ID A0A0G3FZS8_9GAMM Unreviewed; 896 AA.
AC A0A0G3FZS8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:AKJ94478.1};
GN ORFNames=TVD_03430 {ECO:0000313|EMBL:AKJ94478.1};
OS Thioalkalivibrio versutus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=106634 {ECO:0000313|EMBL:AKJ94478.1, ECO:0000313|Proteomes:UP000064201};
RN [1] {ECO:0000313|EMBL:AKJ94478.1, ECO:0000313|Proteomes:UP000064201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D301 {ECO:0000313|EMBL:AKJ94478.1,
RC ECO:0000313|Proteomes:UP000064201};
RA Mu T., Zhou J., Xu X.;
RT "Complete Sequence for the Genome of the Thioalkalivibrio versutus D301.";
RL Submitted (APR-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; CP011367; AKJ94478.1; -; Genomic_DNA.
DR RefSeq; WP_047250810.1; NZ_CP011367.1.
DR AlphaFoldDB; A0A0G3FZS8; -.
DR STRING; 106634.TVD_03430; -.
DR KEGG; tvr:TVD_03430; -.
DR PATRIC; fig|106634.4.peg.699; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000064201; Chromosome.
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; IPR006655; Mopterin_OxRdtase_prok_CS.
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; PS00490; MOLYBDOPTERIN_PROK_2; 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:UP000064201}.
FT DOMAIN 5..63
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 896 AA; 96776 MW; 6D057EE7DE94072F CRC64;
MATSDAVTRT TCPYCGVGCG VEVTATPRAE FPVAVRGDAS HPANAGRLCS KGAALAETLG
DEGRLLHPEI EGVRVDWDAA LDHVAGGFRD VIDRYGPDAV ALYVSGQILT EDYFVANKLM
KGFVGSANID TNSRLCMSTA VAAHTRAFGM DGVPGSYTDF EQADLVVVVG SNMAWAHPVL
FQRLQAARAA RPEMKLVVID PRCTATAQAA DLHLPLAPGT DAWLFNGLLD HLRREDALDP
AFLERHVDGF ADALAAARAS SPSIAVTAET CELAPEAVAT FFRWFARTER TVTAFCQGIN
QSDSGVDKAG TILNVHLATG RIGRPGMGPF SLTGQPNAMG GREVGGLASQ LAAHMGFDEV
SLDRVSRFWN APNLARNPGL KALDLFRAVE SGQVKAIWII GTNPLFSLPE AERFERALRD
CPLVVVSDCV RETETTRVAD VLLPATTWGE KDGTVTNSER RISRQRPFRE PPGEARHDWW
ALAEVARRLG FAEAFPYTQP VEIFREHAAL SAFENDSTRD FDIGALAATD AAAFEALEPV
QWPLPAGAEA GTPQLYADGR FFTANGRARL AAVTPQSPTD TIDAEYPLRL NTGRIRDQWH
SMTRTASTPR LSAHQPEPFV EIHPVDAGLF RAQAGDLAEV TSRHGRLLAR VQVSREQRPG
SVFVPMHWSR PIARLARVDA LVPAHVDPVS GQPAFKHTAV SVRPAAMDWH GFVLSREPVS
LPEADYAVTA RGPRHLRFEL AGRGAPPEIA DWRARLDGPG EWLEFADPAG GRYRAARIHE
GRLACVLFAG PDRGLPEREW LGGLFAAESI TDAERMALLT GRPPNGQAAR GRLVCACFGV
DETRIRTAIR EHGLATCEAV GACLEAGTNC GSCRPEIQTL LNEESEAPTD PVAREG
//