ID ACKA_CORGL Reviewed; 397 AA.
AC P77845;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 01-MAY-2013, entry version 85.
DE RecName: Full=Acetate kinase;
DE EC=2.7.2.1;
DE AltName: Full=Acetokinase;
GN Name=ackA; Synonyms=ack; OrderedLocusNames=Cgl2752, cg3047;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 /
OS LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX PubMed=10075432;
RA Reinscheid D.J., Schnicke S., Rittmann D., Zahnow U., Sahm H.,
RA Eikmanns B.J.;
RT "Cloning, sequence analysis, expression and inactivation of the
RT Corynebacterium glutamicum pta-ack operon encoding
RT phosphotransacetylase and acetate kinase.";
RL Microbiology 145:503-513(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
RX PubMed=12948626; DOI=10.1016/S0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M.,
RA Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L.,
RA Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B.,
RA McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A.,
RA Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I.,
RA Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence
RT and its impact on the production of L-aspartate-derived amino acids
RT and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate
CC and ATP. Can also catalyze the reverse reaction (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate.
CC -!- COFACTOR: Mg(2+). Can also accept Mn(2+) (By similarity).
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA
CC biosynthesis; acetyl-CoA from acetate: step 1/2.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the acetokinase family.
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DR EMBL; X89084; CAA61456.1; -; Genomic_DNA.
DR EMBL; BA000036; BAC00146.1; -; Genomic_DNA.
DR EMBL; BX927156; CAF20774.1; -; Genomic_DNA.
DR RefSeq; NP_601947.1; NC_003450.3.
DR RefSeq; YP_226990.1; NC_006958.1.
DR ProteinModelPortal; P77845; -.
DR STRING; 196627.cg3047; -.
DR World-2DPAGE; 0001:P77845; -.
DR EnsemblBacteria; BAC00146; BAC00146; BAC00146.
DR EnsemblBacteria; CAF20774; CAF20774; cg3047.
DR GeneID; 1020697; -.
DR GeneID; 3344522; -.
DR KEGG; cgb:cg3047; -.
DR KEGG; cgl:NCgl2656; -.
DR PATRIC; 21497542; VBICorGlu203724_2683.
DR eggNOG; COG0282; -.
DR HOGENOM; HOG000288398; -.
DR KO; K00925; -.
DR OMA; MIARDTA; -.
DR ProtClustDB; PRK00180; -.
DR BioCyc; CGLU196627:GJDM-2735-MONOMER; -.
DR UniPathway; UPA00340; UER00458.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008776; F:acetate kinase activity; IEA:HAMAP.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1 397 Acetate kinase.
FT /FTId=PRO_0000107553.
FT NP_BIND 209 213 ATP (By similarity).
FT NP_BIND 283 285 ATP (By similarity).
FT NP_BIND 331 335 ATP (By similarity).
FT ACT_SITE 149 149 Proton donor/acceptor (By similarity).
FT METAL 8 8 Magnesium (By similarity).
FT METAL 385 385 Magnesium (By similarity).
FT BINDING 15 15 ATP (By similarity).
FT BINDING 92 92 Substrate (By similarity).
FT SITE 181 181 Transition state stabilizer (By
FT similarity).
FT SITE 242 242 Transition state stabilizer (By
FT similarity).
SQ SEQUENCE 397 AA; 43092 MW; 248FF97A3C52B0E4 CRC64;
MALALVLNSG SSSIKFQLVN PENSAIDEPY VSGLVEQIGE PNGRIVLKIE GEKYTLETPI
ADHSEGLNLA FDLMDQHNCG PSQLEITAVG HRVVHGGILF SAPELITDEI VEMIRDLIPL
APLHNPANVD GIDVARKILP DVPHVAVFDT GFFHSLPPAA ALYAINKDVA AEHGIRRYGF
HGTSHEFVSK RVVEILEKPT EDINTITFHL GNGASMAAVQ GGRAVDTSMG MTPLAGLVMG
TRSGDIDPGI VFHLSRTAGM SIDEIDNLLN KKSGVKGLSG VNDFRELREM IDNNDQDAWS
AYNIYIHQLR RYLGSYMVAL GRVDTIVFTA GVGENAQFVR EDALAGLEMY GIEIDPERNA
LPNDGPRLIS TDASKVKVFV IPTNEELAIA RYAVKFA
//
