ID A0A0T2Q8N1_9SPHN Unreviewed; 868 AA.
AC A0A0T2Q8N1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:KRA80582.1};
GN ORFNames=ASD76_15610 {ECO:0000313|EMBL:KRA80582.1};
OS Altererythrobacter sp. Root672.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=1736584 {ECO:0000313|EMBL:KRA80582.1, ECO:0000313|Proteomes:UP000051125};
RN [1] {ECO:0000313|EMBL:KRA80582.1, ECO:0000313|Proteomes:UP000051125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root672 {ECO:0000313|EMBL:KRA80582.1,
RC ECO:0000313|Proteomes:UP000051125};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA80582.1, ECO:0000313|Proteomes:UP000051125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root672 {ECO:0000313|EMBL:KRA80582.1,
RC ECO:0000313|Proteomes:UP000051125};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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}.
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:KRA80582.1}.
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DR EMBL; LMHH01000003; KRA80582.1; -; Genomic_DNA.
DR RefSeq; WP_055925202.1; NZ_LMHH01000003.1.
DR AlphaFoldDB; A0A0T2Q8N1; -.
DR STRING; 1736584.ASD76_15610; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000051125; Unassembled WGS sequence.
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:InterPro.
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:UP000051125}.
FT DOMAIN 1..57
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 655..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 868 AA; 94132 MW; F0018B9A95C9F309 CRC64;
MQPIRTTCAY CGVGCGIKAT VTGEREVTIA GDAEHPANRG KLCSKGTHLG ETVGLEGRLL
YPEIKGKRAS WDKAIRQVAR TFAETIERHG PDSVAFYVSG QLLTEDYYVA NKLMKGFIGS
ANIDTNSRLC MSSAVAGYTR AFGEDVVPAT YEDLDKADLV VLVGSNTAWC HPVVYQRIMA
ARLLRGTKVV VIDPRRTETC EEADLHLQLR PGTDVALMNG LLAYCRDAGV LDEAFLAQHV
ATPDDFWSAL GEGSDLWSTA RTCDLAPLDL KRFFELFAAN PRTVTLFSQG INQSIRGTDQ
VNAIVNVHLA TGRIGKPGAA PFSITGQPNA MGGREVGGLA STLAAHRDFA PENVAEVKRF
WAAPRMAEKP GLKAVDLFRS IREGRVKALW VMATNPAVSL PDAAQVREAL ALCPFVVVSD
CIGDTDTSRF ADVKLPAVGW GEKDGTVTNS ERLISRQRAL MPAPGEAKPD WWIVTQVARA
MGWRDAFAYE NAADIYREHA RLSAYRNEGK RKFDIGFHGA ITNREYDAME PTRWGGAPFA
EGRFSTPDGK ARLIAVEQRE LDPALAKWPL TLNTGRYRDQ WHTMTRTGLS PRLSQHRREP
QVEIHFLDAE QQGIGDGDLV RVATPQGESV FRAVISEGQR RGEIFTPIHW TDRQSSGGRT
GLLPRPLVDP HSGQPGFKST PARLEKLAVE WRGFLIAREV PEPIGADYFT KVKVGQGWLV
ELAGNGEPDV TLGNLLAGGQ RIESLDRARG GWRAAVLDGN GRLSAALFVS SAGRLPDREW
LIAQLAAAET ASSVELLAGR PATPQADRGP IVCVCFDVGM KTIVEAIGSQ GLISVEAVGK
ALSAGTNCGS CKPAIQRLIG ETKEAAHA
//