ID E0SB57_DICD3 Unreviewed; 387 AA.
AC E0SB57;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Nitric oxide reductase FlRd-NAD(+) reductase {ECO:0000313|EMBL:ADM97155.1};
DE EC=1.18.1.- {ECO:0000313|EMBL:ADM97155.1};
GN Name=ygbD {ECO:0000313|EMBL:ADM97155.1};
GN OrderedLocusNames=Dda3937_01435 {ECO:0000313|EMBL:ADM97155.1};
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628 {ECO:0000313|EMBL:ADM97155.1, ECO:0000313|Proteomes:UP000006859};
RN [1] {ECO:0000313|EMBL:ADM97155.1, ECO:0000313|Proteomes:UP000006859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937 {ECO:0000313|EMBL:ADM97155.1,
RC ECO:0000313|Proteomes:UP000006859};
RX PubMed=21217001; DOI=10.1128/JB.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006442}.
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DR EMBL; CP002038; ADM97155.1; -; Genomic_DNA.
DR RefSeq; WP_013316628.1; NC_014500.1.
DR AlphaFoldDB; E0SB57; -.
DR STRING; 198628.Dda3937_01435; -.
DR GeneID; 9732357; -.
DR KEGG; ddd:Dda3937_01435; -.
DR PATRIC; fig|198628.6.peg.955; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_4_4_6; -.
DR OrthoDB; 9808980at2; -.
DR Proteomes; UP000006859; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.390.120; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR041364; Rbx-bd.
DR PANTHER; PTHR43429:SF3; NADH OXIDASE-RELATED; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF18113; Rbx_binding; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:ADM97155.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006859}.
FT DOMAIN 4..278
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 317..385
FT /note="Rubredoxin binding"
FT /evidence="ECO:0000259|Pfam:PF18113"
SQ SEQUENCE 387 AA; 41841 MW; A8112FF2921E7823 CRC64;
MSDDIIVIGA GFAARQLIKN LRKQDTQRPI RLITADSGDE YNKPELSHVI SQHRPADDLT
RMSAAQFAEE QRITLLAHTS VTGIDAGRRQ VICDTRHYDY HTLVLATGAS AVIPPVPGHE
WMLTLNSQQE YRRAETRLTQ ATRILILGAG LIGSELAMDM AQAGKHVTLV DRASHLLSAL
LPVDISARLQ DALLRQGVEL MLNSGLQRLE KTDAGLEVTL MSGRTLEVDE VISAIGLRAN
TSLATAAGLT VNRGIVTDSQ MRTSDPHIYA LGDCAEINGK LLPFLQPIQL TANIAASSII
TSTSNTADQI RGGNGSLTLP AMLIKVKTPL FPLQLAGETQ NPELVWHTIA DRGGIVAKGM
EGEQLRGFVV GGDRMKDAFP LLRQLSS
//
