ID A0A0C2IMM5_9PSED Unreviewed; 1434 AA.
AC A0A0C2IMM5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Assimilatory nitrate reductase large subunit {ECO:0000313|EMBL:KIH86242.1};
GN ORFNames=UCMB321_0115 {ECO:0000313|EMBL:KIH86242.1};
OS Pseudomonas batumici.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=226910 {ECO:0000313|EMBL:KIH86242.1, ECO:0000313|Proteomes:UP000031535};
RN [1] {ECO:0000313|EMBL:KIH86242.1, ECO:0000313|Proteomes:UP000031535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCM B-321 {ECO:0000313|EMBL:KIH86242.1,
RC ECO:0000313|Proteomes:UP000031535};
RA Klochko V.V., Zelena L.B., Elena K.A., Reva O.N.;
RT "Complete genome of Pseudomonas batumici UCM B-321 producer of the batumin
RT antibiotic with strong antistaphilococcal and potential anticancer
RT activity.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KIH86242.1}.
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DR EMBL; JXDG01000001; KIH86242.1; -; Genomic_DNA.
DR STRING; 226910.UCMB321_0115; -.
DR PATRIC; fig|226910.6.peg.116; -.
DR Proteomes; UP000031535; 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: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: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; IPR027467; MopterinOxRdtase_cofactor_BS.
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; PS00551; MOLYBDOPTERIN_PROK_1; 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 Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 60..116
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT DOMAIN 892..1030
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 1067..1283
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1434 AA; 156281 MW; B90F4E34027133E0 CRC64;
MPAQAINVDG RVFHSPGNSH DKGAVPLPLK NVEQQALFSF PPEPVFTPRG RPMTETQMPS
KTVRSVCPYC GVGCGIVMQV ENNLIVKVSG DKQHPSNFGR LCTKGSTCGQ AVADSGRMEH
AFLRSQRDRD PARVGIDQAI SATASRLRAI IDTHGADAVA LYVSGQMSLE AQYLANKLTK
GFIRSRHIES NSRLCMASAG SGYKLSLGAD GPPGSYEDFE HSELFLVIGA NMADCHPILF
LRLLDRVKAG AKLIVVDPRR TGTADKADLF LQIKPGTDLA LLNGLLHLLV KNGHSDRDFI
AAFTEGWEVM PDFLEDYTPA RVAELTGLAE ADLLQAAQWI GQAANWMSCW TMGLNQSVQG
TWHTNALCNL HLATGTLCRP GSGPFSLTGQ PNAMGGREMG YMGPGLPGQR SALVSGDRAF
IEDLWQIAPG SLRAEAGEGT VAMFEAMRAG SIKACWIICT NPVASVPNRQ NVIEALQAAE
LVISQDAYLD TETNRYADIL LPGALWAEAQ GVMINSERNL TLMQQAVQPP GETLPDWQII
ARVACEMGYA EAFTYDSAEA VFEEIKQAWN PKTGYDLRGA SYARLREQPL QWPCAEAQGA
TRNPIRYLND GLSQALKHDQ DGRQPAIAFP TESGKAQFFA RPHLMPAEMP DEEFPLVLNT
GRVQHQWHTL TKTGKVPTLN KLNPGPFVEI HPSDATRLDI KERDPVQIRS RRGRAVLPAV
ITDRVRPGNC FAPFHWNDVF GEDLAINAVT SDAIDPLSLQ PAFKFCAVNL LALAPEPTRL
VPELALAGAS TVASEGFSPM QLKAFARLLN LDTPAELSLA ADERLYMQGY LLGLRSAEAK
APGVPTLPAS APFDADKRLL LDGLLAGLFS RTAGPAPEPQ TAATVQATRP EWLVLWASQT
GNSEELAQAC AKLLDAAGQR TRLRAMDEAG LDDLRGASSV LLVTSTFGDG DPPDNAASFW
QALQGAQDQA LAQSRYSVLA LGDANYDQFC GFGRKLDERL SELGAERLLP RLECEQDTQQ
AVEPWLTTLC AALSGSSAPP AALPPVAEVA PATPAAPADI GSPYSRHHPL RAHLLHNQVL
NAPGAEKETR HLVFDLGDQD FPYQAGDALG VWPSNCPESV EQLLGLLELD GASVVTLKDK
APMALREALL DHLDITRITP EILRRVCGLC ASPWLDELQE EANQARLKEW LWGRQLLDLL
REFPISLGAN QLISLLKPLQ PRLYSISSSA KVTPGQVHLT VSTVRYRHGE QIRGGVCSTF
LADRAAGSGA RLFIQRTTHF RVPQDPRTPL IMIGPGTGIA PFRAFLQERQ AQGADGKNWL
FFGEQRATSD FYYREELDAW LRSGHLSRLD TAFSRDQTEK IYVQQRMLEA GAQLWKWLEQ
GACVYVCGDA SRMAKDVDAA LKKIVQVHGR MSGGAAALYV SAMSKDRRYL RDVY
//
