ACKA_METTE
ID ACKA_METTE Reviewed; 408 AA.
AC P38502;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Acetate kinase {ECO:0000255|HAMAP-Rule:MF_00020};
DE EC=2.7.2.1 {ECO:0000255|HAMAP-Rule:MF_00020};
DE AltName: Full=Acetokinase {ECO:0000255|HAMAP-Rule:MF_00020};
GN Name=ackA {ECO:0000255|HAMAP-Rule:MF_00020}; Synonyms=ack;
OS Methanosarcina thermophila.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=2210;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / TM-1;
RX PubMed=8226623; DOI=10.1128/jb.175.21.6822-6829.1993;
RA Latimer M.T., Ferry J.G.;
RT "Cloning, sequence analysis, and hyperexpression of the genes encoding
RT phosphotransacetylase and acetate kinase from Methanosarcina thermophila.";
RL J. Bacteriol. 175:6822-6829(1993).
RN [2]
RP PROTEIN SEQUENCE OF 1-17, CATALYTIC ACTIVITY, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2844814; DOI=10.1016/s0021-9258(19)37608-2;
RA Aceti D.J., Ferry J.G.;
RT "Purification and characterization of acetate kinase from acetate-grown
RT Methanosarcina thermophila. Evidence for regulation of synthesis.";
RL J. Biol. Chem. 263:15444-15448(1988).
RN [3]
RP CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND MUTAGENESIS OF ASN-7; SER-10;
RP SER-12; LYS-14; ASP-148; ASN-211 AND GLU-384.
RX PubMed=11562377; DOI=10.1074/jbc.m108355200;
RA Miles R.D., Iyer P.P., Ferry J.G.;
RT "Site-directed mutational analysis of active site residues in the acetate
RT kinase from Methanosarcina thermophila.";
RL J. Biol. Chem. 276:45059-45064(2001).
RN [4]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF VAL-93; LEU-122; PHE-179 AND PRO-232.
RX PubMed=15774882; DOI=10.1128/jb.187.7.2386-2394.2005;
RA Ingram-Smith C., Gorrell A., Lawrence S.H., Iyer P., Smith K., Ferry J.G.;
RT "Characterization of the acetate binding pocket in the Methanosarcina
RT thermophila acetate kinase.";
RL J. Bacteriol. 187:2386-2394(2005).
RN [5]
RP CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS
RP OF ARG-91 AND ARG-241.
RX PubMed=17999468; DOI=10.1021/bi701292a;
RA Gorrell A., Ferry J.G.;
RT "Investigation of the Methanosarcina thermophila acetate kinase mechanism
RT by fluorescence quenching.";
RL Biochemistry 46:14170-14176(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH THE ATP ANALOG ADP,
RP ACTIVE SITE, AND SUBUNIT.
RX PubMed=11133963; DOI=10.1128/jb.183.2.680-686.2001;
RA Buss K.A., Cooper D.R., Ingram-Smith C., Ferry J.G., Sanders D.A.,
RA Hasson M.S.;
RT "Urkinase: structure of acetate kinase, a member of the ASKHA superfamily
RT of phosphotransferases.";
RL J. Bacteriol. 183:680-686(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-399 IN COMPLEX WITH THE ATP
RP ANALOGS ADP; AMP; ALF3 AND THE SUBSTRATE ACETATE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, ACTIVITY REGULATION, COFACTOR,
RP SUBUNIT, AND MUTAGENESIS OF ARG-91 AND ARG-241.
RX PubMed=15647264; DOI=10.1074/jbc.m412118200;
RA Gorrell A., Lawrence S.H., Ferry J.G.;
RT "Structural and kinetic analyses of arginine residues in the active site of
RT the acetate kinase from Methanosarcina thermophila.";
RL J. Biol. Chem. 280:10731-10742(2005).
CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and
CC ATP. Can also catalyze the reverse reaction. Can also phosphorylate
CC propionate, but has very low activity toward butyrate.
CC {ECO:0000255|HAMAP-Rule:MF_00020, ECO:0000269|PubMed:15774882}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP = acetyl phosphate + ADP; Xref=Rhea:RHEA:11352,
CC ChEBI:CHEBI:22191, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456216; EC=2.7.2.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00020, ECO:0000269|PubMed:11562377,
CC ECO:0000269|PubMed:15647264, ECO:0000269|PubMed:15774882,
CC ECO:0000269|PubMed:17999468, ECO:0000269|PubMed:2844814,
CC ECO:0000269|PubMed:8226623};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020,
CC ECO:0000269|PubMed:11562377, ECO:0000269|PubMed:15647264};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020,
CC ECO:0000269|PubMed:11562377, ECO:0000269|PubMed:15647264};
CC Note=Mg(2+). Can also accept Mn(2+). The Mg(2+) is bound between two
CC conserved protein residues and the ATP phosphate groups.
