ACKA_MYCMM
ID ACKA_MYCMM Reviewed; 388 AA.
AC B2HPZ3;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
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}; OrderedLocusNames=MMAR_0711;
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC BAA-535 / M;
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Crystal structure of acetate kinase AckA from Mycobacterium marinum.";
RL Submitted (FEB-2012) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and
CC ATP. Can also catalyze the reverse reaction. {ECO:0000255|HAMAP-
CC Rule:MF_00020}.
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00020};
CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000255|HAMAP-Rule:MF_00020};
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:0000305|Ref.2}.
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; CP000854; ACC39170.1; -; Genomic_DNA.
DR RefSeq; WP_012392661.1; NC_010612.1.
DR PDB; 4DQ8; X-ray; 2.25 A; A/B=1-387.
DR PDBsum; 4DQ8; -.
DR AlphaFoldDB; B2HPZ3; -.
DR SMR; B2HPZ3; -.
DR STRING; 216594.MMAR_0711; -.
DR EnsemblBacteria; ACC39170; ACC39170; MMAR_0711.
DR GeneID; 64259452; -.
DR KEGG; mmi:MMAR_0711; -.
DR eggNOG; COG0282; Bacteria.
DR HOGENOM; CLU_020352_0_1_11; -.
DR OMA; KIITCHI; -.
DR OrthoDB; 537106at2; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000001190; Chromosome.
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; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..388
FT /note="Acetate kinase"
FT /id="PRO_0000421949"
FT ACT_SITE 137
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 197..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 271..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 319..323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 373
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT SITE 169
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT SITE 230
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:4DQ8"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:4DQ8"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:4DQ8"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:4DQ8"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:4DQ8"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:4DQ8"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:4DQ8"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 170..184
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4DQ8"
FT STRAND 192..208
FT /evidence="ECO:0007829|PDB:4DQ8"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:4DQ8"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 284..308
FT /evidence="ECO:0007829|PDB:4DQ8"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 344..348
FT /evidence="ECO:0007829|PDB:4DQ8"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:4DQ8"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:4DQ8"
FT HELIX 373..383
FT /evidence="ECO:0007829|PDB:4DQ8"
SQ SEQUENCE 388 AA; 41617 MW; BE4CD8FAACB8734A CRC64;
MSASRPNRVV LVLNSGSSSL KFQLVEPDSG MSRATGNIER IGEESSSVPD HDAALRRVFE
ILAEDDIDLQ SCGLVAVGHR VVHGGKDFYE PTLLNDAVIG KLDELSPLAP LHNPPAVLCI
RVARALLPDV PHIAVFDTAF FHQLPPAAAT YAIDRELADV WKIRRYGFHG TSHEYVSQQA
AEFLGKPIGD LNQIVLHLGN GASASAVAGG RPVETSMGLT PLEGLVMGTR SGDLDPGVIG
YLWRTAKLGV DEIESMLNHR SGMLGLAGER DFRRLRAMID DGDPAAELAY DVFIHRLRKY
VGAYLAVLGH TDVVSFTAGI GEHDAAVRRD TLAGMAELGI SLDERRNACP SGGARRISAD
DSPVTVLVIP TNEELAIARH CCSVLVAV
