(data stored in SCRATCH zone)

SWISSPROT: Q9EWF3_STRCO

ID   Q9EWF3_STRCO            Unreviewed;      1227 AA.
AC   Q9EWF3;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   08-MAY-2019, entry version 109.
DE   SubName: Full=Nitrate reductase alpha chain NarG3 {ECO:0000313|EMBL:CAD30933.1};
GN   OrderedLocusNames=SCO4947 {ECO:0000313|EMBL:CAD30933.1};
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226 {ECO:0000313|Proteomes:UP000001973};
RN   [1] {ECO:0000313|EMBL:CAD30933.1, ECO:0000313|Proteomes:UP000001973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145
RC   {ECO:0000313|Proteomes:UP000001973};
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.H., Kieser T., Larke L., Murphy L., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539;
CC         Evidence={ECO:0000256|SAAS:SAAS00648551};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|SAAS:SAAS00607242};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|SAAS:SAAS01108232}.
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DR   EMBL; AL939122; CAD30933.1; -; Genomic_DNA.
DR   RefSeq; NP_629099.1; NC_003888.3.
DR   RefSeq; WP_011029968.1; NC_003888.3.
DR   STRING; 100226.SCO4947; -.
DR   EnsemblBacteria; CAD30933; CAD30933; CAD30933.
DR   GeneID; 1100388; -.
DR   KEGG; sco:SCO4947; -.
DR   PATRIC; fig|100226.15.peg.5027; -.
DR   eggNOG; COG5013; LUCA.
DR   HOGENOM; HOG000237341; -.
DR   InParanoid; Q9EWF3; -.
DR   KO; K00370; -.
DR   OMA; RERWAHD; -.
DR   PhylomeDB; Q9EWF3; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
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:InterPro.
DR   GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR   GO; GO:0042126; P:nitrate metabolic process; IEA:InterPro.
DR   CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-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   InterPro; IPR006468; NarG.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   TIGRFAMs; TIGR01580; narG; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9EWF3.
DR   SWISS-2DPAGE; Q9EWF3.
KW   4Fe-4S {ECO:0000256|SAAS:SAAS00418020};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001973};
KW   Iron {ECO:0000256|SAAS:SAAS00454562};
KW   Iron-sulfur {ECO:0000256|SAAS:SAAS00454505};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00077323};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS01133048};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001973}.
FT   DOMAIN       46    110       4Fe-4S Mo/W bis-MGD-type.
FT                                {ECO:0000259|PROSITE:PS51669}.
SQ   SEQUENCE   1227 AA;  135064 MW;  68FE936C17D4DB6F CRC64;
     MADAADRLLK AGQLLRRSPT TLDLRAVYRT DQNVNDRPYR ERWAHDKVVR STHGVNCTGS
     CSWKVYVKDG LITWETQQTD YPSVGPDRPE YEPRGCPRGA SFSWYTYSPT RVRHPLARGV
     LVEMYRDAKR RHGGDPVAAW AELTSDPEKR RRYQSARGRG GFVRVDWDEA LEIAAAAQVH
     TIAEYGPDRV AGFSPIPAMS MASHAVGARY HSLIGAPMIS FYDWYADLPI ASPQVFGDQT
     DVPESGDWWD AAYLMLWGSN VPVTRTPDAH WMAEARYRGQ KVVVVSPDYA DATKFADEWL
     HPHPGTDGAL AMAMGHVLLT EFFVRRQVPY FTDYVKRFTD LPFLVALDEH AAGRWTPGKF
     VTAADLGLGR HADAGARAWM PVLIDADTDD VVVPNGTLGD RWGKGGEGRW NLDLGGTDPL
     LTLHGHTGGR GDNGVEVVLP RFDEPGATVV RGVPAREIGG RLVTTVYDLL LAQYAVARPG
     LAGHWPTGYD DAEQPCTPAW QERLTSVPAE AAVRAAREFA RTAEQTRGRC MIVMGAGTNH
     WFHSDTIYRS FLSLLILTGC QGVNGGGWAH YVGQEKVRPY TGWQQLSTAA DWVRPSRQMA
     GTPYWYLHTG QWRYESHAAD ALASPTAPGT LAGLHTADLV AQSARLGWMP SYPTFDANPL
     DLGRRARESG QEPGDWIAEQ LGSGAVDFAC EDPDAPRNWP RVLTVWRANL IGSSAKGNEY
     FLRHLLGARD GATSSEAPPE HRPRSVAWRD DAPEGKLDLL LSLDFRMTST TLFSDLVLPA
     ATWYEKHDLS STDMHPFVHA FSPAINPPWQ ARTDFEIFHS LARRLSELAA GRLGTAHDLV
     ATALQHDTPG ETAQPGGRVT DWRDGRTPIE PGRNAPQVSL VERDYTAVAD RLAAFGPLAE
     EHGMTVKGVT VNPHEESRWL AARCGTAPAG PARGRPLLDT DVKFCEAILA LSGTTNGRLA
     AEGFDRLADR VGPGAGLAEL AASVGERRVV FSDTQERPVQ VGASFEWSGK EAPDRRYSPF
     TVNTEHKKPW HTLTGRQHFY VDHDWMAELG EQLPVYRPPL NLAELGDAPI PTGDGRAVTV
     RYLTPHAKWS IHSEYQENLL MQTLARGGPV VWMSPADADA IGAADNDWVE AVNAHGVVVA
     RAIVSHRVPD GTVLMYHVQE RLVNVPKSEA NGRRGGVHNS LTKLLVKPTH LIGGYGQLSF
     APNYYGPTGN QRDAVTTIRR RSQEVTY
//

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