CC {ECO:0000255|HAMAP-Rule:MF_00020, ECO:0000269|PubMed:11562377,
CC ECO:0000269|PubMed:15647264};
CC -!- ACTIVITY REGULATION: Inhibited by diethylpyrocarbonate, hydroxylamine
CC and phenylglyoxal. {ECO:0000269|PubMed:15647264,
CC ECO:0000269|PubMed:8226623}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=71 uM for ATP {ECO:0000269|PubMed:15647264,
CC ECO:0000269|PubMed:15774882, ECO:0000269|PubMed:17999468,
CC ECO:0000269|PubMed:2844814, ECO:0000269|PubMed:8226623};
CC KM=98 uM for ADP {ECO:0000269|PubMed:15647264,
CC ECO:0000269|PubMed:15774882, ECO:0000269|PubMed:17999468,
CC ECO:0000269|PubMed:2844814, ECO:0000269|PubMed:8226623};
CC KM=1.5 mM for acetate {ECO:0000269|PubMed:15647264,
CC ECO:0000269|PubMed:15774882, ECO:0000269|PubMed:17999468,
CC ECO:0000269|PubMed:2844814, ECO:0000269|PubMed:8226623};
CC KM=0.47 mM for acetyl phosphate {ECO:0000269|PubMed:15647264,
CC ECO:0000269|PubMed:15774882, ECO:0000269|PubMed:17999468,
CC ECO:0000269|PubMed:2844814, ECO:0000269|PubMed:8226623};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius. Protected from thermal
CC inactivation by ATP. {ECO:0000269|PubMed:15647264,
CC ECO:0000269|PubMed:15774882, ECO:0000269|PubMed:17999468,
CC ECO:0000269|PubMed:2844814, ECO:0000269|PubMed:8226623};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00020}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00020,
CC ECO:0000269|PubMed:11133963, ECO:0000269|PubMed:11562377,
CC ECO:0000269|PubMed:15647264, ECO:0000269|PubMed:17999468,
CC ECO:0000269|PubMed:2844814}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}.
CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00020}.
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DR EMBL; L23147; AAA72042.1; -; Unassigned_DNA.
DR PIR; B49338; B49338.
DR PDB; 1G99; X-ray; 2.50 A; A/B=1-408.
DR PDB; 1TUU; X-ray; 2.50 A; A/B=1-399.
DR PDB; 1TUY; X-ray; 3.00 A; A/B=1-399.
DR PDBsum; 1G99; -.
DR PDBsum; 1TUU; -.
DR PDBsum; 1TUY; -.
DR AlphaFoldDB; P38502; -.
DR SMR; P38502; -.
DR KEGG; ag:AAA72042; -.
DR BRENDA; 2.7.2.1; 3281.
DR SABIO-RK; P38502; -.
DR UniPathway; UPA00340; UER00458.
DR EvolutionaryTrace; P38502; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006082; P:organic acid metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00020; Acetate_kinase; 1.
DR InterPro; IPR004372; Ac/propionate_kinase.
DR InterPro; IPR000890; Aliphatic_acid_kin_short-chain.
DR InterPro; IPR023865; Aliphatic_acid_kinase_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR21060; PTHR21060; 1.
DR Pfam; PF00871; Acetate_kinase; 1.
DR PIRSF; PIRSF000722; Acetate_prop_kin; 1.
DR PRINTS; PR00471; ACETATEKNASE.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00016; ackA; 1.
DR PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Transferase.
FT CHAIN 1..408
FT /note="Acetate kinase"
FT /id="PRO_0000107650"
FT ACT_SITE 148
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020,
FT ECO:0000269|PubMed:11133963, ECO:0000269|PubMed:15647264"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT BINDING 14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 91
FT /ligand="substrate"
FT BINDING 208..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 283..285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 331..335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 384
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305"
FT SITE 180
FT /note="Transition state stabilizer"
FT SITE 241
FT /note="Transition state stabilizer"
FT MUTAGEN 7
FT /note="N->A: Almost abolishes catalytic activity. Requires
FT increased magnesium levels for activity. Strongly decreases
FT affinity for acetate."
