Q8K9W6 (ACKA_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetate kinase
EC=2.7.2.1

Alternative name(s):
Acetokinase

Gene names

Name:	ackA
Ordered Locus Names:	BUsg_169

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction By similarity. HAMAP-Rule MF_00020
Catalytic activity	ATP + acetate = ADP + acetyl phosphate. HAMAP-Rule MF_00020
Cofactor	Mg2+. Can also accept Mn2+ By similarity.
Pathway	Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2. HAMAP-Rule MF_00020
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the acetokinase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway organic acid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetate kinase activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 403	403	Acetate kinase HAMAP-Rule MF_00020		PRO_0000107539
Regions
	Nucleotide binding	213 – 217	5	ATP By similarity
	Nucleotide binding	288 – 290	3	ATP By similarity
	Nucleotide binding	336 – 340	5	ATP By similarity
Sites
	Active site	153	1	Proton donor/acceptor By similarity
	Metal binding	13	1	Magnesium By similarity
	Metal binding	390	1	Magnesium By similarity
	Binding site	20	1	ATP By similarity
	Binding site	94	1	Substrate By similarity
	Site	185	1	Transition state stabilizer By similarity
	Site	246	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8K9W6 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 408D7ABED18A8FA5	FASTA	403	45,211
	10 20 30 40 50 60 MVKILNNLIF VLNCGSSSVK FAILNPDNKK KYLSGLVECL FLSKTYMKWK DLTTEHKKCI 70 80 90 100 110 120 GSNLSHKDAL NFIFNKFFLE KKDIYKNIVG IGHRVVHGGN KIKSSTLIDD NIIQLIQKAI 130 140 150 160 170 180 SFAPLHNPAN LIGIKTAIEK FPIFAKKNVA VFDTSFYQNM PETSFLYAIP YFFYKEHHIR 190 200 210 220 230 240 RYGAHGTSHH YVASEVALIL NKNFNSLNVI TCHLGNGASV SAVCNGICVD TSMGLTPLEG 250 260 270 280 290 300 LVMGTRSGDI DPSIIFFMYQ KLGMSIDEIH TILTKESGLL GLSGISSDFR YFEKKYYFEK 310 320 330 340 350 360 KARLAVDIFC HRLSKYIASY MSLMENNLDA IVFTGGIGEN VPLIREITLS KLLLIGFKID 370 380 390 400 TQRNLGIKNG KHGLITTDKS RPAFVIPTDE ELAIAQETIK IIK

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. Translation: AAM67736.1.
RefSeq	NP_660525.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q8K9W6.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg169.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM67736; AAM67736; BUsg_169.
GeneID	1005366.
KEGG	bas:BUsg169.
PATRIC	21247119. VBIBucAph100086_0173.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0282.
KO	K00925.
OMA	IDHERNL.
ProtClustDB	PRK00180.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-238-MONOMER.
UniPathway	UPA00340; UER00458.
Family and domain databases
HAMAP	MF_00020. Acetate_kinase.
InterPro	IPR004372. Ac/Proprionate_kinase. IPR000890. Aliphatic_acid_kin_short-chain. IPR023865. Aliphatic_acid_kinase_CS. [Graphical view]
PANTHER	PTHR21060. PTHR21060. 1 hit.
Pfam	PF00871. Acetate_kinase. 1 hit. [Graphical view]
PIRSF	PIRSF000722. Acetate_prop_kin. 1 hit.
PRINTS	PR00471. ACETATEKNASE.
TIGRFAMs	TIGR00016. ackA. 1 hit.
PROSITE	PS01075. ACETATE_KINASE_1. False negative. PS01076. ACETATE_KINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACKA_BUCAP

Accession

Primary (citable) accession number: Q8K9W6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program