(data stored in SCRATCH zone)
SWISSPROT: B2UI65_RALPJ
ID B2UI65_RALPJ Unreviewed; 915 AA.
AC B2UI65;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 08-MAY-2019, entry version 71.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:ACD29266.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:ACD29266.1};
GN OrderedLocusNames=Rpic_4167 {ECO:0000313|EMBL:ACD29266.1};
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29266.1, ECO:0000313|Proteomes:UP000002566};
RN [1] {ECO:0000313|Proteomes:UP000002566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539;
CC Evidence={ECO:0000256|SAAS:SAAS00648551};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|SAAS:SAAS00607242};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily.
CC {ECO:0000256|SAAS:SAAS01159039}.
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DR EMBL; CP001069; ACD29266.1; -; Genomic_DNA.
DR STRING; 402626.Rpic_4167; -.
DR EnsemblBacteria; ACD29266; ACD29266; Rpic_4167.
DR KEGG; rpi:Rpic_4167; -.
DR eggNOG; ENOG4108IEF; Bacteria.
DR eggNOG; COG0243; LUCA.
DR HOGENOM; HOG000031440; -.
DR KO; K00372; -.
DR OMA; AANIDTN; -.
DR BioCyc; RPIC402626:GH94-4162-MONOMER; -.
DR Proteomes; UP000002566; Chromosome 2.
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:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR Gene3D; 1.10.10.1100; -; 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 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; SSF50692; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE 3: Inferred from homology;
DR PRODOM; B2UI65.
DR SWISS-2DPAGE; B2UI65.
KW 4Fe-4S {ECO:0000256|SAAS:SAAS00418020};
KW Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW Iron {ECO:0000256|SAAS:SAAS00454562};
KW Iron-sulfur {ECO:0000256|SAAS:SAAS00454505};
KW Metal-binding {ECO:0000256|SAAS:SAAS00077323};
KW Molybdenum {ECO:0000256|SAAS:SAAS01159040};
KW Nitrate assimilation {ECO:0000256|SAAS:SAAS01159049};
KW Oxidoreductase {ECO:0000256|SAAS:SAAS01133048,
KW ECO:0000313|EMBL:ACD29266.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002566}.
FT DOMAIN 10 66 4Fe-4S Mo/W bis-MGD-type.
FT {ECO:0000259|PROSITE:PS51669}.
SQ SEQUENCE 915 AA; 99059 MW; 454A8A48AE1EBFF6 CRC64;
MTTIPIHPVT DAVRTTCPYC GVGCGVLATP QADGSVSIQG DPTHPANAGR LCVKGSALGE
TVSLDGRLLY PAMRERSRDV DAPEFTKPAP LQRVSWDTAL DAVAQGFRRI AEEHGPDSVA
LYVSGQLLTE DYYVANKLMK GFIGTANIDT NSRLCMSSAV AGHKRAFGED LVPVCYDDLE
TADLIVLVGS NTAWCHPILF QRIMRAKEAR PEMKVVVVDP RHTATCELAD LHLPIKPGTD
VSLFNGLLSF LSRRGVVDRN FVTLHTNGPD AALEAAGTES DDVEAVAKAC KLKLDDLLTF
YSWFADTERT ITAFSMGVNQ STAGTDKVNS IINCHLLTGR IGRAGMGPFS ITGQPNAMGG
REVGGLANML AAHMELNDPS HRDLVQTFWA SPRMADKMGL KAVDLFKAIE DGRVKAVWIM
GTNPVVSLPD ADQARRALAK CELVVASDIV EATDTTVLAD ILLPALGWGE KDGTVTNSER
RISRQRAFLQ APGEARADWD IIADVARRMG YDGFDFKSPR DVFDEHARLS AYANDASGVR
RAFHLGGLAG LDAGAYDGMS PVQWPVATSG NGEARLFSDG RFAHADGRAR FVPTPARAPA
HAADGEYPLI LNTGRVRDQW HTMTRTGRAP RLADHVPEPF VDLHPHDALL AGVREGGLAR
VSSRWGSVVA RVRMTGGIAR GSVFVPIHWN GQFASDARVG AVVNPVVDPV SGEPEFKHTP
VMVEPFDVAW HGFVLSRRAL DTDDATWWTR IQGKQFLRYE LAGRQHLGSV HDWARTLLGV
TDPHADWLEY EDATARVYRA VHVVDDRIEA CVFLSPRPDL PSRNWLAGLF AQERLEDLDR
AGVLLGQPIE AGVDVGPTVC SCFGVGRNTI CDAIRTKGLQ STGEITACLK AGGNCGSCVP
ELKRLLVEAR VQQAA
//
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