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).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//