ID A0A1E5XAR7_9PSED Unreviewed; 902 AA.
AC A0A1E5XAR7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:OEO25464.1};
GN ORFNames=AX279_11210 {ECO:0000313|EMBL:OEO25464.1};
OS Pseudomonas sp. J237.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1904754 {ECO:0000313|EMBL:OEO25464.1, ECO:0000313|Proteomes:UP000095383};
RN [1] {ECO:0000313|EMBL:OEO25464.1, ECO:0000313|Proteomes:UP000095383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J237 {ECO:0000313|EMBL:OEO25464.1,
RC ECO:0000313|Proteomes:UP000095383};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) 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:OEO25464.1}.
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DR EMBL; MKEP01000008; OEO25464.1; -; Genomic_DNA.
DR RefSeq; WP_069900135.1; NZ_MKEP01000008.1.
DR AlphaFoldDB; A0A1E5XAR7; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000095383; 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: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:UniProtKB-KW.
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}.
FT DOMAIN 3..59
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 902 AA; 97999 MW; 97F0F589E8C90BCE CRC64;
MATTTTASTC CYCGVGCGVL IEHDGDTIVD VKGDPEHPAN FGKLCSKGST LHLTGDLDAR
GLYPELRLGK QLARARTSWD EALDHAASVF AETIREHGPD SVAFYVSGQL LTEDYYAFNK
LARGLIGTNN IDSNSRLCMS SAVVGYKRSL GADAPPCNYQ DIELSDCIVI AGSNMAYAHP
VLFRRLEEAK AANPDMRVIV IDPRRTDTCD LADVHVAILP GTDVALFHGI LHILMWEGWI
DRNYIEQHTD GFDALKQLVR NYTPGVVAEI CGISLEQLQQ CAQLIGKAEN FLSLWCMGLN
QSSAGTAKNS ALINLHLATG QIGKAGAGPF SLTGQPNAMG GRETGSLSNL LPGHREAANA
DDRQAVADYW GVESLPSSPG LSAIELFEQV NAGKIKALWI ACTNPAQSLP DQHNVQKALA
SCPFVVVQEA FFTTETCAFA DLLLPAASWG EKAGTVTNSE RRISHVRRAV SAPGAARPDW
AITTDFARRL EQHLRPGMPG LFEFESEEQL FEQYKQLTAG RDLDISGLTY SLLDEIGPQQ
WPFPAGAQHG TARLYSDGKF ATANGRAQFV SEAYAAPKEK RDARHSLTLN TGRLRDHWHG
MSRTGNAARL FGHVQTAALS VHPDELRRRR LQDGDLVRVS SRRGKLVVAV QGDDSVRSGQ
AYLPMHWGDR FLKGLGTNAL TLPAVDPLSR QPELKHCAIN IEKADLPWQL FALIEGNVQQ
RFSQLRPLFE SFSYANFALT GRDRPALMIS AANEQAPSSE LLAMIDQLLA VDNGPVLAYD
DPVRAVGKRV RIEQGRITSI RLAGETAARH WLKDLWNKGQ ADESLRRWLL APLSAAPGTV
SIESSKTLCN CMNISLQQVN SAIAGGADLA QLKTQLGCGT SCGSCIPEIN QLLRSHHCAL
SA
//
