ID A0A0P1GMK6_9RHOB Unreviewed; 881 AA.
AC A0A0P1GMK6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:CUH77147.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:CUH77147.1};
GN Name=nasA {ECO:0000313|EMBL:CUH77147.1};
GN ORFNames=TRM7557_01230 {ECO:0000313|EMBL:CUH77147.1};
OS Tritonibacter multivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=928856 {ECO:0000313|EMBL:CUH77147.1, ECO:0000313|Proteomes:UP000052022};
RN [1] {ECO:0000313|EMBL:CUH77147.1, ECO:0000313|Proteomes:UP000052022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7557 {ECO:0000313|EMBL:CUH77147.1,
RC ECO:0000313|Proteomes:UP000052022};
RG Swine Surveillance;
RL Submitted (SEP-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; CYSD01000018; CUH77147.1; -; Genomic_DNA.
DR RefSeq; WP_058289340.1; NZ_JAQIPA010000021.1.
DR AlphaFoldDB; A0A0P1GMK6; -.
DR STRING; 928856.SAMN04488049_11524; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000052022; 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: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 InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
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.
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 ECO:0000313|EMBL:CUH77147.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052022}.
FT DOMAIN 11..67
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 881 AA; 94576 MW; 3799DB3B894DF902 CRC64;
MSREDQFSDD QTWTRSTCPY CGVGCGVLLR RDAEGGVEVK GDPSHPANLG RLCSKGSALG
ETVGLEGRLL APRIHGINAS WDNALDLVAE KFSTTIAEHG PDSVAFYVSG QLLTEDYYVA
NKLMKGFIGS ANIDTNSRLC MASSVAGHKR AFGTDTVPGT YEDLEQADLV VLVGSNLAWC
HPVLYQRLMV ARAERGTKIV VIDPRRTASC DGADLHLPLR SGSDVALFNH LLAQIDAQGA
VEADFLNNVD GFDAALSTAK DASLDPTGLD ADLVQAFCDM WIGNPKVVTI YSQGVNQSSS
GADKVNAILN CHLATGRIGL PGCGPFSVTG QPNAMGGREV GGLANMLANH LDIENEAHRD
LVQSHWNAPT IATTQGLKAV DMFEAIHAGK IKALWVIHTN PAVTLPDAGR VAEAIQNCDF
TVVSDITATT DTARLADVIL PASAWGEKSG TVTNSDRTIS RQRSLMPAPG QARADWKILC
DVAKRMGWAE AFDYETEADI FREYTALSTA ARVFGKDLDL SGWDGMSNAD YDALRPTRWP
ISDTRQGGRF FADGQFFHAG GKAKMLAVTH RAPATKRAPK YPFRLNTGRI RDQWHTMTRT
GLSPRLSSHL AEPFVDIHPQ DAEGLGITAA DLVQLTSPQG QSILRARITT DVRRGDVFAP
IHWTGETAPS ARIDQLVAPF VDPVSGQPES KASVVALAPY KAAWYGFAIC AEDLDPACEY
WARARTQQGW RAELAGLNAP ADWEVEARKI FNLPEATAQV MRDPAKGTAR IAFHDEGRLL
AALFVAPEPV AVMRDYLARL PGSEAAGVLT GRAPLDLPDP GPVLCSCFSV GINTILDAIE
TRGLMTVDAI GEALDAGTNC GSCRPEIADL LARVHMAEAA E
//