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1KHG

PEPCK

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004611molecular_functionphosphoenolpyruvate carboxykinase activity
A0004613molecular_functionphosphoenolpyruvate carboxykinase (GTP) activity
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006094biological_processgluconeogenesis
A0006107biological_processoxaloacetate metabolic process
A0006629biological_processlipid metabolic process
A0009617biological_processresponse to bacterium
A0014823biological_processresponse to activity
A0016301molecular_functionkinase activity
A0016831molecular_functioncarboxy-lyase activity
A0017076molecular_functionpurine nucleotide binding
A0018105biological_processpeptidyl-serine phosphorylation
A0019003molecular_functionGDP binding
A0019543biological_processpropionate catabolic process
A0030145molecular_functionmanganese ion binding
A0031406molecular_functioncarboxylic acid binding
A0031667biological_processresponse to nutrient levels
A0032496biological_processresponse to lipopolysaccharide
A0032868biological_processresponse to insulin
A0032869biological_processcellular response to insulin stimulus
A0033993biological_processresponse to lipid
A0042593biological_processglucose homeostasis
A0042594biological_processresponse to starvation
A0043382biological_processpositive regulation of memory T cell differentiation
A0043648biological_processdicarboxylic acid metabolic process
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046166biological_processglyceraldehyde-3-phosphate biosynthetic process
A0046327biological_processglycerol biosynthetic process from pyruvate
A0046872molecular_functionmetal ion binding
A0046889biological_processpositive regulation of lipid biosynthetic process
A0046890biological_processregulation of lipid biosynthetic process
A0051365biological_processcellular response to potassium ion starvation
A0070062cellular_componentextracellular exosome
A0070365biological_processhepatocyte differentiation
A0070741biological_processresponse to interleukin-6
A0071300biological_processcellular response to retinoic acid
A0071320biological_processcellular response to cAMP
A0071332biological_processcellular response to fructose stimulus
A0071333biological_processcellular response to glucose stimulus
A0071347biological_processcellular response to interleukin-1
A0071356biological_processcellular response to tumor necrosis factor
A0071377biological_processcellular response to glucagon stimulus
A0071456biological_processcellular response to hypoxia
A0071474biological_processcellular hyperosmotic response
A0071475biological_processcellular hyperosmotic salinity response
A0071476biological_processcellular hypotonic response
A0071477biological_processcellular hypotonic salinity response
A0071549biological_processcellular response to dexamethasone stimulus
A0072350biological_processtricarboxylic acid metabolic process
A0097403biological_processcellular response to raffinose
A0106264molecular_functionprotein serine kinase activity (using GTP as donor)
A1904628biological_processcellular response to phorbol 13-acetate 12-myristate
A1904640biological_processresponse to methionine
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A 701
ChainResidue
ALYS244
AHIS264
AASP311

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 702
ChainResidue
AALA447
ATRP450
APRO509
AILE511

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 703
ChainResidue
AVAL368
AILE373
AGLU375
AHOH738
ATYR72
AGLN352

Functional Information from PROSITE/UniProt
site_idPS00505
Number of Residues9
DetailsPEPCK_GTP Phosphoenolpyruvate carboxykinase (GTP) signature. FPSACGKTN
ChainResidueDetails
APHE284-ASN292

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:11851336, ECO:0000305|PubMed:32322062
ChainResidueDetails
ACYS288

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:11851336, ECO:0000269|PubMed:14552798, ECO:0000269|PubMed:17532214
ChainResidueDetails
ATYR235
ALYS244
AHIS264
AASP311
AASN403
APHE530
AARG87

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P07379
ChainResidueDetails
ASER286

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:11851336
ChainResidueDetails
AARG436
AALA287
AARG405

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER19

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: N6-acetyllysine; by p300/EP300 => ECO:0000269|PubMed:20167786, ECO:0000269|PubMed:21726808
ChainResidueDetails
ALYS71
ALYS594
ALYS70

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKB/AKT1 => ECO:0000269|PubMed:32322062
ChainResidueDetails
ASER90

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; by p300/EP300 => ECO:0000269|PubMed:30193097
ChainResidueDetails
ALYS91

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Z2V4
ChainResidueDetails
ASER118

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q16822
ChainResidueDetails
ATHR178

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q16822
ChainResidueDetails
ASER286

site_idSWS_FT_FI12
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07379
ChainResidueDetails
ALYS521
ALYS524
ALYS473

Catalytic Information from CSA
site_idMCSA1
Number of Residues8
DetailsM-CSA 863
ChainResidueDetails
AARG87electrostatic stabiliser, enhance reactivity
ATYR235electrostatic stabiliser, steric role
ALYS244metal ligand
AHIS264metal ligand
ASER286electrostatic stabiliser
ACYS288metal ligand
AASP311metal ligand
AARG405electrostatic stabiliser, enhance reactivity

221051

PDB entries from 2024-06-12

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