ID A0A1I4RHX4_9BURK Unreviewed; 941 AA.
AC A0A1I4RHX4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Assimilatory nitrate reductase (NADH) alpha subunit apoprotein {ECO:0000313|EMBL:SFM51553.1};
GN ORFNames=SAMN05444747_10622 {ECO:0000313|EMBL:SFM51553.1};
OS Variovorax sp. OV329.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882825 {ECO:0000313|EMBL:SFM51553.1, ECO:0000313|Proteomes:UP000199688};
RN [1] {ECO:0000313|EMBL:SFM51553.1, ECO:0000313|Proteomes:UP000199688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV329 {ECO:0000313|EMBL:SFM51553.1,
RC ECO:0000313|Proteomes:UP000199688};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOUG01000006; SFM51553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4RHX4; -.
DR STRING; 1882825.SAMN05444747_10622; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000199688; 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:UP000199688}.
FT DOMAIN 1..57
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 941 AA; 100836 MW; 0A947B554310B7F8 CRC64;
MTETRSTCPY CGVGCGVIIE SDGTQITGVR GDPQHPANFG RLCTKGSTLH LTASAEITRQ
TRLLQPMQRL QRGTEPQPVS WDHALDTAAL KFSNVIREHG PDAVGFYVSG QLLTEDYYVF
NKLAKGLIGT NNIDTNSRLC MSSAVAGYKK TLGADAPPAC YEDFDHAQCL FIVGSNTAWA
HPILFRRIED AKRANPAMKI VVADPRRTDT AEIADLFLPI QPGTDVMLFH GMLHLMLREG
WTQPGYIAAH TSGFDALEAV VRDCTPEKAA QVCGIAVEDL REAARLFATS AATLSLYCQG
LNQSSSGTAK NAALINLHLA TAQIGKPGAG PFSLTGQPNA MGGREVGGLA NLLSAHRDLG
NPAHRAEVAA LWGVPDVPAT PGKTAVEMFQ AAADGEIRAL WIACTNPAQS MPDQRTVRRA
LERCELVVVQ EAFASTATCA YADLLLPATT WGEKVGTVTN SERRISRVRP AVPAPGEARH
DWSAATDFAR RLEALLPARK TSIALFPYEL DSETGAVAIW NEHRESTRGR DLDITGLSWS
VLDSQGPQQW PMPAGQPVGR QRLYKDGVFP TPDGRARFVA TAYQPVAEQC EARYPIALNT
GRLRDQWHGM SRTGTLGRLF GHVPEPVVQL HPQDMAQRKL QDGDLVYLTS RRGSIVLPAQ
GSSELGASQA FVAMHWGSEF LGGRASAGET LAGINALTTP AYCPDSKQPE LKHTAVKVLK
AELPWSLLAA AWLPDDSALQ TLRSLRELMK EFPFASCVPF GAAGALDGDS ERSGVLFRAA
GHDPASPALL AQVESLLGLA GTDVIRYADA RSGQRRAARL VRAGGEAYLE AFLLGGDIRA
ESWIKALLQQ RLPAQSLGRQ LLRPGPKAPA GVRSSGKTVC SCFGVSETAI DQALQCGSGS
EAERLSALQG ALRCGTNCGS CVPELKRKVR VLVASREAVG A
//
