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Isocitrate dehydrogenase kinase/phosphatase (IDH kinase/phosphatase) (IDHK/P) (EC 2.7.11.5) (EC 3.1.3.-)

 F4ANK5_GLAS4            Unreviewed;       570 AA.
F4ANK5;
28-JUN-2011, integrated into UniProtKB/TrEMBL.
28-JUN-2011, sequence version 1.
27-SEP-2017, entry version 39.
RecName: Full=Isocitrate dehydrogenase kinase/phosphatase {ECO:0000256|HAMAP-Rule:MF_00747, ECO:0000256|SAAS:SAAS00370253};
Short=IDH kinase/phosphatase {ECO:0000256|HAMAP-Rule:MF_00747};
Short=IDHK/P {ECO:0000256|HAMAP-Rule:MF_00747};
EC=2.7.11.5 {ECO:0000256|HAMAP-Rule:MF_00747, ECO:0000256|SAAS:SAAS00370260};
EC=3.1.3.- {ECO:0000256|HAMAP-Rule:MF_00747, ECO:0000256|SAAS:SAAS00370257};
Name=aceK {ECO:0000256|HAMAP-Rule:MF_00747};
OrderedLocusNames=Glaag_0763 {ECO:0000313|EMBL:AEE21726.1};
Glaciecola sp. (strain 4H-3-7+YE-5).
Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
Alteromonadaceae; Glaciecola.
NCBI_TaxID=983545 {ECO:0000313|EMBL:AEE21726.1, ECO:0000313|Proteomes:UP000006544};
[1] {ECO:0000313|EMBL:AEE21726.1, ECO:0000313|Proteomes:UP000006544}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=4H-3-7+YE-5 {ECO:0000313|EMBL:AEE21726.1,
ECO:0000313|Proteomes:UP000006544};
PubMed=21705587; DOI=10.1128/JB.05468-11;
US DOE Joint Genome Institute;
Klippel B., Lochner A., Bruce D.C., Davenport K.W., Detter C.,
Goodwin L.A., Han J., Han S., Land M.L., Mikhailova N., Nolan M.,
Pennacchio L., Pitluck S., Tapia R., Woyke T., Wiebusch S., Basner A.,
Abe F., Horikoshi K., Keller M., Antranikian G.;
"Complete genome sequence of the marine, cellulose and xylan degrading
bacterium Glaciecola sp. 4H-3-7+YE-5.";
J. Bacteriol. 193:4547-4548(2011).
[2]
NUCLEOTIDE SEQUENCE.
STRAIN=4H-3-7+YE-5;
US DOE Joint Genome Institute;
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I.,
Piela B., Lochner A., Antranikian F.I., Woyke T.;
"Complete sequence of chromosome of Glaciecola sp. 4H-3-7+YE-5.";
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Bifunctional enzyme which can phosphorylate or
dephosphorylate isocitrate dehydrogenase (IDH) on a specific
serine residue. This is a regulatory mechanism which enables
bacteria to bypass the Krebs cycle via the glyoxylate shunt in
response to the source of carbon. When bacteria are grown on
glucose, IDH is fully active and unphosphorylated, but when grown
on acetate or ethanol, the activity of IDH declines drastically
concomitant with its phosphorylation. {ECO:0000256|HAMAP-
Rule:MF_00747, ECO:0000256|SAAS:SAAS00370251}.
-!- CATALYTIC ACTIVITY: ATP + [isocitrate dehydrogenase (NADP(+))] =
ADP + [isocitrate dehydrogenase (NADP(+))] phosphate.
{ECO:0000256|HAMAP-Rule:MF_00747, ECO:0000256|SAAS:SAAS00370256}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00747,
ECO:0000256|SAAS:SAAS00370243}.
-!- SIMILARITY: Belongs to the AceK family. {ECO:0000256|HAMAP-
Rule:MF_00747, ECO:0000256|SAAS:SAAS00561021}.
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EMBL; CP002526; AEE21726.1; -; Genomic_DNA.
STRING; 983545.Glaag_0763; -.
EnsemblBacteria; AEE21726; AEE21726; Glaag_0763.
KEGG; gag:Glaag_0763; -.
eggNOG; ENOG4105VS7; Bacteria.
eggNOG; COG4579; LUCA.
KO; K00906; -.
OrthoDB; POG091H04UC; -.
Proteomes; UP000006544; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008772; F:[isocitrate dehydrogenase (NADP+)] kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0101014; F:[isocitrate dehydrogenase (NADP+)] phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniRule.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
HAMAP; MF_00747; AceK; 1.
InterPro; IPR010452; Isocitrate_DH_AceK.
Pfam; PF06315; AceK; 1.
PIRSF; PIRSF000719; AceK; 1.
ProDom; PD043552; Isocitrate_DH_AceK; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00747,
ECO:0000256|SAAS:SAAS00447836};
Complete proteome {ECO:0000313|Proteomes:UP000006544};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00747,
ECO:0000256|SAAS:SAAS00063073};
Glyoxylate bypass {ECO:0000256|HAMAP-Rule:MF_00747,
ECO:0000256|SAAS:SAAS00063062};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_00747,
ECO:0000256|SAAS:SAAS00063057};
Kinase {ECO:0000256|HAMAP-Rule:MF_00747,
ECO:0000256|SAAS:SAAS00063059};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00747,
ECO:0000256|SAAS:SAAS00447836};
Protein phosphatase {ECO:0000256|HAMAP-Rule:MF_00747,
ECO:0000256|SAAS:SAAS00063057};
Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_00747,
ECO:0000256|SAAS:SAAS00063059};
Transferase {ECO:0000256|HAMAP-Rule:MF_00747,
ECO:0000256|SAAS:SAAS00063059};
Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00747,
ECO:0000256|SAAS:SAAS00063085}.
NP_BIND 317 323 ATP. {ECO:0000256|HAMAP-Rule:MF_00747}.
ACT_SITE 373 373 {ECO:0000256|HAMAP-Rule:MF_00747}.
BINDING 338 338 ATP. {ECO:0000256|HAMAP-Rule:MF_00747}.
SEQUENCE 570 AA; 66532 MW; 2A2E031F60FD5D5F CRC64;
MLNKVAFLIL HGFDKSYRRH SRITRDAQQR FEQAKWQETQ KAMKERIAIY ERTLADAVGE
IYQQVFPHQE NDQFWLDLKI RYQKILSDHP QYELAETFYN SVIGRIFKHQ QINDDMMFIM
PTRCYLAGLQ RHLVVHSFDT SGTVRKMLED IFNRYHFDIA FQDIQRDLKH LDGALRARLN
TAQLASVHTV EMLKPVFYRS KSAYIIGRIC MPDETLPFVI PLSIYSTNTS DESNQIVVEA
LLTERQDLSV IFSFARSYFM ADTQHPAEVV AFLHELLPHK KKFELYIALG LYKHGKTVFY
RNFLAHIEDS SDQFAIAPGI RGLVMAVFHL PSYGVVFKII KDEFPESKKI TRQHVKDCYK
LVKMTDRVGR MADTHEYVNF RLPRHRVEQA LIDELLETCA SSVELTDDEV IIKHLYIERK
MTPLNIFLAQ QEDPKLITNA LNDLGLCIKQ IAAAHIFAGD MLHKNFGITR GGRVIFYDYD
EICYLTEREF RALPKSNDPY AIDTLSVGPT DVFPEQFEHF IVGKKHLKQE LKALHGEIMT
AEYWQHMQAQ SLKGDVPDFI PYDQTKRFVN


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