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Acetate kinase (EC 2.7.2.1) (Acetokinase)

 R5M0Z7_9MOLU            Unreviewed;       393 AA.
R5M0Z7;
24-JUL-2013, integrated into UniProtKB/TrEMBL.
24-JUL-2013, sequence version 1.
27-SEP-2017, entry version 23.
RecName: Full=Acetate kinase {ECO:0000256|HAMAP-Rule:MF_00020};
EC=2.7.2.1 {ECO:0000256|HAMAP-Rule:MF_00020};
AltName: Full=Acetokinase {ECO:0000256|HAMAP-Rule:MF_00020};
Name=ackA {ECO:0000256|HAMAP-Rule:MF_00020};
ORFNames=BN801_00197 {ECO:0000313|EMBL:CCY78912.1};
Mycoplasma sp. CAG:877.
Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma;
environmental samples.
NCBI_TaxID=1262907 {ECO:0000313|EMBL:CCY78912.1, ECO:0000313|Proteomes:UP000018280};
[1] {ECO:0000313|EMBL:CCY78912.1, ECO:0000313|Proteomes:UP000018280}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MGS:877 {ECO:0000313|Proteomes:UP000018280};
Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
Brunak S., Ehrlich S.D.;
"Dependencies among metagenomic species, viruses, plasmids and units
of genetic variation.";
Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate
and ATP. Can also catalyze the reverse reaction.
{ECO:0000256|HAMAP-Rule:MF_00020}.
-!- CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate.
{ECO:0000256|HAMAP-Rule:MF_00020}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00020};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|HAMAP-Rule:MF_00020};
Note=Mg(2+). Can also accept Mn(2+). {ECO:0000256|HAMAP-
Rule:MF_00020};
-!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA
biosynthesis; acetyl-CoA from acetate: step 1/2.
{ECO:0000256|HAMAP-Rule:MF_00020}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00020}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020,
ECO:0000256|SAAS:SAAS00011667}.
-!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000256|HAMAP-
Rule:MF_00020, ECO:0000256|RuleBase:RU003835,
ECO:0000256|SAAS:SAAS00688878}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:CCY78912.1}.
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EMBL; CAYV010000007; CCY78912.1; -; Genomic_DNA.
UniPathway; UPA00340; UER00458.
Proteomes; UP000018280; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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 {ECO:0000256|HAMAP-Rule:MF_00020,
ECO:0000256|SAAS:SAAS00483886};
Complete proteome {ECO:0000313|Proteomes:UP000018280};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020,
ECO:0000256|SAAS:SAAS00011637};
Kinase {ECO:0000256|HAMAP-Rule:MF_00020,
ECO:0000256|RuleBase:RU003835, ECO:0000256|SAAS:SAAS00483909,
ECO:0000313|EMBL:CCY78912.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00020,
ECO:0000256|SAAS:SAAS00011608};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00020,
ECO:0000256|SAAS:SAAS00011656};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00020,
ECO:0000256|SAAS:SAAS00483886};
Reference proteome {ECO:0000313|Proteomes:UP000018280};
Transferase {ECO:0000256|HAMAP-Rule:MF_00020,
ECO:0000256|RuleBase:RU003835, ECO:0000256|SAAS:SAAS00483909,
ECO:0000313|EMBL:CCY78912.1}.
NP_BIND 203 207 ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
NP_BIND 278 280 ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
NP_BIND 326 330 ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
ACT_SITE 145 145 Proton donor/acceptor.
{ECO:0000256|HAMAP-Rule:MF_00020}.
METAL 7 7 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00020}.
METAL 379 379 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_00020}.
BINDING 14 14 ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
BINDING 88 88 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00020}.
SITE 177 177 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_00020}.
SITE 236 236 Transition state stabilizer.
{ECO:0000256|HAMAP-Rule:MF_00020}.
SEQUENCE 393 AA; 43727 MW; 490D8032BEAA02C0 CRC64;
MKVLSVNAGS SSLKFSLFDM ANDNVLTSGV FERIGIEGST FTIKFNGEKI VQEVELNNHV
DAVNILIDRL ISLDIIKSLE EINGIGHRVA HGKDYFDKST IINDSVLEKL RGVKDMAPLH
NPANLLGIEA FEKVLPNVVQ VAVFDTAYHQ SMDEVSYLYP VPYSWYKDYG LRKYGFHGTS
HKYIAREAKK LLGRDNYKLI SCHIGNGGSI CAIKDGKCVD TSMGFTPLAG IMMGTRSGDV
DPSIIPYIME KEGKNASEVI EDLNKKSGLY GMSEFSNDMR DILARCDEGD HRALVAKEKY
VRRIVDYIAQ YYVLLGGVDM IALTAGVGEN NKVIRKEILD KLECLGVKIS DEANETVGEE
VKLSTKDSKI LVYVIPTDEE LMIAKDTYNL INR


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