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1TUU

Acetate Kinase crystallized with ATPgS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006082biological_processorganic acid metabolic process
A0006083biological_processacetate metabolic process
A0006085biological_processacetyl-CoA biosynthetic process
A0008776molecular_functionacetate kinase activity
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0016774molecular_functionphosphotransferase activity, carboxyl group as acceptor
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006082biological_processorganic acid metabolic process
B0006083biological_processacetate metabolic process
B0006085biological_processacetyl-CoA biosynthetic process
B0008776molecular_functionacetate kinase activity
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0016774molecular_functionphosphotransferase activity, carboxyl group as acceptor
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 400
ChainResidue
AARG91
AHIS123
AHIS180
AGLY212
AARG241
AHOH418

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NH4 B 2852
ChainResidue
BPIS2854

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ADP A 401
ChainResidue
AASN211
AASP283
APHE284
AARG285
AGLY331
AILE332
AASN335
AHOH411
ALYS14
AGLY210

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE AMP B 2853
ChainResidue
BGLY210
BASP283
BPHE284
BARG285
BGLY331
BILE332
BASN335
BSER336
BARG362
BPIS2854

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PIS B 2854
ChainResidue
BHIS180
BASN211
BGLY212
BMET228
BARG241
BNH42852
BAMP2853

Functional Information from PROSITE/UniProt
site_idPS01075
Number of Residues12
DetailsACETATE_KINASE_1 Acetate and butyrate kinases family signature 1. VLvINaGSSSlK
ChainResidueDetails
AVAL3-LYS14

site_idPS01076
Number of Residues18
DetailsACETATE_KINASE_2 Acetate and butyrate kinases family signature 2. IItcHlGnGsSItAvegG
ChainResidueDetails
AILE204-GLY221

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00020","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11133963","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15647264","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1g99
ChainResidueDetails
AGLY212
ASER10
AASP148
AARG91
AARG241

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1g99
ChainResidueDetails
BGLY212
BSER10
BASP148
BARG91
BARG241

site_idMCSA1
Number of Residues5
DetailsM-CSA 643
ChainResidueDetails
AASN7metal ligand
AARG91electrostatic stabiliser, polar interaction
AHIS180electrostatic stabiliser, polar interaction
AARG241electrostatic stabiliser, polar interaction
AGLU384metal ligand

site_idMCSA2
Number of Residues5
DetailsM-CSA 643
ChainResidueDetails
BASN7metal ligand
BARG91electrostatic stabiliser, polar interaction
BHIS180electrostatic stabiliser, polar interaction
BARG241electrostatic stabiliser, polar interaction
BGLU384metal ligand

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PDB entries from 2025-12-24

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