NARB_SYNE7
ID NARB_SYNE7 Reviewed; 729 AA.
AC P39458; Q31NV4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Nitrate reductase;
DE EC=1.7.5.1;
GN Name=narB; OrderedLocusNames=Synpcc7942_1235;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Andriesse A.J., Bakker H.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX PubMed=8437564; DOI=10.1007/bf00277112;
RA Omata T., Andriesse X., Hirano A.;
RT "Identification and characterization of a gene cluster involved in nitrate
RT transport in the cyanobacterium Synechococcus sp. PCC7942.";
RL Mol. Gen. Genet. 236:193-202(1993).
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 (denitrification);
CC dinitrogen from nitrate: step 1/4.
CC -!- INTERACTION:
CC P39458; P00221: PETF; Xeno; NbExp=2; IntAct=EBI-932578, EBI-864933;
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily. {ECO:0000305}.
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DR EMBL; X74597; CAA52675.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57265.1; -; Genomic_DNA.
DR EMBL; X61625; CAA43813.1; -; Genomic_DNA.
DR PIR; S36605; S36605.
DR RefSeq; WP_011377931.1; NC_007604.1.
DR AlphaFoldDB; P39458; -.
DR SMR; P39458; -.
DR IntAct; P39458; 2.
DR STRING; 1140.Synpcc7942_1235; -.
DR PRIDE; P39458; -.
DR EnsemblBacteria; ABB57265; ABB57265; Synpcc7942_1235.
DR KEGG; syf:Synpcc7942_1235; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_3; -.
DR OMA; DGPPCCY; -.
DR OrthoDB; 323168at2; -.
DR BioCyc; MetaCyc:MON-13441; -.
DR BioCyc; SYNEL:SYNPCC7942_1235-MON; -.
DR BRENDA; 1.7.7.2; 6187.
DR UniPathway; UPA00652; UER00706.
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:0019333; P:denitrification pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR InterPro; IPR009010; Asp_de-COase-like_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 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; SSF50692; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Nitrate assimilation;
KW Oxidoreductase.
FT CHAIN 1..729
FT /note="Nitrate reductase"
FT /id="PRO_0000063237"
FT DOMAIN 16..84
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 23
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 26
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 30
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT CONFLICT 615..616
FT /note="GH -> PD (in Ref. 1; CAA52675)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 729 AA; 79854 MW; 455798C8631755A6 CRC64;
MFDLSKFLPV ITPLMIDTAK TLCPYCGVGC GLEAVPPAQP GRATVRDREG TPIWQIRGDR
QHPSSQGMVC VKGATVAESV SKSRLKYPMF RASLDDPFTE ISWDEALDRL CDRIQQTQAD
YGKDGICFYG SGQFQTEDYY IAQKLVKGCL GTNNFDTNSR LCMSSAVSAY SLCLGSDGPP
ACYEDLDLAD CLLIVGSNTA ECHPILFNRY RKRHKQGGTN LIVVDPRCTP TAEVADLHLA
LKPGSDVALL NGLGWLLYQM GYVKKDFIAN QTEGFEDWLA IIEDYPPQRT AELTGLAVAE
LVRAADLIAS AQRWLSLWSM GVNQSIQGTA KATSLINLHL LTRQIGLPGC GPFSLTGQPN
AMGGRETGGL AHLLPGYRKV IDPQHRADVE TIWGLPMGSI SPQPGRTAWQ MIEGLEQGAV
GFLWVAATNP AVSLPDVKRA QAALKRSPFT VLQDAYHPTE TTTYAHLLLP AAQWSEKTGT
MTNSERRVTL CQAFRQPPGE ARADWQIFAE VGRRLGFAFD YTDAAAVFAE YVQVTAGRLC
DLSGLSHELL AQAGPQQWPF PAGAEPTTES KRLYTKHHFA YADGRARFQP FHHLGVAEPP
DDRYPLVLTV GRLYGHWHTQ TRTGRIDKIN KLHPSAFVEI HPRDADRYNI SEGQAVVIRS
RRGEGCFPAK VTTAISPGVL FVPMHWGALW GDRTEANALT HPAACPISGE PELKACAVQI
EAASSTFTI
