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Database: UniProt/TrEMBL
Entry: H2FR23_CORPS
LinkDB: H2FR23_CORPS
Original site: H2FR23_CORPS 
ID   H2FR23_CORPS            Unreviewed;       400 AA.
AC   H2FR23;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   26-NOV-2014, entry version 22.
DE   RecName: Full=Acetate kinase {ECO:0000256|HAMAP-Rule:MF_00020};
DE            EC=2.7.2.1 {ECO:0000256|HAMAP-Rule:MF_00020};
DE   AltName: Full=Acetokinase {ECO:0000256|HAMAP-Rule:MF_00020};
GN   Name=ackA {ECO:0000256|HAMAP-Rule:MF_00020,
GN   ECO:0000313|EMBL:AEX40333.1};
GN   ORFNames=Cp3995_1883 {ECO:0000313|EMBL:AEX40333.1};
OS   Corynebacterium pseudotuberculosis 3/99-5.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1087452 {ECO:0000313|EMBL:AEX40333.1, ECO:0000313|Proteomes:UP000008359};
RN   [1] {ECO:0000313|EMBL:AEX40333.1, ECO:0000313|Proteomes:UP000008359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3/99-5 {ECO:0000313|EMBL:AEX40333.1};
RX   PubMed=22887652; DOI=10.1128/JB.00918-12;
RA   Pethick F.E., Lainson A.F., Yaga R., Flockhart A., Smith D.G.,
RA   Donachie W., Cerdeira L.T., Silva A., Bol E., Lopes T.S.,
RA   Barbosa M.S., Pinto A.C., Dos Santos A.R., Soares S.C., Almeida S.S.,
RA   Guimaraes L.C., Aburjaile F.F., Abreu V.A., Ribeiro D., Fiaux K.K.,
RA   Diniz C.A., Barbosa E.G., Pereira U.P., Hassan S.S., Ali A.,
RA   Bakhtiar S.M., Dorella F.A., Carneiro A.R., Ramos R.T., Rocha F.S.,
RA   Schneider M.P., Miyoshi A., Azevedo V., Fontaine M.C.;
RT   "Complete Genome Sequences of Corynebacterium pseudotuberculosis
RT   Strains 3/99-5 and 42/02-A, Isolated from Sheep in Scotland and
RT   Australia, Respectively.";
RL   J. Bacteriol. 194:4736-4737(2012).
CC   -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate
CC       and ATP. Can also catalyze the reverse reaction.
CC       {ECO:0000256|HAMAP-Rule:MF_00020}.
CC   -!- CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_00020}.
CC   -!- COFACTOR:
CC       Note=Mg(2+). Can also accept Mn(2+). {ECO:0000256|HAMAP-
CC       Rule:MF_00020};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA
CC       biosynthesis; acetyl-CoA from acetate: step 1/2.
CC       {ECO:0000256|HAMAP-Rule:MF_00020}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00020}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020,
CC       ECO:0000256|SAAS:SAAS00130554}.
CC   -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00020, ECO:0000256|RuleBase:RU003835}.
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DR   EMBL; CP003152; AEX40333.1; -; Genomic_DNA.
DR   RefSeq; YP_005123982.1; NC_016781.1.
DR   ProteinModelPortal; H2FR23; -.
DR   EnsemblBacteria; AEX40333; AEX40333; Cp3995_1883.
DR   GeneID; 11674761; -.
DR   KEGG; cpl:Cp3995_1883; -.
DR   KO; K00925; -.
DR   BioCyc; CPSE1087452:GJTM-1940-MONOMER; -.
DR   UniPathway; UPA00340; UER00458.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006082; P:organic acid metabolic process; IEA:InterPro.
DR   HAMAP; MF_00020; Acetate_kinase; 1.
DR   InterPro; IPR004372; Ac/Proprionate_kinase.
DR   InterPro; IPR000890; Aliphatic_acid_kin_short-chain.
DR   InterPro; IPR023865; Aliphatic_acid_kinase_CS.
DR   PANTHER; PTHR21060; PTHR21060; 1.
DR   Pfam; PF00871; Acetate_kinase; 1.
DR   PIRSF; PIRSF000722; Acetate_prop_kin; 1.
DR   PRINTS; PR00471; ACETATEKNASE.
DR   TIGRFAMs; TIGR00016; ackA; 1.
DR   PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR   PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00091196};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008359};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00130644};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|RuleBase:RU003835};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00091199};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00091203};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|SAAS:SAAS00091197};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00020,
KW   ECO:0000256|RuleBase:RU003835}.
FT   NP_BIND     209    213       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   NP_BIND     283    285       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   NP_BIND     331    335       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   ACT_SITE    149    149       Proton donor/acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   METAL         8      8       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   METAL       385    385       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   BINDING      15     15       ATP. {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   BINDING      92     92       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00020}.
FT   SITE        181    181       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
FT   SITE        242    242       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00020}.
SQ   SEQUENCE   400 AA;  42855 MW;  3A32ECB8502BE121 CRC64;
     MALVLVLNSG SSSIKFQLVD PTQHATDAPF ASGLVEQIGE PKGKITLKHG GEKYVVEAPI
     ADHTAGLDLA FKLMGEHGCG PKDVELEAVG HRVVHGGQVF SQPELITDEV VEAIRGLIPL
     APLHNPANIS GIEVARTLLP ELPHVAVFDT GFFYSMPPAS ALYAIESETA TKNGVRRYGF
     HGTSHEYISQ QVPKLLGKDP EDVNQITLHL GNGASAAAIR QGNPIDTSMG MTPLAGLAMG
     TRSGDIDPGI IFHLYRTAGM SIDEIDDLLN KRSGVKGISG VNDFRELHQL IAEGNEDARL
     AYKVYIQQLR RFIGSYMISL GRIDAITFTA GVGENDDAVR ADALADLENF GIKIDLEANA
     VRADGAREIS TPDSTIKVFV VPTNEELAIA RYAKTIAESV
//
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