ACKA_PORG3
ID ACKA_PORG3 Reviewed; 398 AA.
AC B2RK02;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=PGN_1178;
OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS 12257 / NCTC 11834 / 2561).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=431947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA Nakayama K.;
RT "Determination of the genome sequence of Porphyromonas gingivalis strain
RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT rearrangements in P. gingivalis.";
RL DNA Res. 15:215-225(2008).
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:0000255|HAMAP-Rule:MF_00020}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}.
CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00020}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP009380; BAG33697.1; -; Genomic_DNA.
DR RefSeq; WP_012458083.1; NZ_CP025930.1.
DR PDB; 6IOY; X-ray; 1.94 A; A/B/C/D=2-398.
DR PDBsum; 6IOY; -.
DR AlphaFoldDB; B2RK02; -.
DR SMR; B2RK02; -.
DR STRING; 431947.PGN_1178; -.
DR EnsemblBacteria; BAG33697; BAG33697; PGN_1178.
DR GeneID; 29256384; -.
DR KEGG; pgn:PGN_1178; -.
DR eggNOG; COG0282; Bacteria.
DR HOGENOM; CLU_020352_0_1_10; -.
DR OMA; KIITCHI; -.
DR BioCyc; PGIN431947:G1G2V-1347-MON; -.
DR BRENDA; 2.7.2.1; 756.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000008842; 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; Transferase.
FT CHAIN 1..398
FT /note="Acetate kinase"
FT /id="PRO_1000089989"
FT ACT_SITE 148
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 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 208..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 283..285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 331..335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT SITE 180
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT SITE 241
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:6IOY"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:6IOY"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:6IOY"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:6IOY"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:6IOY"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:6IOY"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:6IOY"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:6IOY"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:6IOY"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:6IOY"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:6IOY"
FT STRAND 203..219
FT /evidence="ECO:0007829|PDB:6IOY"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:6IOY"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 261..270
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 296..320
FT /evidence="ECO:0007829|PDB:6IOY"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 330..335
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 337..344
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:6IOY"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:6IOY"
FT HELIX 385..397
FT /evidence="ECO:0007829|PDB:6IOY"
SQ SEQUENCE 398 AA; 43272 MW; DAA0452BCFE70092 CRC64;
MKVLVLNCGS SSVKYKLLEM PKGDVLAQGG VEKLGLPGSF LKLTMPNGEK VVLEKDMPEH
TIAVEFILSV LKDDKYGCIK SYEEIDAVGH RLVHGGEKFS NSVEITPEVI AKVEECIPLA
PLHNPANLKG VVAIEKLLPG IRQVGVFDTA FFQTMPEHVY RYALPYDMCN KHGVRRYGFH
GTSHRYVSAR ACEILGLDYD KTRIITAHIG NGASIAAIKN GKALDVSLGM TPVEGLMMGT
RSGDVDPGVL TFLMEAEGLQ AAGISELINK KSGVLGVSGV SSDLREIEDA IKNGNERATL
AMTMYDYRIK KYVGAYAAAM GGVDVLVFTG GVGENQYTTR EKVCTDMEFM GIVFDSKVNE
GMRGKEMVIS KPESKVTVIV VPTDEEYMIA SDTMTILK
