NARB_SYNY3
ID NARB_SYNY3 Reviewed; 714 AA.
AC P73448;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Nitrate reductase;
DE EC=1.7.5.1;
GN Name=narB; OrderedLocusNames=sll1454;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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 -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily. {ECO:0000305}.
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DR EMBL; BA000022; BAA17488.1; -; Genomic_DNA.
DR PIR; S77385; S77385.
DR AlphaFoldDB; P73448; -.
DR SMR; P73448; -.
DR IntAct; P73448; 7.
DR STRING; 1148.1652567; -.
DR PaxDb; P73448; -.
DR EnsemblBacteria; BAA17488; BAA17488; BAA17488.
DR KEGG; syn:sll1454; -.
DR eggNOG; COG0243; Bacteria.
DR InParanoid; P73448; -.
DR OMA; DGPPCCY; -.
DR PhylomeDB; P73448; -.
DR UniPathway; UPA00652; UER00706.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
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; IBA:GO_Central.
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; 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.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Nitrate assimilation;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..714
FT /note="Nitrate reductase"
FT /id="PRO_0000063238"
FT DOMAIN 7..70
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
SQ SEQUENCE 714 AA; 79632 MW; 702AA57ED9E605AA CRC64;
MDSPAILPTT RTLCPYCGVG CGLEAVASPQ KSVVDAGHAH KIRGDRQHPS SQGMVCVKGA
TVMESMDKQR LLYPMFRSSL DQPWQQISWE AALEIVVDKI QQVKQTLGVS GLCMYASGQM
QTEDYYVAQK LFKGCLGTNN FDTNSRLCMS SAVSAYSLSF GSDGPPCCYE DLEITDCAFL
IGTNTADCHP IIFNRLRKHH KQNPHVKLIV VDPRCTATAE VADLHLAINP GSDITLLHGI
AYLLKKWNLI DQKFIDNHTQ DFEQYCQVID HYPPEKVTQI CGISLEQLET AAHYWGNAKT
VLSLWSMGMN QSFQGTAKGR CLINLHLLTG QIGKPGSGPF SLTGQPNAMG GREAGGLSHL
LPGYRSIKNP QHRQEVEQLW QISPGRINPE PGLSAWEMFM GLENQQVGFL WIVATNPVVS
MPDLERVKKA LQQSTFTIHQ DAYSPTETAE YAHLLLPAAQ WSEKTGTMTN SERRVTLSPA
FRSPPGEARP DWEIFAEVGR RLGFENQFNF VDSAAVHREY VQLTAERLCD QSGVSYEKLQ
KLGPLQWPCR QSDQESQLLS TKRLYTDYKF CTENGRANFC LDHSRGLAEP VDPNYPFVLT
NGRLYGHWHT QTRTGHIEKI KKMHPKPILE MHPKDAEKLG IKSQDLVAIK SRRGSAQLEV
LVTRAIAPGT VFMPMHWGFL WDDNAEVNSL THATACPISK QPELKACAVN ITPV
