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G1094_PHOV8
ID   G1094_PHOV8             Reviewed;         516 AA.
AC   A6KWM1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Glycosyl hydrolase family 109 protein 4;
DE            EC=3.2.1.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=BVU_0105;
OS   Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS   NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Phocaeicola.
OX   NCBI_TaxID=435590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC   11154;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000139; ABR37835.1; -; Genomic_DNA.
DR   RefSeq; WP_005843044.1; NC_009614.1.
DR   AlphaFoldDB; A6KWM1; -.
DR   SMR; A6KWM1; -.
DR   STRING; 435590.BVU_0105; -.
DR   CAZy; GH109; Glycoside Hydrolase Family 109.
DR   EnsemblBacteria; ABR37835; ABR37835; BVU_0105.
DR   KEGG; bvu:BVU_0105; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_046965_0_0_10; -.
DR   OMA; HPLWKKY; -.
DR   OrthoDB; 1465613at2; -.
DR   BioCyc; BVUL435590:G1G59-111-MON; -.
DR   Proteomes; UP000002861; 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; Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           19..516
FT                   /note="Glycosyl hydrolase family 109 protein 4"
FT                   /id="PRO_0000348556"
FT   BINDING         76..77
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         98
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         146..149
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         166..167
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         259..262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         337
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   516 AA;  57404 MW;  21CE4700350390EE CRC64;
     MKKIKLLLVA GACVVLSACS PQAPTVHTTD KGTQWEWNEG TIVVKSPERP AGQKSVIGLT
     APKMEVVRVG FVGLGMRGPG AVSRFTHIPG TQIVALCDYD PKRAEACQNI LKKASMPKAA
     IYSGETGYEE LCKRDDIDLV YIAADWLHHF PIAKCALENG KHVAIEVPSA MNLQECWDLV
     NLSETTRKHC FILENCCYDW FEMNTLNMAQ NGVFGEVIRA QGAYIHNLSD FWDYYWKNGE
     NDKLGWRLEF NMRHRGDVYA THGLGPVAQV LDIHRGDRMK TLTAMDTKSV VGKGLVEAKT
     GSECTNFRNG DHTTTMIRTE NGKVIEIQHN VMTPQPYNRL YQLTGVKGFA NKYPTEGYAL
     GADQLSASGV QPKVDNLSSH GFLPQAEMDA LVEKYQHPIL KKYGEIAKEV GGHGGMDFIM
     DSRLVYCLQN GLPLDMDVYD LAEWCALAEL GEISMDNNCA AVEFPDFTRG EWNVVKGYKH
     AYASPEEEQA SMEKAKAFTA KLKERGAKEW ATEADK
 
 
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