ACKA_MYCS2
ID ACKA_MYCS2 Reviewed; 376 AA.
AC A0QQK1;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
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};
GN OrderedLocusNames=MSMEG_0784, MSMEI_0768;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH THE ATP ANALOG AMP,
RP AND SUBUNIT.
RC STRAIN=ATCC 700084 / mc(2)155;
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Crystal structure of an acetate kinase from Mycobacterium smegmatis bound
RT to AMP and sulfate.";
RL Submitted (JAN-2013) 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.4}.
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; CP000480; ABK74906.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37248.1; -; Genomic_DNA.
DR RefSeq; WP_011727188.1; NZ_SIJM01000036.1.
DR RefSeq; YP_885189.1; NC_008596.1.
DR PDB; 4IJN; X-ray; 1.70 A; A/B=2-376.
DR PDBsum; 4IJN; -.
DR AlphaFoldDB; A0QQK1; -.
DR SMR; A0QQK1; -.
DR STRING; 246196.MSMEI_0768; -.
DR PRIDE; A0QQK1; -.
DR EnsemblBacteria; ABK74906; ABK74906; MSMEG_0784.
DR EnsemblBacteria; AFP37248; AFP37248; MSMEI_0768.
DR GeneID; 66738959; -.
DR KEGG; msg:MSMEI_0768; -.
DR KEGG; msm:MSMEG_0784; -.
DR PATRIC; fig|246196.19.peg.779; -.
DR eggNOG; COG0282; Bacteria.
DR OMA; KIITCHI; -.
DR OrthoDB; 537106at2; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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..376
FT /note="Acetate kinase"
FT /id="PRO_0000421948"
FT ACT_SITE 128
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 188..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 262..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 310..314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT SITE 160
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT SITE 221
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:4IJN"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:4IJN"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:4IJN"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 42..55
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4IJN"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:4IJN"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:4IJN"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:4IJN"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 161..174
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4IJN"
FT STRAND 183..199
FT /evidence="ECO:0007829|PDB:4IJN"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:4IJN"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 253..258
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 275..299
FT /evidence="ECO:0007829|PDB:4IJN"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 316..323
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:4IJN"
FT STRAND 354..359
FT /evidence="ECO:0007829|PDB:4IJN"
FT HELIX 364..372
FT /evidence="ECO:0007829|PDB:4IJN"
SQ SEQUENCE 376 AA; 40116 MW; 5F9BBCA380D2A161 CRC64;
MTVLVVNSGS SSLKYAVVRP ASGEFLADGI IEEIGSGAVP DHDAALRAAF DELAAAGLHL
EDLDLKAVGH RMVHGGKTFY KPSVVDDELI AKARELSPLA PLHNPPAIKG IEVARKLLPD
LPHIAVFDTA FFHDLPAPAS TYAIDRELAE TWHIKRYGFH GTSHEYVSQQ AAIFLDRPLE
SLNQIVLHLG NGASASAVAG GKAVDTSMGL TPMEGLVMGT RSGDIDPGVI MYLWRTAGMS
VDDIESMLNR RSGVLGLGGA SDFRKLRELI ESGDEHAKLA YDVYIHRLRK YIGAYMAVLG
RTDVISFTAG VGENVPPVRR DALAGLGGLG IEIDDALNSA KSDEPRLIST PDSRVTVLVV
PTNEELAIAR ACVGVV
