ID Q1IDH0_PSEE4 Unreviewed; 1331 AA.
AC Q1IDH0;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE SubName: Full=Assimilatory nitrate reductase {ECO:0000313|EMBL:CAK14289.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:CAK14289.1};
GN Name=narB {ECO:0000313|EMBL:CAK14289.1};
GN OrderedLocusNames=PSEEN1417 {ECO:0000313|EMBL:CAK14289.1};
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676 {ECO:0000313|EMBL:CAK14289.1, ECO:0000313|Proteomes:UP000000658};
RN [1] {ECO:0000313|EMBL:CAK14289.1, ECO:0000313|Proteomes:UP000000658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48 {ECO:0000313|EMBL:CAK14289.1,
RC ECO:0000313|Proteomes:UP000000658};
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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; CT573326; CAK14289.1; -; Genomic_DNA.
DR RefSeq; WP_011532705.1; NC_008027.1.
DR STRING; 384676.PSEEN1417; -.
DR GeneID; 32804677; -.
DR KEGG; pen:PSEEN1417; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG0369; Bacteria.
DR HOGENOM; CLU_000422_6_1_6; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000000658; Chromosome.
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:0010181; F:FMN binding; IEA:InterPro.
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 GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProt.
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 CDD; cd06199; SiR; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
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; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CAK14289.1}; Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 3..59
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 811..949
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 971..1181
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1331 AA; 145810 MW; D34D9547EBEC610A CRC64;
MSSSEVRSVC PYCGVGCGTV MSVADGKVVK VSGDKQHPSN FGRLCTKGLT AHIPLTTGRM
AHAWLRRQRD QEPVRDGLDE AIAETASRLR AIIDRHGADA VALYVSGQMS LEAQYLANKL
AKGYIRTRHI ESNSRLCMAS AGSGYKQSLG ADGPPGSYQD FEHAEVFLVI GANMADCHPI
LFLRLLDRVK AGARLIVVDP RRTATADKAD LFLQVRPGTD LALLNGLLHL LHANGHTAPD
FIARHTEGWE ALPAFLADYT PERVATITGL PEADIRQAAT WIGQSKNWMS CWTMGLNQSI
HGTWHSNALC NLHLATGAIC RLGSGPFSLT GQPNAMGGRE MGYMGPGLPG QRSAQVDADR
AFVERQWQLA PGTLRSDGGE GTVALFEQMK QGEVKACWII CSNPVASVAN RQQVIDGLRQ
AELVICQDAF LDTETNRHAD ILLPAALWAE GEGVMVNSER NLTLMPRAVE PPGESLEDWR
LIARVASAMG YGQAFDYPDA EAVYEEIRRF WNPATGYDLR GIGYPELRER PRQWPCAPGR
EDARSPLRYR NDGVSQQVLH DEQGARPALA FPTPSGKARF LARPWLPAAE QADEAYPFVL
NTGRVQHQWH TLTKTGQVPS LNKLEPGPFV EINPEDAQRL GIRDRDTVAI RSRRGLAQLP
ARISARVLPG GCFAPFHWND LYGEQLAINA VTCDAVDPTS LQPAFKYCAV ALERVAGERI
DAIDLVSEPA RMPTATLSRL LGLDVLPAPE LAEDERHYLQ GFLLGLGQAR AEGVPRLPAD
APLAPARRLF VEGLLAALFS QPPAANEVPS HHVVWASQTG NSETLAERCA QHLREAGLPV
RLSCMDALGP AQLQGAASVL LIASTFGDGD APDCATAFWQ ALQGEEGGHC ATLPYAVLAL
GDSSYDQFCG FGRKLDQRLA ELGARRLLAR VDCEGDIDEA FSGWLDALMK QLGSAMPTPV
EPKPVTGCGK QQPWCAAVLE NRLLNTPGSA KETRQLVFDL RDSGFTYQPG DALGVWPRNC
PVLIEELLLL MQLDGQAAVE LKGHAPMPLS VALEHHLDIT RVTSQQLERF SQGSDDLRRL
LQPERKTELK GWLWGRQLAD VLRAFPQRLS LTDWLGLLKP LQPRLYSISS SPSAHPDQVH
LTVSTVRYGA RKGVCSSFLA DRAGALKVAI FPQPSKHFRL PEDDATPIIM IGPGTGIAPF
RAFLEEREVR GASGRNWLFF GEQHAASDFY YREQLLAWEG SGHVRLSTAF SRDQPEKIYV
QQRLLEQGAE LWRWLEEGAF IYVCGDAQRM ARDVDAALRQ VVAVQGGMND EAAAAWVEAL
GKAGRYRRDV Y
//
