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Database: UniProt/TrEMBL
Entry: B4VD25_9ACTN
LinkDB: B4VD25_9ACTN
Original site: B4VD25_9ACTN 
ID   B4VD25_9ACTN            Unreviewed;       739 AA.
AC   B4VD25;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   SubName: Full=Isocitrate dehydrogenase {ECO:0000313|EMBL:EDX25862.1};
DE            EC=1.1.1.42 {ECO:0000313|EMBL:AKL65164.1};
GN   ORFNames=M444_06935 {ECO:0000313|EMBL:AKL65164.1}, SSAG_05549
GN   {ECO:0000313|EMBL:EDX25862.1};
OS   Streptomyces sp. Mg1.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=465541 {ECO:0000313|EMBL:EDX25862.1, ECO:0000313|Proteomes:UP000005764};
RN   [1] {ECO:0000313|EMBL:EDX25862.1, ECO:0000313|Proteomes:UP000005764}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mg1 {ECO:0000313|EMBL:EDX25862.1,
RC   ECO:0000313|Proteomes:UP000005764};
RG   The Broad Institute Genome Sequencing Platform;
RA   Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A.,
RA   Heiman D., Hepburn T., Sykes S., Mehta T., Alvarado L., Kodira C.D.,
RA   Straight P., Clardy J., Hung D., Kolter R., Mekalanos J., Walker S.,
RA   Walsh C.T., Lander E., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. Mg1.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKL65164.1, ECO:0000313|Proteomes:UP000035653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mg1 {ECO:0000313|EMBL:AKL65164.1,
RC   ECO:0000313|Proteomes:UP000035653};
RX   PubMed=23908282;
RA   Hoefler B.C., Konganti K., Straight P.D.;
RT   "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using
RT   PacBio Single-Molecule Sequencing.";
RL   Genome Announc. 1:e00535-13(2013).
RN   [3] {ECO:0000313|EMBL:AKL65164.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mg1 {ECO:0000313|EMBL:AKL65164.1};
RA   Hoefler B.C., Straight P.D.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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; CP011664; AKL65164.1; -; Genomic_DNA.
DR   EMBL; DS570434; EDX25862.1; -; Genomic_DNA.
DR   RefSeq; WP_008742879.1; NZ_DS570434.1.
DR   STRING; 465541.SSAG_05549; -.
DR   EnsemblBacteria; AKL65164; AKL65164; M444_06935.
DR   EnsemblBacteria; EDX25862; EDX25862; SSAG_05549.
DR   KEGG; strm:M444_06935; -.
DR   PATRIC; fig|465541.12.peg.1582; -.
DR   eggNOG; ENOG4105E9K; Bacteria.
DR   eggNOG; COG2838; LUCA.
DR   KO; K00031; -.
DR   OrthoDB; POG091H0B3N; -.
DR   Proteomes; UP000005764; Unassembled WGS sequence.
DR   Proteomes; UP000035653; 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:UP000005764,
KW   ECO:0000313|Proteomes:UP000035653};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR009407-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3};
KW   Oxidoreductase {ECO:0000313|EMBL:AKL65164.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035653}.
FT   REGION      132    139       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR009407-2}.
FT   METAL       348    348       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR009407-3}.
FT   METAL       546    546       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR009407-3}.
FT   METAL       550    550       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR009407-3}.
FT   BINDING     145    145       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR009407-2}.
FT   BINDING     545    545       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR009407-2}.
FT   SITE        255    255       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR009407-1}.
FT   SITE        418    418       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR009407-1}.
SQ   SEQUENCE   739 AA;  78828 MW;  94E3FAC4E1384852 CRC64;
     MTDSTIIYTH TDEAPALATY SFLPVIQAYA STAGVNVETR DISLAGRIIA SFPEHLEEGQ
     RIADALAELG ELAKTPEANI IKLPNISASI PQLKAAIAEL QGQGYALPNY PDDPKTDEER
     ETRARYDKVK GSAVNPVLRE GNSDRRAPAS VKNYAKAHPH RMGAWTPESK TNVATMGEND
     FRSTEKSAVI SEAGTLRIEH VAADGATTVL RDSVPVLAGE VVDASVLHVD ALRTFLNAQI
     ERAKAEDVLF SVHLKATMMK VSDPIVFGHV VRAFFPKTFA RYGETLAAAG LSPNDGLGTI
     LNGLGALPDA DAIKASFDAE IAEGPALAMV DSDKGITNLH VPSDVIVDAS MPAMIRTSGH
     MWGPDGNEAD TLAVLPDSSY AGVYQAVIDD CRAHGAFDPA TMGSVPNVGL MAQKAEEYGS
     HDKTFEIAAA GTVRLVDAEG NTVLEQEVAA GDIFRACQTK DAPIQDWVKL AVTRARATGV
     PAVFWLDEGR AHDAQLIAKV KTYLADHDTE GLTIEILSPV KATAYSLERI RRGEDTISVT
     GNVLRDYLTD LFPILELGTS AKMLSVVPLM NGGGLFETGA GGSAPKHVQQ LVKENYLRWD
     SLGEFLALAV SFEHLATTTG NARAQVLADT LDRATGTFLN EDKSPSRKLG GIDNRGSHFY
     LALYWAQELA RQTDAPKLAA AFDPLAKTLA ESEDKIVAEL IAVQGSPAEI GGYYQPDAAK
     AAAIMRPSAT FNQAIASLA
//
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