ID A0A258TVJ3_9PROT Unreviewed; 892 AA.
AC A0A258TVJ3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:OYY95468.1};
GN ORFNames=B7Y41_02910 {ECO:0000313|EMBL:OYY95468.1};
OS Hydrogenophilales bacterium 28-61-23.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX NCBI_TaxID=1970530 {ECO:0000313|EMBL:OYY95468.1, ECO:0000313|Proteomes:UP000215898};
RN [1] {ECO:0000313|EMBL:OYY95468.1, ECO:0000313|Proteomes:UP000215898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-61-23 {ECO:0000313|EMBL:OYY95468.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:OYY95468.1}.
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DR EMBL; NCGJ01000002; OYY95468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258TVJ3; -.
DR Proteomes; UP000215898; 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 3..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 892 AA; 96515 MW; EB79A03D49B992FE CRC64;
MTLSPIRTTC PYCGVGCGVL VSREDDDYKV RGDPEHPANL GRLCSKGAAL GETLSLDDRL
LHPEIDGVAT SWDIALDTVA NRFRDVIAEH GPDAVAFYVS GQLLTEDYYV ANKLMKGFIG
SGNIDTNSRL CMSSAVAAHK RAFGADSVPA CYEDLELADL VVLVGSNAAW AHPVVFQRLV
AAKKARPEMK VVLIDPRRTA TAEILQPGAD LHLAIKPGAD AWLFNGLLNH LKREDALNWA
YIEAHVEGFG AALQAVSGVS IPQVAQACGL TEADVAAFFR LFAHTPRTVT LFSQGINQSS
SGVDKGNAII NCHLATGRVG LPGASPFSIT GQPNAMGGRE VGGLANQLAA HMDFSAEAID
RVGRFWRAPN MAQQPGLKAV DMFRAVDDGR IKALWIIATN PAVSLPQADD VVAALRKCPF
VVVSDVVART DTSVHAHVRL PAAAWGEKDG TVTNSERRIS RQRAFLPLPG EARPDWWIVD
QVARRMGHAA AFAFTGPAQI FNEHAALSGF ENDTARDFDL SGLLPAMPVK TGMSAENYDA
LQPVQWPVTA QGGTSRLFAD GRFFTPSGRA RMVPISPRAP VHAVDAAHPF TLNTGRIRDQ
WHTMTRTAMT PKLLAHIAEP YIEIHPDDAR RAGLTEGALA RVSNAHGELL ARVQVGAAQQ
RGSVFAPIHW NAQFSARGRV DVLAHAVTDP ISGQPEFKQT PVAVEAYAAT WQGFVMTRAP
LDCGKQTGYW SKIRGKACWR HEIAGIDQPA DWPADWSKHM RDWLALPGDW IEMADRAAGR
YRGALIRDEQ VQAVYFLERE AAKLPPRHWL ESLFEREALS NDERSALLLG RPSQAVPDCG
RIVCACFGVG ENELNQAIAS GAASVEALGI ELKAGSNCGS CIPELKRLLQ RP
//