FT /evidence="ECO:0000269|PubMed:11562377"
FT MUTAGEN 7
FT /note="N->D: Almost abolishes catalytic activity. Strongly
FT decreases affinity for acetate."
FT /evidence="ECO:0000269|PubMed:11562377"
FT MUTAGEN 10
FT /note="S->A,T: Strongly decreases catalytic activity.
FT Strongly decreases affinity for acetate."
FT /evidence="ECO:0000269|PubMed:11562377"
FT MUTAGEN 11
FT /note="S->A: Decreases catalytic activity. Decreases
FT affinity for acetate."
FT MUTAGEN 11
FT /note="S->T: Strongly decreases catalytic activity.
FT Strongly decreases affinity for acetate."
FT MUTAGEN 12
FT /note="S->A: Decreases catalytic activity. Strongly
FT decreases affinity for acetate. Requires increased
FT magnesium levels for enzyme activity."
FT /evidence="ECO:0000269|PubMed:11562377"
FT MUTAGEN 12
FT /note="S->T: Decreases catalytic activity. Strongly
FT decreases affinity for acetate."
FT /evidence="ECO:0000269|PubMed:11562377"
FT MUTAGEN 14
FT /note="K->A: Strongly decreases enzyme activity."
FT /evidence="ECO:0000269|PubMed:11562377"
FT MUTAGEN 14
FT /note="K->R: Reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:11562377"
FT MUTAGEN 91
FT /note="R->A,L: Decreases catalytic activity. Decreases
FT affinity for acetate."
FT /evidence="ECO:0000269|PubMed:15647264,
FT ECO:0000269|PubMed:17999468"
FT MUTAGEN 93
FT /note="V->A: Decreases affinity for acetate."
FT /evidence="ECO:0000269|PubMed:15774882"
FT MUTAGEN 122
FT /note="L->A: Decreases affinity for acetate."
FT /evidence="ECO:0000269|PubMed:15774882"
FT MUTAGEN 148
FT /note="D->A,E,N: Abolishes catalytic activity. Decreases
FT affinity for acetate, but not for ATP."
FT /evidence="ECO:0000269|PubMed:11562377"
FT MUTAGEN 179
FT /note="F->A: Decreases affinity for acetate."
FT /evidence="ECO:0000269|PubMed:15774882"
FT MUTAGEN 211
FT /note="N->A: Slightly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:11562377"
FT MUTAGEN 232
FT /note="P->A: Decreases affinity for acetate."
FT /evidence="ECO:0000269|PubMed:15774882"
FT MUTAGEN 241
FT /note="R->K,L: Decreases catalytic activity. Strongly
FT reduced affinity for ATP."
FT /evidence="ECO:0000269|PubMed:15647264,
FT ECO:0000269|PubMed:17999468"
FT MUTAGEN 384
FT /note="E->A: Almost abolishes catalytic activity. Strongly
FT decreases affinity for acetate. Requires strongly increased
FT magnesium levels for enzyme activity."
FT /evidence="ECO:0000269|PubMed:11562377"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:1G99"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:1G99"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:1G99"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:1G99"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1G99"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1G99"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:1G99"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1G99"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:1G99"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1G99"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:1G99"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1G99"
FT STRAND 203..219
FT /evidence="ECO:0007829|PDB:1G99"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:1G99"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 261..270
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 296..319
FT /evidence="ECO:0007829|PDB:1G99"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 330..335
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 337..344
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:1G99"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:1G99"
FT HELIX 384..397
FT /evidence="ECO:0007829|PDB:1G99"
SQ SEQUENCE 408 AA; 44337 MW; 1A484DF8A7258800 CRC64;
MKVLVINAGS SSLKYQLIDM TNESALAVGL CERIGIDNSI ITQKKFDGKK LEKLTDLPTH
KDALEEVVKA LTDDEFGVIK DMGEINAVGH RVVHGGEKFT TSALYDEGVE KAIKDCFELA
PLHNPPNMMG ISACAEIMPG TPMVIVFDTA FHQTMPPYAY MYALPYDLYE KHGVRKYGFH
GTSHKYVAER AALMLGKPAE ETKIITCHLG NGSSITAVEG GKSVETSMGF TPLEGLAMGT
RCGSIDPAIV PFLMEKEGLT TREIDTLMNK KSGVLGVSGL SNDFRDLDEA ASKGNRKAEL
ALEIFAYKVK KFIGEYSAVL NGADAVVFTA GIGENSASIR KRILTGLDGI GIKIDDEKNK
IRGQEIDIST PDAKVRVFVI PTNEELAIAR ETKEIVETEV KLRSSIPV
