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Database: UniProt/TrEMBL
Entry: F2R731_STRVP
LinkDB: F2R731_STRVP
Original site: F2R731_STRVP 
ID   F2R731_STRVP            Unreviewed;       741 AA.
AC   F2R731;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   07-JUN-2017, entry version 36.
DE   SubName: Full=Isocitrate dehydrogenase {ECO:0000313|EMBL:CCA53723.1};
DE            EC=1.1.1.42 {ECO:0000313|EMBL:CCA53723.1};
GN   OrderedLocusNames=SVEN_0436 {ECO:0000313|EMBL:CCA53723.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 /
OS   JCM 4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA53723.1, ECO:0000313|Proteomes:UP000006854};
RN   [1] {ECO:0000313|EMBL:CCA53723.1, ECO:0000313|Proteomes:UP000006854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC   PD 04745 {ECO:0000313|Proteomes:UP000006854};
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
RT   actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC       {ECO:0000256|PIRSR:PIRSR009407-3};
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DR   EMBL; FR845719; CCA53723.1; -; Genomic_DNA.
DR   RefSeq; WP_015031642.1; NC_018750.1.
DR   ProteinModelPortal; F2R731; -.
DR   EnsemblBacteria; CCA53723; CCA53723; SVEN_0436.
DR   GeneID; 28668434; -.
DR   KEGG; sve:SVEN_0436; -.
DR   PATRIC; fig|953739.5.peg.6004; -.
DR   KO; K00031; -.
DR   OMA; RDSGKMW; -.
DR   OrthoDB; POG091H0B3N; -.
DR   BioCyc; SVEN953739:G13G2-434-MONOMER; -.
DR   Proteomes; UP000006854; Chromosome.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   InterPro; IPR004436; Isocitrate_DH_NADP_mono.
DR   Pfam; PF03971; IDH; 1.
DR   PIRSF; PIRSF009407; IDH_monmr; 1.
DR   TIGRFAMs; TIGR00178; monomer_idh; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006854};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR009407-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3};
KW   Oxidoreductase {ECO:0000313|EMBL:CCA53723.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006854}.
FT   REGION      132    139       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR009407-2}.
FT   METAL       350    350       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR009407-3}.
FT   METAL       548    548       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR009407-3}.
FT   METAL       552    552       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR009407-3}.
FT   BINDING     145    145       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR009407-2}.
FT   BINDING     547    547       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR009407-2}.
FT   SITE        255    255       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR009407-1}.
FT   SITE        420    420       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR009407-1}.
SQ   SEQUENCE   741 AA;  79412 MW;  CAE97C28F40E784F CRC64;
     MTDSTIIYTH TDEAPALATY SFLPVIQAYA SQAGVTVETR DISLAGRIIA VFPEFLEEGQ
     RIPDALSELG DLAKTPGANI IKLPNVSASI PQLKAAIAEL QAQGYALPDY PDDPRTEQDK
     DVRARYDKIK GSAVNPVLRE GNSDRRAPGS VKNYAKNHPH RMGAWTPESK TNVATMSEND
     FASTEKSVVI AKDDTLRFEF TAADGTTSEL RQPLKVIAGE VVDAAVMRAA ALRTFLGEQV
     ARAKAENVLF SVHLKATMMK VSDPIVFGHV VRAFFPATFA KYGEVLAGAG LSPNDGLGTV
     LGGLDAIPHG LGAEIKASFE AELAAGPALA MVDSDKGITN LHVPSDVIVD ASMPAMIRTS
     GHMWGPDGQE ADTLAVLPDH SYSGVYQAVI DDCRAHGAFD PSTMGSVPNV GLMAQKAEEY
     GSHDKTFEMA QAGTVRLVDS EGTALLEQEV AEGDIFRACQ TKDLPIQDWV KLAVTRARAT
     GAPAVFWLDE NRAHDAQLIA KVNEYLPQHD TEGLDIRVLS PVEATKFSLE RIRRGEDTIS
     VTGNVLRDYL TDLFPILELG TSAKMLSVVP LMAGGGLFET GAGGSAPKHV QQLVKENYLR
     WDSLGEFFAL AASFEHLATS TGNSRAQVLA DTLDRATGTF LNEDKSPTRR LGGIDNRGSH
     FYLALYWAQE LAAQTEDAEL AKAFAPLAET LSTNEQKIVD ELVAVQGSPA EIGGYYQPDP
     AKAAAVMRPS ATFNEAVASL A
//
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