ID D0Z295_PHODD Unreviewed; 673 AA.
AC D0Z295;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=2-enoate reductase (Two distinct NAD(FAD)-dependent dehydrogenase domains) {ECO:0000313|EMBL:EEZ39526.1};
GN ORFNames=VDA_000546 {ECO:0000313|EMBL:EEZ39526.1};
OS Photobacterium damselae subsp. damselae CIP 102761.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ39526.1, ECO:0000313|Proteomes:UP000003579};
RN [1] {ECO:0000313|EMBL:EEZ39526.1, ECO:0000313|Proteomes:UP000003579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ39526.1,
RC ECO:0000313|Proteomes:UP000003579};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA Bartels D.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; ADBS01000002; EEZ39526.1; -; Genomic_DNA.
DR RefSeq; WP_005304684.1; NZ_ADBS01000002.1.
DR AlphaFoldDB; D0Z295; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR Proteomes; UP000003579; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000003579}.
FT DOMAIN 8..359
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 406..658
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 673 AA; 73994 MW; 293C0E35E9BC87E8 CRC64;
MKQEHQILFT PLKIGTLTLK NRYSMAPMGT LGCVDSDGAY NARGVEYYVA RAKGGVGLII
TGVQMVENEL EQFPMPSLPC PSYNPTAYIR SARELTERVH SYGCKIFAQL TAGWGRSCIP
GFTPNDKCVA PSKAANRFDP TLEHRELATQ EVKHFIAKFA ESAAIAQKAG YDGVEIHAVH
EGYLLDQFSL SFFNQRTDEY GGSFENRYRF AVEIVKAIKS VCGERFPVSL RYSVKSNMKG
YGQGILPEED AVEVGRDLEE GLRAAKYLQD AGYDALNVDA GTYDSWYWNH PANYFKPGMY
QPYCKAVSEV VDIPVLMAGR MEDPDLAAKA VQEGVADGIS MGRPLLADPD VVNKIRSGKF
EQVRPCLSCH QGCLGRMAEV GNISCAVNPA CGREEEYKLT PCLIKKKVMI IGGGVAGMEA
ARVSALRGHE VHLFEATSYL GGNVIPGSQP PFKHDDKLLI RWFEGELQRQ GVYVHLNTKV
TQDIIQECNA DAVIFATGSK PEVPAWLSGA DQSHVSVAED ILMNPELITG QSVCVIGGGL
VGSELALWLA QKNKDVTLIE ADNDIIGGPH GTCFANYQML KELLVKHKVD VKLSTKLRTI
TETGIEIEDQ DSNISSIDYP HVVLALGYKA ESSMYDQLAN QLEVDEIYNI GDSQQARTIM
AAIWEGYEVA RQI
//
