ID NARB_SHEFN Reviewed; 938 AA.
AC O33732; Q084F9;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Nitrate reductase;
DE EC=1.7.5.1;
GN OrderedLocusNames=Sfri_1505;
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-397.
RX PubMed=10861223; DOI=10.1042/0264-6021:3490153;
RA Gordon E.H.J., Pike A.D., Hill A.E., Cuthbertson P.M., Chapman S.K.,
RA Reid G.A.;
RT "Identification and characterization of a novel cytochrome c3 from
RT Shewanella frigidimarina that is involved in Fe(III) respiration.";
RL Biochem. J. 349:153-158(2000).
CC -!- FUNCTION: Nitrate reductase is a key enzyme involved in the first step
CC of nitrate assimilation in plants, fungi and bacteria.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + nitrate = a quinone + H2O + nitrite;
CC Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301,
CC ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily. {ECO:0000305}.
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DR EMBL; CP000447; ABI71356.1; -; Genomic_DNA.
DR EMBL; AJ000006; CAA03851.1; -; Genomic_DNA.
DR RefSeq; WP_011636976.1; NC_008345.1.
DR AlphaFoldDB; O33732; -.
DR SMR; O33732; -.
DR STRING; 318167.Sfri_1505; -.
DR KEGG; sfr:Sfri_1505; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_6; -.
DR OrthoDB; 9810782at2; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000000684; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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-UniPathway.
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; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
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 PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 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.
PE 3: Inferred from homology;
KW 4Fe-4S; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW Nitrate assimilation; Oxidoreductase; Reference proteome.
FT CHAIN 1..938
FT /note="Nitrate reductase"
FT /id="PRO_0000063236"
FT DOMAIN 1..64
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 8
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 11
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
SQ SEQUENCE 938 AA; 101087 MW; C8951CAC0306A663 CRC64;
MSVVQSSCAY CGVGCGVSVS SNKPNWTDVD AADLILVGDN KHPANYGHLC AKGERLLDSL
AQPNVLRYPK LRSGMPLDWD KASTLIADTF AKTIAEHGPD SVALYLSGQL LTEDYYVANK
FAKGFLKTAN VDTNSRLCMS SAVSAMQRAF GEDVVPGCYD DLEQADVIVL VGANTAWTHP
VLFQRILAAI KANNAQLVVI DPLSTATAKQ ADLHLAIKPG ADLTLFHGLL GYLADQNRVD
HAYIAAHTEG FDTVVLQAQQ LSANLADLAT QVGVSVTQLT QFYQLVANNK KVLTASCQGV
NQSTIGTDAT NAMINCHLAL GHIGQAGCGF FSLTGQPNAM GGREVGGLAT QLACHMGFSQ
PEQQLLADFW KVDSIADQKG LVAVEMFDAL AEGKIKAIWI MGTNPVVSLP NSEKIAQALA
DCPFVVVSEI SPDSDTAKLA DVLLPAQGWS EKCGTVTNSE RTITRQRGFI TAKGQAKPDW
WAVSQVAKKM GFDGFEFDDN ASIFSEFAAL SAKVKQVFPT KVFDLTGLTE LSKAQYDALA
PTQWPIASAT QIGQQNVRVF GLGEFATATG KAQFVTPAVV SVPQQSLPSN TLLLNTGRSR
DQWHTMTRTG HIASLRASIP EPVVHLHSSQ LSALSLTEGG LVRIEAIQNQ IEQYSTETAN
PDLFTHASFT MARAVVDDDI PTNMALMSMH WSAQFSLTKG VNQALDARVD PISKQPGFKC
QPVTLTPVEL ALQGVVFGQH YSSAHGLCWQ VAQTLENGVC HHIGFTDTDD GFAYQATVHS
LKWTLTVVGQ PLYIQCNMDK GLLKALKVLS HTQVNVALYQ MNDFIGKPVD KQLIKQLHQQ
IKAGNSPLIC ACTGVTEANI NDEINQQFND QVMSDGLANI SFEQALDSTQ LLLGCGRQCG
SCHSEVKQCA KQSWKDALSY CESYSDIDHQ PSVAEDVA
//
