ID A0A0J6NKP7_9NEIS Unreviewed; 897 AA.
AC A0A0J6NKP7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:KMN81289.1};
GN ORFNames=VK98_14305 {ECO:0000313|EMBL:KMN81289.1};
OS Chromobacterium sp. LK11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=1628212 {ECO:0000313|EMBL:KMN81289.1, ECO:0000313|Proteomes:UP000036114};
RN [1] {ECO:0000313|EMBL:KMN81289.1, ECO:0000313|Proteomes:UP000036114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LK11 {ECO:0000313|EMBL:KMN81289.1,
RC ECO:0000313|Proteomes:UP000036114};
RA Chan X.Y.;
RT "Draft genome of Chromobacterium aquaticum LK11.";
RL Submitted (MAY-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}.
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:KMN81289.1}.
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DR EMBL; LDUR01000022; KMN81289.1; -; Genomic_DNA.
DR RefSeq; WP_048414678.1; NZ_LDUR01000022.1.
DR AlphaFoldDB; A0A0J6NKP7; -.
DR STRING; 1628212.VK98_14305; -.
DR PATRIC; fig|1628212.3.peg.1959; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000036114; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000036114}.
FT DOMAIN 1..57
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 897 AA; 95784 MW; AAA1E8499FDCD487 CRC64;
MSTTPSTCCY CGVGCGVLIH SDGARITGVE GDPAHPANHG RLCSKGLALA DSCASLSGRA
LHPELRLSRD AARRRVDWDC ALDTVAERLA GVIRRHGPDA VAVYASGQLL TEDYYLFNKL
TKGLIGSNNI DTNSRLCMSS AVSGYKLALG ADGPPTCYQD LELADCVLLA GSNMAYAHPV
LFRRLEAAKA ARPDSKWIVV DPRRTDTAAL ADLHLQIQPG SDVALFNGML HHLIWEGLID
EGYIAAHTEG FDALKRLLRD YSPRQAAGLC GIAEADLTAA AEWFGRSPAS LSLYCMGLNQ
SSHGTAKNLA LINLHLAAGQ IGRPGAGPFS LTGQPNAMGG REVGGMATML AAHRDIANPQ
HRAEVAAHWG LPPERLSDRP GLPAIALFDA LKAGRVKAVW IVCTNPAHSL PDLEQARQAL
AQAEFVIVQD AYADTDTAAC ADALLPAASW GEKEGTVTNS ERRVSRVRAA APPPGEARAD
GWIAAEVGRR LERLLYPDAP SLFRDCEPAA VFAEHAALTA GRDLDLSGLS HALLERDGPQ
QWPFPAGAAG GQARRYQDGR FPTASGRAQF HATPYRPPAD AVNAHYPFRL LTGRLRDQWH
GMSRSGRVAR LFSHAPEPTL DMHPADAARR GLQAGELVKV ESRRGGLVLP LALSEDLPGG
CVFAAMHWSG QHLDSGGVNQ ACSPAVDPQS FQPELKHAAV RVERAELPWR VRAASRHPDL
PALRARLQPL LAGCGYAALS LRPPDILVLS AAHAQPRPDW LSELAWLLEL DGGPQLQSFS
DARRGLEQRI AWRDDAPWAF VFAGGQDDGA RLLAAMQSGK PWPGSRLSAL LPDIAAAPAA
ARIVCNCLQV DAERIRAAIA AGADLAGLKG QLGCGGVCGS CLPELKRMLA RQTEREY
//