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Database: UniProt
Entry: G8PHV2_PSEUV
LinkDB: G8PHV2_PSEUV
Original site: G8PHV2_PSEUV 
ID   G8PHV2_PSEUV            Unreviewed;       328 AA.
AC   G8PHV2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Oxidoreductase, zinc-binding dehydrogenase family protein {ECO:0000313|EMBL:AEV36545.1};
GN   OrderedLocusNames=PSE_2035 {ECO:0000313|EMBL:AEV36545.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Stappiaceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV36545.1, 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};
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:AEV36545.1, ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV36545.1,
RC   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; CP003147; AEV36545.1; -; Genomic_DNA.
DR   RefSeq; WP_014284712.1; NC_016642.1.
DR   AlphaFoldDB; G8PHV2; -.
DR   STRING; 911045.PSE_2035; -.
DR   KEGG; psf:PSE_2035; -.
DR   eggNOG; COG0604; Bacteria.
DR   HOGENOM; CLU_026673_3_1_5; -.
DR   Proteomes; UP000005634; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd08241; QOR1; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR43677:SF3; PROSTAGLANDIN REDUCTASE 3; 1.
DR   PANTHER; PTHR43677; SHORT-CHAIN DEHYDROGENASE/REDUCTASE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
FT   DOMAIN          10..323
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   328 AA;  35030 MW;  2DAAC8E771D5FBEC CRC64;
     MRAVVCSEYG PPEALRVEDV ERKEPKKGQV RIVVEAAGVN FPDTLVIAGK YQIKPPMPFV
     PGGEVAGRIE VVGEGVTDFA PGDPVMALLL QQGGYAEEVV VDASAVMKRP ETMSAQVAAG
     FTMTYGTSMH ALKQRAQLQP GETLLVLGAG GGVGLTAVEI GKIMGAKVIA AASSAEKLEA
     ARKAGADELI NYSTQDLRER LKEIVGKAGV DVVYDPVGGD LFEQALRSTA WNGRALVVGF
     AAGDIPSIPT NLPLLKGCSV MGVFWGAFRM REPSNDQNNF SELFKWLQEG KLKPTVSKSY
     SLEEAPQALR DLMERRVVGK VVLETGRT
//
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