ACKA_CORGL
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 03-AUG-2022, entry version 126.
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}; Synonyms=ack;
GN OrderedLocusNames=Cgl2752, cg3047;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=10075432; DOI=10.1099/13500872-145-2-503;
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 phosphotransacetylase
RT and acetate kinase.";
RL Microbiology 145:503-513(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 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 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=15090522; DOI=10.1128/jb.186.9.2798-2809.2004;
RA Gerstmeir R., Cramer A., Dangel P., Schaffer S., Eikmanns B.J.;
RT "RamB, a novel transcriptional regulator of genes involved in acetate
RT metabolism of Corynebacterium glutamicum.";
RL J. Bacteriol. 186:2798-2809(2004).
RN [5]
RP INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=16547043; DOI=10.1128/jb.188.7.2554-2567.2006;
RA Cramer A., Gerstmeir R., Schaffer S., Bott M., Eikmanns B.J.;
RT "Identification of RamA, a novel LuxR-type transcriptional regulator of
RT genes involved in acetate metabolism of Corynebacterium glutamicum.";
RL J. Bacteriol. 188:2554-2567(2006).
RN [6]
RP INDUCTION.
RX PubMed=18355281; DOI=10.1111/j.1574-6968.2008.01098.x;
RA Jungwirth B., Emer D., Brune I., Hansmeier N., Puehler A., Eikmanns B.J.,
RA Tauch A.;
RT "Triple transcriptional control of the resuscitation promoting factor 2
RT (rpf2) gene of Corynebacterium glutamicum by the regulators of acetate
RT metabolism RamA and RamB and the cAMP-dependent regulator GlxR.";
RL FEMS Microbiol. Lett. 281:190-197(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.
CC -!- INDUCTION: Activated by RamA and repressed by RamB and GlxR.
CC {ECO:0000269|PubMed:15090522, ECO:0000269|PubMed:16547043,
CC ECO:0000269|PubMed:18355281}.
CC -!- SIMILARITY: Belongs to the acetokinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00020}.
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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; WP_003862874.1; NC_006958.1.
DR AlphaFoldDB; P77845; -.
DR SMR; P77845; -.
DR STRING; 196627.cg3047; -.
DR World-2DPAGE; 0001:P77845; -.
DR KEGG; cgb:cg3047; -.
DR KEGG; cgl:Cgl2752; -.
DR PATRIC; fig|196627.13.peg.2683; -.
DR eggNOG; COG0282; Bacteria.
DR HOGENOM; CLU_020352_0_1_11; -.
DR OMA; KIITCHI; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000000582; 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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..397
FT /note="Acetate kinase"
FT /id="PRO_0000107553"
FT ACT_SITE 149
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT BINDING 209..213
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 181
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
FT SITE 242
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00020"
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
