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Database: UniProt
Entry: G8PV63_PSEUV
LinkDB: G8PV63_PSEUV
Original site: G8PV63_PSEUV 
ID   G8PV63_PSEUV            Unreviewed;       353 AA.
AC   G8PV63;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Oxidoreductase domain protein {ECO:0000313|EMBL:AEV39651.1};
GN   OrderedLocusNames=PSE_p0069 {ECO:0000313|EMBL:AEV39651.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OG   Plasmid FO-BEG1 {ECO:0000313|Proteomes:UP000005634}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Stappiaceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV39651.1, ECO:0000313|Proteomes:UP000005634};
RN   [1] {ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RC   PLASMID=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA   Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT   interacting bacteria.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV39651.1, ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV39651.1,
RC   ECO:0000313|Proteomes:UP000005634};
RC   PLASMID=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RX   PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA   Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT   for symbiosis.";
RL   Environ. Microbiol. 15:2095-2113(2013).
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DR   EMBL; CP003148; AEV39651.1; -; Genomic_DNA.
DR   RefSeq; WP_014290187.1; NC_016646.1.
DR   AlphaFoldDB; G8PV63; -.
DR   KEGG; psf:PSE_p0069; -.
DR   eggNOG; COG0673; Bacteria.
DR   HOGENOM; CLU_023194_1_0_5; -.
DR   Proteomes; UP000005634; Plasmid FO-BEG1.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR004104; Gfo/Idh/MocA-like_OxRdtase_C.
DR   InterPro; IPR000683; Gfo/Idh/MocA-like_OxRdtase_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43708; CONSERVED EXPRESSED OXIDOREDUCTASE (EUROFUNG); 1.
DR   PANTHER; PTHR43708:SF4; OXIDOREDUCTASE YCEM-RELATED; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   Pfam; PF02894; GFO_IDH_MocA_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   4: Predicted;
KW   Plasmid {ECO:0000313|EMBL:AEV39651.1}.
FT   DOMAIN          5..121
FT                   /note="Gfo/Idh/MocA-like oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01408"
FT   DOMAIN          135..341
FT                   /note="Gfo/Idh/MocA-like oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02894"
SQ   SEQUENCE   353 AA;  38143 MW;  F8B50EE50EADA41A CRC64;
     MPSISLAVVG LGMAAKPHLE ALDLLRNHVE VAGLYNRTKA KAEAVAEKYG WTCFDSPEEI
     AGDPEIDAVL LLTPPDQRHD LVELFSNAGK HILTEKPLER TYEAAAELVE LCDYAGIKYG
     VVFQHRFREG AKQLRALLSE GALGDIHLVR ANIPWWRDQA YYDQAGRGTY ERDGGGVLIT
     QAIHVLDLML SLTGPAKSVQ ALCATTGAHK MEAEDFATAG VEFHSGAVGS IMATTATYPD
     AKETLVFDGS KASAHLEGSK LTVTYRDGSI DVFGGRNGSK DGTGGGANPM AFPCDWHRDL
     IDDFALSIIE HRDPKVTGHD ALMVHALIEA IETSSRTGTR ADVREAEPSK AYI
//
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