ID A0A0U5L5X1_9GAMM Unreviewed; 868 AA.
AC A0A0U5L5X1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:CUU23863.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:CUU23863.1};
GN Name=nasA {ECO:0000313|EMBL:CUU23863.1};
GN ORFNames=EM595_1629 {ECO:0000313|EMBL:CUU23863.1};
OS Duffyella gerundensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Duffyella.
OX NCBI_TaxID=1619313 {ECO:0000313|EMBL:CUU23863.1, ECO:0000313|Proteomes:UP000059419};
RN [1] {ECO:0000313|Proteomes:UP000059419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Blom J.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Nitrogen metabolism. {ECO:0000256|ARBA:ARBA00004909}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
CC {ECO:0000256|ARBA:ARBA00008747}.
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DR EMBL; LN907827; CUU23863.1; -; Genomic_DNA.
DR RefSeq; WP_067430139.1; NZ_LN907827.1.
DR AlphaFoldDB; A0A0U5L5X1; -.
DR STRING; 1619313.EM595_1629; -.
DR KEGG; ege:EM595_1629; -.
DR PATRIC; fig|1619313.3.peg.1693; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000059419; Chromosome 1.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR CDD; cd02754; MopB_Nitrate-R-NapA-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CUU23863.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059419}.
FT DOMAIN 1..53
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 868 AA; 93322 MW; 5D638AFF09533729 CRC64;
MNSTCPYCGV GCGVTVTSRA GAVQVSGDGE HPANAGRLCV KGAALADTLG ETGRLRYPHV
NGSRVSWETA LDAVASGLQQ VIDQHGSQAV AFYASGQLLT EDYYVANKLM KGFIGAGNID
TNSRLCMASA VVGYKRAFGA DAVPCSYADL DHADLVILCG SNTAWAHPVL WQRLVQAKLQ
RPAMQVVVID PRRTASCDIA DVHLALRAGS DAALFNGLLH WLAQQGTDSS MLPHLADVPT
ALDAASGWSP AQVAAYCQLS EEQVTAFYRA FASQRNVLTL YCMGINQSTS GSDKCNAIIN
CHLLSGKIGR NGSGPFSLTG QPNAMGGREV GGLATQLAAH MDFSAENVAR LQRFWGSDRV
AQQPGLSAVA LFDAVARGEV KAIWIMGTNP AVSLPEASRV RQALAHCPLV IVSDVAAQTD
TSELAHICLP AAAWGEKNGT VTNSERRISR QRAFVPPVGE ARPDWWILAQ VAQRLGFHQA
FAWHHPAEIF CEHAALSGFE NHGSRAFDIS GLASLSVAEW DRLQPVQWPV NASAPQGTAR
LFSDRRFFHP DGRARLIAVT PRLPLAACTT AYPLLLNTGR IRDQWHTMTR TGQVPRLMQH
VSEPYVAMHP QDAADYQLQA RDLVRVQSSQ GWMIARAVLT DDQPVGTLFA PMHWNCQFAA
QSSVGALVAA QVCPLSGQPE SKQTAVQIAR WHSHWQGTLF SRDNVTFPDG VWWSRIPHTH
ATRYQLAGSG PLSALLSALD LNDMACQRME GTNELRLLAW HDGELMLALW LGPRVPELDL
AFIDAAFASP PTRAADRHAL LGGRAAEREN AGRTVCSCFG TGEQTILCAV AAGDNSLAAL
GARLKCGTNC GSCIPELKQL IARFPAHA
//