ACKA_MYCA1
ID ACKA_MYCA1 Reviewed; 387 AA.
AC A0QLU8;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=MAV_4758;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS), AND SUBUNIT.
RC STRAIN=104;
RG Seattle structural genomics center for infectious disease (SSGCID);
RA Edwards T.E., Gardberg A.S.;
RT "Crystal structure of acetate kinase from Mycobacterium avium.";
RL Submitted (OCT-2010) 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; CP000479; ABK64849.1; -; Genomic_DNA.
DR RefSeq; WP_011726229.1; NC_008595.1.
DR PDB; 3P4I; X-ray; 2.35 A; A/B=2-387.
DR PDB; 4IZ9; X-ray; 1.98 A; A=2-387.
DR PDBsum; 3P4I; -.
DR PDBsum; 4IZ9; -.
DR AlphaFoldDB; A0QLU8; -.
DR SMR; A0QLU8; -.
DR EnsemblBacteria; ABK64849; ABK64849; MAV_4758.
DR KEGG; mav:MAV_4758; -.
DR HOGENOM; CLU_020352_0_1_11; -.
DR OMA; KIITCHI; -.
DR OrthoDB; 537106at2; -.
DR UniPathway; UPA00340; UER00458.
DR EvolutionaryTrace; A0QLU8; -.
DR Proteomes; UP000001574; 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.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..387
FT /note="Acetate kinase"
FT /id="PRO_0000421950"
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:4IZ9"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:4IZ9"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:4IZ9"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:4IZ9"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:4IZ9"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:4IZ9"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:4IZ9"
FT TURN 104..108
FT /evidence="ECO:0007829|PDB:4IZ9"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:4IZ9"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 155..161
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 170..184
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4IZ9"
FT STRAND 192..208
FT /evidence="ECO:0007829|PDB:4IZ9"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:4IZ9"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 284..308
FT /evidence="ECO:0007829|PDB:4IZ9"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:4IZ9"
FT TURN 344..347
FT /evidence="ECO:0007829|PDB:4IZ9"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:4IZ9"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:4IZ9"
FT HELIX 373..384
FT /evidence="ECO:0007829|PDB:4IZ9"
SQ SEQUENCE 387 AA; 41203 MW; 39014EA8917B3E4F CRC64;
MDGSDGARRV LVINSGSSSL KFQLVDPESG VAASTGIVER IGEESSPVPD HDAALRRAFD
MLAGDGVDLN TAGLVAVGHR VVHGGNTFYR PTVLDDAVIA RLHELSELAP LHNPPALLGI
EVARRLLPGI AHVAVFDTGF FHDLPPAAAT YAIDRELADR WQIRRYGFHG TSHRYVSEQA
AAFLDRPLRG LKQIVLHLGN GCSASAIAGT RPLDTSMGLT PLEGLVMGTR SGDIDPSVVS
YLCHTAGMGV DDVESMLNHR SGVVGLSGVR DFRRLRELIE SGDGAAQLAY SVFTHRLRKY
IGAYLAVLGH TDVISFTAGI GENDAAVRRD AVSGMEELGI VLDERRNLPG AKGARQISAD
DSPITVLVVP TNEELAIARD CVRVLGG
