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Database: UniProt
Entry: A4XU39_PSEMY
LinkDB: A4XU39_PSEMY
Original site: A4XU39_PSEMY 
ID   A4XU39_PSEMY            Unreviewed;       905 AA.
AC   A4XU39;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=Assimilatory nitrate reductase (NADH) alpha subunit apoprotein {ECO:0000313|EMBL:ABP84855.1};
DE            EC=1.7.1.1 {ECO:0000313|EMBL:ABP84855.1};
GN   OrderedLocusNames=Pmen_2094 {ECO:0000313|EMBL:ABP84855.1};
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP84855.1};
RN   [1] {ECO:0000313|EMBL:ABP84855.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ymp {ECO:0000313|EMBL:ABP84855.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) 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; CP000680; ABP84855.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4XU39; -.
DR   STRING; 399739.Pmen_2094; -.
DR   KEGG; pmy:Pmen_2094; -.
DR   PATRIC; fig|399739.8.peg.2124; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_1_6; -.
DR   OrthoDB; 9816402at2; -.
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:0009703; F:nitrate reductase (NADH) activity; IEA:UniProtKB-EC.
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   ECO:0000313|EMBL:ABP84855.1}.
FT   DOMAIN          5..61
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   905 AA;  98597 MW;  EAB27B3275603DB3 CRC64;
     MPTQSQITAS TCCYCGVGCG VLIEHDGEKI LGVAGDPSHP ANFGKLCSKG STLHLTGDLD
     ARALHPELRL GKGLARSRTD WDSALDHAAA VFAETIREHG PDSVAFYISG QLLTEDYYAF
     NKLARALVGT NNIDSNSRLC MSSAVVGYKR SLGADAPPCS YEDIEQSDCL LIAGSNMAYA
     HPVLFRRLEE AKARRPEMQI IVVDPRRTDT CELADLHLAI LPGTDVALFH GILHILLWEG
     WVDRRYIDAH TEGFAALKNL VRDYSPAATA DICGISLDAL QRCAELIGRA PSFLSLWCMG
     LNQSSAGSAK NSALINLHLA TGQIGKPGAG PFSLTGQPNA MGGRETGSLS NLLPGHREAG
     NAEHRAEVAA YWGVDALPET PGLSAIELFD AVHDGRIKAL WIACTNPAQS LPNQNKVHEA
     LAACPFVVVQ EAFFTTETCR YADLLLPAAS WGEKEGTVTN SERRVSHVRR AVPAPAEARS
     DWSITCDFAR RLETLLRPGL PSLFDFTSSE ALFEEYKHLT AERDLDLSGL SYALLDDQGP
     QQWPFAPGAR QGTARLYADG LFPTASGRAQ FHADPYRAPK EKREARYSLT LNTGRLRDQW
     HGMSRTGTAA RLFGHVEAAV LGLHPDELRR RRLQDGDLVK LRSRRGSLIL PVQADESVRP
     GQAWLPMHWG DRFLKGLGTN VLTQPAFDPL SKQPELKHAG VEVDKVELPW QLFALVEGEV
     QSRFEALRPL FEEFAYASLT PTGRERPALL IRAASAVAPQ PELLAQIDRL LRLNQGPVLA
     YDDPRRAVGK RVRIEDGRIV STRLAGETAA SEWLRSLWLD GQADADLRRW LLAPVSAPPG
     NATATTRGKT LCNCLNVSES AVCAGIERGL DLNGLKQELK CGTSCGSCVP EIKRLLAQQP
     MATQA
//
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