Reviewed, UniProtKB/Swiss-Prot P38502 (ACKA_METTE)

Names and origin

Protein names

Recommended name:
    Acetate kinase
    EC=2.7.2.1
Alternative name(s):
    Acetokinase

Gene names

Name:	ackA
Synonyms:	ack

Organism

Methanosarcina thermophila

Taxonomic identifier

2210 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	408 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + acetate = ADP + acetyl phosphate. ATP + propanoate = ADP + propanoyl phosphate.
Enzyme regulation	Inhibited by diethylpyrocarbonate and phenylglyoxal.
Pathway	Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2.
Subunit structure	Homodimer.
Subcellular location	CytoplasmBy similarity.
Sequence similarities	Belongs to the acetokinase family.
Biophysicochemical properties	Temperature dependence: Optimum temperature is 65 degrees Celsius. Protected from thermal inactivation by ATP.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Kinase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	phosphorylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	acetate kinase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 408

408

Acetate kinase

Secondary structure

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408

Helix Strand Turn

Details...

Beta strand

2 – 8

7

Beta strand

13 – 19

7

Turn

20 – 23

4

Beta strand

24 – 33

10

Beta strand

36 – 38

3

Beta strand

40 – 45

6

Beta strand

50 – 54

5

Helix

60 – 71

12

Turn

74 – 76

3

Helix

82 – 84

3

Beta strand

87 – 93

7

Turn

96 – 98

3

Helix

107 – 115

9

Helix

117 – 119

3

Turn

121 – 123

3

Helix

124 – 137

14

Beta strand

143 – 147

5

Helix

150 – 154

5

Helix

157 – 160

4

Helix

166 – 172

7

Helix

181 – 195

15

Helix

199 – 201

3

Beta strand

203 – 219

17

Beta strand

222 – 227

6

Beta strand

234 – 236

3

Helix

249 – 257

9

Helix

261 – 270

10

Helix

273 – 278

6

Helix

284 – 292

9

Helix

296 – 319

24

Beta strand

324 – 329

6

Helix

330 – 335

6

Helix

337 – 344

8

Helix

348 – 350

3

Helix

358 – 360

3

Beta strand

374 – 379

6

Helix

384 – 397

14

Sequences

	Sequence		Length	Mass (Da)
	P38502-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 1A484DF8A7258800	FASTA	408	44,337
	10 20 30 40 50 60 MKVLVINAGS SSLKYQLIDM TNESALAVGL CERIGIDNSI ITQKKFDGKK LEKLTDLPTH 70 80 90 100 110 120 KDALEEVVKA LTDDEFGVIK DMGEINAVGH RVVHGGEKFT TSALYDEGVE KAIKDCFELA 130 140 150 160 170 180 PLHNPPNMMG ISACAEIMPG TPMVIVFDTA FHQTMPPYAY MYALPYDLYE KHGVRKYGFH 190 200 210 220 230 240 GTSHKYVAER AALMLGKPAE ETKIITCHLG NGSSITAVEG GKSVETSMGF TPLEGLAMGT 250 260 270 280 290 300 RCGSIDPAIV PFLMEKEGLT TREIDTLMNK KSGVLGVSGL SNDFRDLDEA ASKGNRKAEL 310 320 330 340 350 360 ALEIFAYKVK KFIGEYSAVL NGADAVVFTA GIGENSASIR KRILTGLDGI GIKIDDEKNK 370 380 390 400 IRGQEIDIST PDAKVRVFVI PTNEELAIAR ETKEIVETEV KLRSSIPV

References

[1]	"Cloning, sequence analysis, and hyperexpression of the genes encoding phosphotransacetylase and acetate kinase from Methanosarcina thermophila." Latimer M.T., Ferry J.G. J. Bacteriol. 175:6822-6829(1993) [PubMed: 8226623] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 1825 / TM-1.
[2]	"Purification and characterization of acetate kinase from acetate-grown Methanosarcina thermophila. Evidence for regulation of synthesis." Aceti D.J., Ferry J.G. J. Biol. Chem. 263:15444-15448(1988) [PubMed: 2844814] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-17.
[3]	"Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases." Buss K.A., Cooper D.R., Ingram-Smith C., Ferry J.G., Sanders D.A., Hasson M.S. J. Bacteriol. 183:680-686(2001) [PubMed: 11133963] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 9-408.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L23147 Unassigned DNA. Translation: AAA72042.1.

PIR

B49338.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G99	X-ray	2.50	A/B	1-408	[»]
1TUU	X-ray	2.50	A/B	1-399	[»]
1TUY	X-ray	3.00	A/B	1-399	[»]

ModBase

Search...

Family and domain databases

HAMAP

MF_00020.
[Tree]

InterPro

IPR000890. Acetate_kin.
IPR004372. AckA.
[Graphical view]

PANTHER

PTHR21060. Acetate_kin. 1 hit.
PTHR21060:SF11. AckA. 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. 1 hit.
PS01076. ACETATE_KINASE_2. 1 hit.
[Graphical view]

ProDom

P38502.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

DrugBank

DB00131. Adenosine monophosphate.

ProtoNet

Search...

Entry information

Entry name

ACKA_METTE

Accession

Primary (citable) accession number: P38502

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	July 22, 2008
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)