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Database: UniProt/TrEMBL
Entry: F2JWD6_MARM1
LinkDB: F2JWD6_MARM1
Original site: F2JWD6_MARM1 
ID   F2JWD6_MARM1            Unreviewed;       739 AA.
AC   F2JWD6;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   20-DEC-2017, entry version 39.
DE   SubName: Full=Isocitrate dehydrogenase, NADP-dependent {ECO:0000313|EMBL:ADZ90609.1};
DE            EC=1.1.1.42 {ECO:0000313|EMBL:ADZ90609.1};
GN   OrderedLocusNames=Marme_1336 {ECO:0000313|EMBL:ADZ90609.1};
OS   Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028
OS   / MMB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Marinomonas.
OX   NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ90609.1, ECO:0000313|Proteomes:UP000001062};
RN   [1] {ECO:0000313|Proteomes:UP000001062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC   {ECO:0000313|Proteomes:UP000001062};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I.,
RA   Lucas-Elio P., Johnston A.W.B., Sanchez-Amat A., Woyke T.;
RT   "Complete sequence of Marinomonas mediterranea MMB-1.";
RL   Submitted (MAR-2011) 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; CP002583; ADZ90609.1; -; Genomic_DNA.
DR   RefSeq; WP_013660514.1; NC_015276.1.
DR   ProteinModelPortal; F2JWD6; -.
DR   STRING; 717774.Marme_1336; -.
DR   EnsemblBacteria; ADZ90609; ADZ90609; Marme_1336.
DR   KEGG; mme:Marme_1336; -.
DR   PATRIC; fig|717774.3.peg.1384; -.
DR   eggNOG; ENOG4105E9K; Bacteria.
DR   eggNOG; COG2838; LUCA.
DR   KO; K00031; -.
DR   OMA; RDSGKMW; -.
DR   OrthoDB; POG091H0B3N; -.
DR   Proteomes; UP000001062; 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   PANTHER; PTHR36999; PTHR36999; 1.
DR   Pfam; PF03971; IDH; 1.
DR   PIRSF; PIRSF009407; IDH_monmr; 1.
DR   TIGRFAMs; TIGR00178; monomer_idh; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001062};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR009407-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3};
KW   Oxidoreductase {ECO:0000313|EMBL:ADZ90609.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001062}.
FT   REGION      132    139       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR009407-2}.
FT   COILED      618    638       {ECO:0000256|SAM:Coils}.
FT   METAL       349    349       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR009407-3}.
FT   METAL       547    547       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR009407-3}.
FT   METAL       551    551       Magnesium or manganese.
FT                                {ECO:0000256|PIRSR:PIRSR009407-3}.
FT   BINDING     145    145       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR009407-2}.
FT   BINDING     546    546       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR009407-2}.
FT   SITE        254    254       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR009407-1}.
FT   SITE        419    419       Critical for catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR009407-1}.
SQ   SEQUENCE   739 AA;  82315 MW;  E7DAF5E2241CCA22 CRC64;
     MSKHTIYYTL TDEAPALATA SLLPIFQAFA KEADINLQLT DISLAARVLS LFTDRLPEDK
     QVEDGLSFLG ELTADPDANF IKLPNISASI PQLTATIKEL QSQGYEIPDY PEAPATDEEK
     EINSRYSKVL GSAVNPVLRQ GNSDRRAPAA VKGFARKHPH SMGKWQKTSQ THADYMRDGD
     FFSSEQSVTM DKAQEVRIEF VNKSGEVDVK KTLPLLEGEV LDGMRMSASK LRDFFEQSLQ
     EAKEAGIMWS LHVKATMMKV SHPIVFGHAV TVYYKEVWDK FGDLFDELGV NPNNGIGSVY
     DKIKTLPQST QDEILESIHD CYEHRPEIAM VDSVRGITNL HVPSDVIVDA SMPAMIRSSG
     KMWGRDGKTK DTKAVMPEST YARIYQEVIN FCKTNGAFDP TTMGTVPNVG LMAQKAEEYG
     SHDKTFEVQE NGTMRVRDAE GNVLMQHDVE KGDIWRACQT KDAPIKDWVK LGVTRARNSG
     TPAVFWLDAE RAHDNELRKK VKLYLQDHDL EGLEIHIMSY NEAIRFSMER MMRGQDTISV
     SGNVLRDYLT DLFPIMELGT SAKMLSIVPM LNGGGMYETG AGGSAPKHVQ QLQEENYLRW
     DSLGEFLATA VSFEELGIKQ DNAKAKVLAA ALDRATEQLL DNNKSPSRKV GDIDNRGSHF
     YLTMYWAQAL ATQTDDAELA DKFASVAKAL VENESKIVEE LNSVQGKDAG LEGYYHMDLD
     AVTKVMRPSA TFNEILAAI
//
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