ID A0A345P6L1_9GAMM Unreviewed; 913 AA.
AC A0A345P6L1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:AXI02920.1};
GN ORFNames=HYN46_08755 {ECO:0000313|EMBL:AXI02920.1};
OS Aquirhabdus parva.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Aquirhabdus.
OX NCBI_TaxID=2283318 {ECO:0000313|EMBL:AXI02920.1, ECO:0000313|Proteomes:UP000253940};
RN [1] {ECO:0000313|EMBL:AXI02920.1, ECO:0000313|Proteomes:UP000253940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYN0046 {ECO:0000313|EMBL:AXI02920.1,
RC ECO:0000313|Proteomes:UP000253940};
RA Kim M., Yi H.;
RT "Genome sequencing of Moraxellaceae gen. HYN0046.";
RL Submitted (JUL-2018) 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; CP031222; AXI02920.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345P6L1; -.
DR KEGG; mbah:HYN46_08755; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000253940; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000253940}.
FT DOMAIN 13..69
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 913 AA; 98830 MW; 507166B26220F476 CRC64;
MTVDTVLTAS LRGEAIKTTC AYCGVGCGVL ATVDADRHFS ISGDLEHPAN FGRLCVKGSA
LGETVGLEGR LLYPAIGGVR ADWDHTTTYI ASQLKDIIAE HGPEAVAFYV SGQFLTEDYY
VVNKLAKGFI GTPNVDTNSR LCMSSAVAGH KRAFGTDTVP NSYEDFEHAD LLTFVGSNAA
WCHPILYQRI KKAKANNPEM KIVSIDPRKT DTNEIVDLHL PIKSGMDVLL FNYLLVEVSK
SPALNTTYID QFTDGLADAL LAAQRDVALG DVAERLGVDG VTLAQFVEWF IATPKAMTLF
SMGVNQSGQG TDKVNAIINV HLATGRIGSE GAGPFSLTGQ PNAMGGREVG GLANMLAAHL
DIHEPSHRAL VQDFWQSPTM IEKQGLKAVD LFDAVATGKV KAVWIMATNP IVSMPNADRV
RDALANCPLV IVSDVIADTD CTRVADVVLP ALGWGEKDGT VTNSERCISR QRGILAGAGE
SRADWWALAQ VAQKMGFEGF DYQSARDVFV EHAALSGVDN QEGGVLRDFD ISALSALTQG
EYDALNPIQW PIKLVDQKLV GTQRLFEQGG FFTTNRRAKI VPVQNVATGN VTSNEFPYAL
NTGRIRDQWH TMTRTGLTSR LTRHIGEPFA ELNPKDAEKL HVSSGDILQI NSQWGQALAR
VIISDGQQPG MVFVPIHWNG INSTQSRIGA VVNPVVDPYS GQPECKHTPV MLKKAALNTH
GFIMSLNSLN LIKADYAVNV RTLNGFRHEF AFTDDMLHET NLNLSEWLSS QVVVPVQAER
MEYIDLAQGI VRFAWVLDQQ LIAFAAIASN PDARATLPPR SWLDDQLGQE VSSVTRRTLL
SGLAADPNSD VGPIVCSCFS VGKNTITRAI HAQNLTTVAA VGQCLKAGTN CGSCQSEIFR
LLEQECKPVA SAV
//
