ACKA_MYCPA
ID ACKA_MYCPA Reviewed; 387 AA.
AC Q73T33;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=MAP_3886;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC BAA-968 / K-10;
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Crystal structure of AckA from Mycobacterium paratuberculosis ATCC BAA-968
RT / K-10.";
RL Submitted (MAR-2011) 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; AE016958; AAS06436.1; -; Genomic_DNA.
DR RefSeq; WP_003873824.1; NC_002944.2.
DR PDB; 3R9P; X-ray; 1.90 A; A/B=1-387.
DR PDBsum; 3R9P; -.
DR AlphaFoldDB; Q73T33; -.
DR SMR; Q73T33; -.
DR STRING; 262316.MAP_3886; -.
DR EnsemblBacteria; AAS06436; AAS06436; MAP_3886.
DR KEGG; mpa:MAP_3886; -.
DR PATRIC; fig|262316.17.peg.4137; -.
DR eggNOG; COG0282; Bacteria.
DR HOGENOM; CLU_020352_0_1_11; -.
DR OMA; KIITCHI; -.
DR UniPathway; UPA00340; UER00458.
DR EvolutionaryTrace; Q73T33; -.
DR Proteomes; UP000000580; 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; Reference proteome; Transferase.
FT CHAIN 1..387
FT /note="Acetate kinase"
FT /id="PRO_0000421947"
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:3R9P"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:3R9P"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:3R9P"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:3R9P"
FT TURN 69..73
FT /evidence="ECO:0007829|PDB:3R9P"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:3R9P"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:3R9P"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:3R9P"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 170..183
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3R9P"
FT STRAND 192..208
FT /evidence="ECO:0007829|PDB:3R9P"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:3R9P"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 273..280
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 284..308
FT /evidence="ECO:0007829|PDB:3R9P"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:3R9P"
FT STRAND 353..356
FT /evidence="ECO:0007829|PDB:3R9P"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:3R9P"
FT HELIX 373..384
FT /evidence="ECO:0007829|PDB:3R9P"
SQ SEQUENCE 387 AA; 41310 MW; 3608EB4D41710C0F CRC64;
MDGSDGARRV LVINSGSSSL KFQLVDPEFG VAASTGIVER IGEESSPVPD HDAALRRAFD
MLAGDGVDLN TAGLVAVGHR VVHGGNTFYR PTVLDDAVIA RLHELSELAP LHNPPALQGI
EVARRLLPDI AHVAVFDTGF FHDLPPAAAT YAIDRELADR WQIRRYGFHG TSHRYVSEQA
AAFLDRPLRG LKQIVLHLGN GCSASAIAGT RPLDTSMGLT PLEGLVMGTR SGDIDPSIVS
YLCHTAGMGV DDVESMLNHR SGVVGLSGVR DFRRLRELIE SGDGAAQLAY SVFTHRLRKY
IGAYLAVLGH TDVISFTAGI GENDAAVRRD AVSGMEELGI VLDERRNLAG GKGARQISAD
DSPITVLVVP TNEELAIARD CVRVLGG
