NC_003228.3.
DR AlphaFoldDB; Q5LGZ0; -.
DR SMR; Q5LGZ0; -.
DR STRING; 272559.BF9343_0815; -.
DR CAZy; GH109; Glycoside Hydrolase Family 109.
DR EnsemblBacteria; CAH06596; CAH06596; BF9343_0815.
DR GeneID; 66330087; -.
DR KEGG; bfs:BF9343_0815; -.
DR eggNOG; COG0673; Bacteria.
DR HOGENOM; CLU_046965_0_0_10; -.
DR OMA; MESGKHA; -.
DR OrthoDB; 1465613at2; -.
DR Proteomes; UP000006731; 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 1: Evidence at protein level;
KW Cell membrane; Glycosidase; Hydrolase; Lipoprotein; Membrane; NAD;
KW Palmitate; Reference proteome; 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_0000348546"
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
