ID A0A0S8A558_9GAMM Unreviewed; 891 AA.
AC A0A0S8A558;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:KPJ93867.1};
GN ORFNames=AMJ55_07300 {ECO:0000313|EMBL:KPJ93867.1};
OS Gammaproteobacteria bacterium SG8_15.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1703403 {ECO:0000313|EMBL:KPJ93867.1, ECO:0000313|Proteomes:UP000053644};
RN [1] {ECO:0000313|EMBL:KPJ93867.1, ECO:0000313|Proteomes:UP000053644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_15 {ECO:0000313|EMBL:KPJ93867.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPJ93867.1}.
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DR EMBL; LJNL01000115; KPJ93867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8A558; -.
DR PATRIC; fig|1703403.3.peg.414; -.
DR Proteomes; UP000053644; Unassembled WGS sequence.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
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.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 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}.
FT DOMAIN 2..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 891 AA; 98263 MW; AD14002E7404E3E8 CRC64;
MEQVTKTTCP YCGVGCGVIM TQDSKGVTSV TGDPDHPANF GRLCSKGAAL AQTIDLPGRL
LHPTVNSERV GWGDAIDEVA QGFSNVIDRY GPDALAFYVS GQILTEDYYV ANKLMKGFVG
SANIDTNSRL CMSSSVAGHK RAFGADIVPC CYEDLERSNM IVLTGSNTAW CHPVLFQRIK
QAKKNNPQLY VVVVDPRRTS TCDIADLHLP LAAGSDANLF TGLLAYLHRQ GEENQLFTRA
FTEGLLETLN IALSSAFELE QVAAGCGLSV DQVKTFYQHF ARTERVITVY SQGVNQSSSG
TDKVNSIINC HLYTGRIGRP GMGPFSFTGQ PNAMGGREVG GLANQLAAHM DIDNEQHRAL
VQQFWQSPHI ATQQGLKAVD LFDAIYQGRI KAVWIMGTNP AVSLPDARRV KDALARCQFV
VVSDCMQHTD TTKFAHVLLP AATWGEKDGT VTNSERRISR QRAFITPPGE AKPDWWIITQ
VARAMGYSDA FHYQSPYDIF LEHASLSGFE NNDERDFDIS GLTALSQQQY DELNPVQWPV
KADQDAQANQ RFFADGRFYT PSRKARFVAV SPRKPANAPT SDFPLVLNTG RLRDQWHTMT
RTGKSGRLTS HEPEPYIAIH AEDADKYRIV DNGLVVVKSR WGELTVKARL SDEQSPGTVF
IPMHWNLQFA SAASVGDVIN PALDPVSGQP EFKHTPVSIE PRQFAWRGFL LSRRTLPVEE
ANFWVKVYGN QFVRYELAGD SPASDWAQWA RQLLCQSDSN VNWIEYFDGS SNYRGARMLG
DKLESCVFIS ATGNLPSREW LSNLFGKEEI SQQERVYLLS GKPPSEATDI GHVVCACFGV
GEKQILHAIQ QQGCSTVEAI GAAMQAGTNC GSCIPELQEL LRNQAELLSS A
//
