ID A0A1Y2QIE9_9BURK Unreviewed; 951 AA.
AC A0A1Y2QIE9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:OSZ67724.1};
GN ORFNames=CAP38_02895 {ECO:0000313|EMBL:OSZ67724.1};
OS Hydrogenophaga sp. IBVHS2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1985170 {ECO:0000313|EMBL:OSZ67724.1, ECO:0000313|Proteomes:UP000243193};
RN [1] {ECO:0000313|EMBL:OSZ67724.1, ECO:0000313|Proteomes:UP000243193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBVHS2 {ECO:0000313|EMBL:OSZ67724.1,
RC ECO:0000313|Proteomes:UP000243193};
RA Orr R.J.;
RT "Draft genome sequences of novel bacteria, isolated from environmental
RT samples.";
RL Submitted (MAY-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:OSZ67724.1}.
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DR EMBL; NFUT01000001; OSZ67724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2QIE9; -.
DR STRING; 1985170.CAP38_02895; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000243193; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000243193}.
FT DOMAIN 7..63
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 951 AA; 101523 MW; 667ABA58C5C99446 CRC64;
MTSSGPARST RSTCPYCGVG CGVIIHSEGD RITGVSGDPD HPANFGRLCS KGQTLHLTAD
PVVQRQTRLL QPLHRAQRGG PALPLGWDTA LDLAAERIGG IVQQHGADAV GFYVSGQLLT
EDYYVFNKLV KGLLGSNHID TNSRLCMSSA VAGYKLTLGA DAPPACYDDV QHAGCLFVAG
SNAAYAHPVL FRRIEDARGQ RPDMKMVVVD PRRTDTATQA DLHLAIRPGT DVMLFHGLLH
TLLVQGWVDE AYIQAHTSGF EALQELVGGC TPARVAEVCG VTAADLLTAA RWFAWGGADT
PARNGEARAA TLSLYCQGLN QSQSGTAKNA SLINLHLATG QIGRAGAGPF SLTGQPNAMG
GREVGGLANL LSAHRDLAHP QHRAEVAALW GVPDVPSKPG LTAVEMFQAA ADGQVKALWI
ACTNPAQSMP DQTTVRRALE RAEFVVVQEA FATAATADFA DLLLPATTWG EKDGTVTNSE
RRITRVRPAV PAPGQARHDW RIGVDLAHRL EARLRPGQPT LFPYDRPEAV WNEHRESTRG
RDLDITGLSY AALEQAPQQW PLPEGQTTGR ARLYEDGIYP TADGRARFAA LPWQPLAEER
VSEFPFSLTT GRLRDHWHGM TRTGTLGRLF GHVPEPRIDL HPDDLPPLGL QAGDLVQVTS
KRGRIVVPVQ ADDGVAPGQA FMAMHWGSEY LSGRDRDGRP LAGVNALTTS AHCPRSKQPE
LKHAAVRIEP AGLGWSLLAA AWLPADTALS TREALRRLLP ELAFASCVPF GHDGTGLLLR
AADAAAPDPA LLARITALLG LDTPATLAYS DAARGQWRRV LTSTDHSRRV QGFLLAGDTR
AEAWLLPLLI QREVVQADAR ALLVPGAQAP QPARARSPQV CGCHAVDAAA IDAALTQQAP
DLSEDARLQA LQAGLRCGTG CGSCVPEIRQ RIRTATGMAA PSGLITASHL A
//
