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Database: UniProt
Entry: F2R8H3_STRVP
LinkDB: F2R8H3_STRVP
Original site: F2R8H3_STRVP 
ID   F2R8H3_STRVP            Unreviewed;       802 AA.
AC   F2R8H3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Assimilatory nitrate reductase large subunit {ECO:0000313|EMBL:CCA53891.1};
DE            EC=1.7.99.4 {ECO:0000313|EMBL:CCA53891.1};
GN   OrderedLocusNames=SVEN_0604 {ECO:0000313|EMBL:CCA53891.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA53891.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA53891.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA53891.1};
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
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; FR845719; CCA53891.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2R8H3; -.
DR   STRING; 953739.SVEN_0604; -.
DR   KEGG; sve:SVEN_0604; -.
DR   PATRIC; fig|953739.5.peg.788; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_4_11; -.
DR   Proteomes; UP000006854; 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; 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; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   PANTHER; PTHR43105:SF9; NITRATE REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G15190)-RELATED; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 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; 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,
KW   ECO:0000313|EMBL:CCA53891.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006854}.
FT   DOMAIN          47..103
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   802 AA;  87533 MW;  3A742378B306F272 CRC64;
     MRRNPLVLSD ERIADPWGRR TPYGRGGRWP ERTDSCLAEG VAEEDVDAWV RAASLLHSDG
     DAMDIAVRDG RIVGVRGRAG DRVNRGRLEP KDLYAWQANG SADRLTRPLI REGTRLVETD
     WPTAMGRVVA RSRELIDSQG PKSVAFYTSG QLFLEEYYTL AVLARAGIGT PHLDGNTRLC
     TATAAEALKE SFGSDGQPGS YEDIDHADAI ALFGHNIAET QVVQWMRILD RLEGDRPPRL
     LCVDPRLTPV ARRADVHLAP RLGTNVALLN ALLHEVVRRG WTDPGYIARC TVGFDALCAQ
     VEPCTPRWAA GICDVPAAAI EEAAELVGTA DRLLSTVLQG FYQANQATAA AVQVDNLHLI
     RGMLGRPGAG VLQMNGQPTA ENTRECGADG DLPGFRNWQN EDHVADLARV WNVDPSAIPH
     DAPPTHAMEI FRLAEQGAVR MLWISATNPA VSLPDLARIR AVLSREGLFT VVQDLFLTET
     AQFADVVLPA ATWGEKTGTF TNADRTVHLS EKAVEPPGEA RPDLDIFLDY AARMGFEDKD
     GGRLVHWSGP EEAFEAWKRC SAGRPCDYTG LTYAKLRGPS GIQWPCTEDA PDGTDRLYGD
     GVSWAHPDLC ETYGKDLVTG EPLGEEWYRS TNPDGKALIR AAPYVQPREW PDEEHPFQLT
     TGRTLYHFHT RTKTGRVPQL ADAAPDVWVQ IAASDASRLG LAEGDLVEVT TRTGALRGRL
     RIGSMRPGVL FLPFHYGYWD TPGGRSPAPG APGRAVNEVI PTAWDPVSKQ PQFKTAAAAL
     TLVAPAPRKP QEGGRDTARP TG
//
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