ID D3IBG2_9BACT Unreviewed; 515 AA.
AC D3IBG2;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFC71061.2};
GN ORFNames=HMPREF0669_00766 {ECO:0000313|EMBL:EFC71061.2};
OS Prevotella sp. oral taxon 299 str. F0039.
OG Plasmid unnamed {ECO:0000313|EMBL:EFC71061.2}.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=575614 {ECO:0000313|EMBL:EFC71061.2, ECO:0000313|Proteomes:UP000015929};
RN [1] {ECO:0000313|EMBL:EFC71061.2, ECO:0000313|Proteomes:UP000015929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0039 {ECO:0000313|EMBL:EFC71061.2,
RC ECO:0000313|Proteomes:UP000015929};
RC PLASMID=unnamed {ECO:0000313|EMBL:EFC71061.2};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFC71061.2, ECO:0000313|Proteomes:UP000015929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0039 {ECO:0000313|EMBL:EFC71061.2,
RC ECO:0000313|Proteomes:UP000015929};
RC PLASMID=Plasmid {ECO:0000313|Proteomes:UP000015929};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA Blanton J.M., Tanner A.C., Dewhirst F.E., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella sp. Oral Taxon 299 strain F0039.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
CC -!- SIMILARITY: Belongs to the Gfo/Idh/MocA family. Glycosyl hydrolase 109
CC subfamily. {ECO:0000256|ARBA:ARBA00009329}.
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DR EMBL; CP003667; EFC71061.2; -; Genomic_DNA.
DR RefSeq; WP_020967342.1; NC_022111.1.
DR AlphaFoldDB; D3IBG2; -.
DR KEGG; pro:HMPREF0669_00766; -.
DR HOGENOM; CLU_046965_0_0_10; -.
DR OrthoDB; 9771072at2; -.
DR Proteomes; UP000015929; Plasmid.
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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR InterPro; IPR049303; Glyco_hydro_109_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43818; BCDNA.GH03377; 1.
DR PANTHER; PTHR43818:SF1; GLYCOSYL HYDROLASE FAMILY 109 PROTEIN; 1.
DR Pfam; PF01408; GFO_IDH_MocA; 1.
DR Pfam; PF21252; Glyco_hydro_109_C; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Plasmid {ECO:0000313|EMBL:EFC71061.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000015929};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..515
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003046496"
FT DOMAIN 62..183
FT /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01408"
FT DOMAIN 200..349
FT /note="Glycosyl hydrolase 109 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21252"
SQ SEQUENCE 515 AA; 58166 MW; 2D630AFA4E6BAA83 CRC64;
MTKNKVLLAL LAVVFLALPQ SLCAQFNWKY TVEKGKIVTE VPLRAPGQTT ALQLTTPKMP
VVRVGFVGLG MRGPSAVERW MHIPGIEVVA LCDYEAKRAE ACQKILRDNS MPAAAIYSGE
EGYKELCKRK DIDLVYIATD WDHHFLVAKC AMENGKHAAI EVPSAINLRE IWTLIDLSEK
TRLHCVMLEN CCYDFFELNS LNMAQKGVFG DVIYAQGAYK HELSSFWKYY WKKNAQDKLG
WRLEYNKDYR GDLYATHGLG PIAQVLNIHR GDRMRTLVAM DTKSFNGKKL VEKYTGEPCE
KFENGDQTMT LIRTEQGKVI EIHHNVMTPQ PYNRMYQLTG TEGFANKYPV EGFAVSAKKM
EAGGVKPSAD NLSGHSYLSE KDKKALEEKY LSPIIKRYGE EAKEVGGHGG MDFIMDSRLV
YCLQNGLPMD IDVYDLAEWC CLGELGAISM NNDFMPVEVP DFTRGDWNKV KGFTHAYASP
ADEAATLAQA KAFTAKLKEK GKRYWDAFDK KNKKK
//
