ID K9XR68_STAC7 Unreviewed; 756 AA.
AC K9XR68;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Nitrate reductase {ECO:0000313|EMBL:AFZ35100.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:AFZ35100.1};
GN OrderedLocusNames=Sta7437_1533 {ECO:0000313|EMBL:AFZ35100.1};
OS Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC Stanieria.
OX NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ35100.1, ECO:0000313|Proteomes:UP000010473};
RN [1] {ECO:0000313|Proteomes:UP000010473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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}.
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DR EMBL; CP003653; AFZ35100.1; -; Genomic_DNA.
DR RefSeq; WP_015192771.1; NC_019748.1.
DR AlphaFoldDB; K9XR68; -.
DR STRING; 111780.Sta7437_1533; -.
DR KEGG; scs:Sta7437_1533; -.
DR PATRIC; fig|111780.3.peg.1597; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_3; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000010473; Chromosome.
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:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
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; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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 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 PIRSF; PIRSF000144; CbbBc; 2.
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 {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,
KW ECO:0000313|EMBL:AFZ35100.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010473}.
FT DOMAIN 2..70
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 25..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 756 AA; 84135 MW; 48B40DE88D91C7BC CRC64;
MTEPTKTLCP YCGVGCGLEV LPPAQPGKAT NRDQQGNPIW QVRGDRSHPS SQGKICVKGG
TIAESLDKNR LKYPMIRESL DQPFRRASWD EALEKIVNRI QELRTTQGSD SICMYGSGQF
QTEDYYIAQK LLKGCLGTNN FDANSRLCMS SAVAGYTQSF GSDGPPCCYD DLELTDCAFL
IGTNTAECHP IVFNRLRVHH KKNRKVKMIV VDPRRTPTAE AADLHLAIKP GTDIDLLNGI
AHLLLRWGYL DTLFIDECTQ GFSQYTEVIQ HYPPEVVARK CGIRIDLLEQ AARYWGESER
VLSLWSMGVN QSSEGTAKVR TIINLHLMTG NIGKPGAGPF SLTGQPNAMG GREAGGLAHI
LPGYRVVKNP QHRAEVEQLW GLTPGSISPN PGKDAWSMIT GLETGTVGLL WIAATNPAVS
MPDLERTKQA LMRSPLTVYQ DAYYPTETSA YAHILLPAAQ WSEKTGTMTN SERVVTLCPQ
FREPPGEAKA DWEIFAEVGR RLGFTQEFNF TNSEAVYAEF VQLTRDRPCD VTGLSYQRLQ
QQGPIQWPCP LEEEGEIGRK GEAEETGIFS ALFKEKKQEK VAKRLYTDGI FNTPDGRAKF
AAFHSKGLAE PPNNEYPFVL TVGRVYEHWH TMTRTGRIEK IMKKQPQPFL EIHPRDAEQL
AIEEGMLIEI HSRRGKGIFP ARITKAIAPG TVFVPMHWGA LWAENAEANV LTHPEACPIS
LEPELKACAV KLIPVKPELQ QERSLFQQKA KESVSV
//
