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Acetate kinase (EC 2.7.2.1) (Acetokinase)

 ACKA_MYCCT              Reviewed;         393 AA.
Q49113; Q2SSP6;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-JUN-2017, entry version 107.
RecName: Full=Acetate kinase {ECO:0000255|HAMAP-Rule:MF_00020};
EC=2.7.2.1 {ECO:0000255|HAMAP-Rule:MF_00020};
AltName: Full=Acetokinase {ECO:0000255|HAMAP-Rule:MF_00020};
Name=ackA {ECO:0000255|HAMAP-Rule:MF_00020}; Synonyms=ack;
OrderedLocusNames=MCAP_0230;
Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC
27343 / NCTC 10154).
Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
NCBI_TaxID=340047;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8844861; DOI=10.1002/pro.5560050825;
Zhu P.P., Peterkofsky A.;
"Sequence and organization of genes encoding enzymes involved in
pyruvate metabolism in Mycoplasma capricolum.";
Protein Sci. 5:1719-1736(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=California kid / ATCC 27343 / NCTC 10154;
Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C.,
Nierman W.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate
and ATP. Can also catalyze the reverse reaction.
{ECO:0000255|HAMAP-Rule:MF_00020}.
-!- CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate.
{ECO:0000255|HAMAP-Rule:MF_00020}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_00020};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000255|HAMAP-Rule:MF_00020};
Note=Mg(2+). Can also accept Mn(2+). {ECO:0000255|HAMAP-
Rule:MF_00020};
-!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA
biosynthesis; acetyl-CoA from acetate: step 1/2.
{ECO:0000255|HAMAP-Rule:MF_00020}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00020}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}.
-!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP-
Rule:MF_00020}.
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EMBL; U62057; AAC44347.1; -; Genomic_DNA.
EMBL; CP000123; ABC01230.1; -; Genomic_DNA.
RefSeq; WP_011387118.1; NC_007633.1.
ProteinModelPortal; Q49113; -.
SMR; Q49113; -.
EnsemblBacteria; ABC01230; ABC01230; MCAP_0230.
GeneID; 23778817; -.
KEGG; mcp:MCAP_0230; -.
HOGENOM; HOG000288398; -.
KO; K00925; -.
OMA; WKALTGT; -.
OrthoDB; POG091H02K4; -.
UniPathway; UPA00340; UER00458.
Proteomes; UP000001928; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006082; P:organic acid metabolic process; IEA:InterPro.
HAMAP; MF_00020; Acetate_kinase; 1.
InterPro; IPR004372; Ac/propionate_kinase.
InterPro; IPR000890; Aliphatic_acid_kin_short-chain.
InterPro; IPR023865; Aliphatic_acid_kinase_CS.
PANTHER; PTHR21060; PTHR21060; 1.
Pfam; PF00871; Acetate_kinase; 1.
PIRSF; PIRSF000722; Acetate_prop_kin; 1.
PRINTS; PR00471; ACETATEKNASE.
TIGRFAMs; TIGR00016; ackA; 1.
PROSITE; PS01075; ACETATE_KINASE_1; 1.
PROSITE; PS01076; ACETATE_KINASE_2; 1.
3: Inferred from homology;
ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium;
Metal-binding; Nucleotide-binding; Transferase.
CHAIN 1 393 Acetate kinase.
/FTId=PRO_0000107584.
NP_BIND 203 207 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
NP_BIND 278 280 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
NP_BIND 326 330 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
ACT_SITE 143 143 Proton donor/acceptor.
{ECO:0000255|HAMAP-Rule:MF_00020}.
METAL 6 6 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_00020}.
METAL 380 380 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_00020}.
BINDING 13 13 ATP. {ECO:0000255|HAMAP-Rule:MF_00020}.
BINDING 87 87 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00020}.
SITE 175 175 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_00020}.
SITE 236 236 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_00020}.
SEQUENCE 393 AA; 44138 MW; 3F4A0A72843FABAE CRC64;
MILVINSGSS SIKFKLFDTS KAIEPILDGL AERIGIDGFL KFEHNNQKYK FEDPLPDHEH
AIQLILNKLL ELKIISNIDE IKGVGFRVVH GGEISHSSII NEEVLQKIQE SVKLAPLHNP
AAIIAIKAVK KLMPNTSMIA CFDTAFHQTM PQVNYLYSVP YKWYEEFGVR KYGFHGISYE
YIVNKCEEIL NKKKEHLNLI VCHLGNGASI SCIKDGKSYD TSMGLTPLAG LMMGTRSGDI
DVSICEYVAK QTNSDIFAIT QILNKQSGLL GLSQTSADMR DVLEQYDRND KKAIIAVEKY
VQVVADFIVK YANYLDSIDA VVFTAGIGEN ADVIRDLICK RVKLLGLQID QEKNESKYSD
YKLISSEKSK IPVYAIRTNE EKMICLDTLN LIK


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