[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; PubMed=10075432 [NCBI, ExPASy, EBI, Israel, Japan] Reinscheid D.J., Schnicke S., Rittmann D., Zahnow U., Sahm H., Eikmanns B.J.; "Cloning, sequence analysis, expression and inactivation of the Corynebacterium glutamicum pta-ack operon encoding phosphotransacetylase and acetate kinase."; Microbiology 145:503-513(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; Nakagawa S.; "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; DOI=10.1016/S0168-1656(03)00154-8; PubMed=12948626 [NCBI, ExPASy, EBI, Israel, Japan] Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.; "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."; J. Biotechnol. 104:5-25(2003).

Comments

FUNCTION: Involved in the activation of acetate to acetyl CoA and the secretion of acetate (By similarity).
CATALYTIC ACTIVITY: ATP + acetate = ADP + acetyl phosphate.
CATALYTIC ACTIVITY: ATP + propanoate = ADP + propanoyl phosphate.
PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2 .
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the acetokinase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X89084; CAA61456.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000036; BAC00146.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX927156; CAF20774.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_601947.1; -.
YP_226990.1; -.

3D structure databases

HSSP

P38502; 1G99. [HSSP ENTRY / PDB]

ModBase

P77845.

Enzyme and pathway databases

BioCyc

CGLU196627-1:CG3047-MON; -.

2D gel databases

World-2DPAGE

0001:P77845; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0008776;	Molecular function: acetate kinase activity (inferred from electronic annotation from HAMAP).
GO:0016310;	Biological process: phosphorylation (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00020; -; 1.
PBIL [Tree]

InterPro

IPR000890; Acetate_kin.
IPR004372; AckA.
Graphical view of domain structure.

PANTHER

PTHR21060; Acetate_kin; 1.
PTHR21060:SF11; AckA; 1.

Pfam

PF00871; Acetate_kinase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000722; Acetate_prop_kin; 1.

PRINTS

PR00471; ACETATEKNASE.

TIGRFAMs

TIGR00016; ackA; 1.

PROSITE

PS01075; ACETATE_KINASE_1; 1.
PS01076; ACETATE_KINASE_2; 1.

BLOCKS

P77845.

Genome annotation databases

GeneID

1020697; -.
3344522; -.

GenomeReviews

BX927147_GR; cg3047.
BA000036_GR; Cgl2752.

KEGG

cgb:cg3047; -.
cgl:NCgl2656; -.

Phylogenomic databases

HOGENOM

P77845; -.

Genome annotation databases

CMR

P77845; Cgl2752.

Other

ProtoNet

P77845.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Kinase; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 397`	`397`		`Acetate kinase.`	`PRO_0000107553`

Sequence information

Length: 397 AA [This is the length of the unprocessed precursor]

Molecular weight: 43092 Da [This is the MW of the unprocessed precursor]

CRC64: 248FF97A3C52B0E4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALALVLNSG SSSIKFQLVN PENSAIDEPY VSGLVEQIGE PNGRIVLKIE GEKYTLETPI 

        70         80         90        100        110        120 
ADHSEGLNLA FDLMDQHNCG PSQLEITAVG HRVVHGGILF SAPELITDEI VEMIRDLIPL 

       130        140        150        160        170        180 
APLHNPANVD GIDVARKILP DVPHVAVFDT GFFHSLPPAA ALYAINKDVA AEHGIRRYGF 

       190        200        210        220        230        240 
HGTSHEFVSK RVVEILEKPT EDINTITFHL GNGASMAAVQ GGRAVDTSMG MTPLAGLVMG 

       250        260        270        280        290        300 
TRSGDIDPGI VFHLSRTAGM SIDEIDNLLN KKSGVKGLSG VNDFRELREM IDNNDQDAWS 

       310        320        330        340        350        360 
AYNIYIHQLR RYLGSYMVAL GRVDTIVFTA GVGENAQFVR EDALAGLEMY GIEIDPERNA 

       370        380        390 
LPNDGPRLIS TDASKVKVFV IPTNEELAIA RYAVKFA

P77845 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools