Reviewed, UniProtKB/Swiss-Prot P38503 (PTA_METTE)

Names and origin

Protein names

Recommended name:
    Phosphate acetyltransferase
    EC=2.3.1.8
Alternative name(s):
    Phosphotransacetylase

Gene names

Name:

pta

Organism

Methanosarcina thermophila

Taxonomic identifier

2210 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Acetyl-CoA + phosphate = CoA + acetyl phosphate.
Pathway	Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 2/2.
Subunit structure	Homodimer. Ref.3
Subcellular location	Cell membrane; Peripheral membrane protein.
Sequence similarities	Belongs to the phosphate acetyltransferase and butyryltransferase family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	phosphate acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 333

332

Phosphate acetyltransferase

PRO_0000179151

Experimental info

Mutagenesis

159

1

C → A: Loss of activity.

Mutagenesis

159

1

C → S: No loss of activity.

Secondary structure

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333

Helix Strand Turn

Details...

Helix

3 – 15

13

Beta strand

18 – 21

4

Helix

27 – 39

13

Beta strand

43 – 48

6

Helix

50 – 57

8

Beta strand

65 – 68

4

Helix

76 – 87

12

Helix

88 – 90

3

Helix

94 – 100

7

Helix

104 – 113

10

Beta strand

118 – 122

5

Helix

129 – 138

10

Beta strand

149 – 155

7

Beta strand

166 – 170

5

Beta strand

172 – 174

3

Helix

180 – 198

19

Beta strand

203 – 207

5

Helix

218 – 233

16

Beta strand

237 – 243

7

Helix

245 – 249

5

Helix

251 – 257

7

Beta strand

269 – 271

3

Helix

275 – 287

13

Beta strand

292 – 303

12

Beta strand

305 – 307

3

Helix

314 – 332

19

Sequences

	Sequence		Length	Mass (Da)
	P38503-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: EC87B47A387B8398	FASTA	333	35,220
	10 20 30 40 50 60 MVTFLEKISE RAKKLNKTIA LPETEDIRTL QAAAKILERG IADIVLVGNE ADIKALAGDL 70 80 90 100 110 120 DLSKAKIVDP KTYEKKDEYI NAFYELRKHK GITLENAAEI MSDYVYFAVM MAKLGEVDGV 130 140 150 160 170 180 VSGAAHSSSD TLRPAVQIVK TAKGAALASA FFIISVPDCE YGSDGTFLFA DSGMVEMPSV 190 200 210 220 230 240 EDVANIAVIS AKTFELLVQD VPKVAMLSYS TKGSAKSKLT EATIASTKLA QELAPDIAID 250 260 270 280 290 300 GELQVDAAIV PKVAASKAPG SPVAGKANVF IFPDLNCGNI AYKIAQRLAK AEAYGPITQG 310 320 330 LAKPINDLSR GCSDEDIVGA VAITCVQAAA QDK

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], PROTEIN SEQUENCE OF 2-21. Strain: DSM 1825 / TM-1.
[2]	"Identification of cysteine and arginine residues essential for the phosphotransacetylase from Methanosarcina thermophila." Rasche M.E., Smith K.S., Ferry J.G. J. Bacteriol. 179:7712-7717(1997) [PubMed: 9401029] [Abstract] Cited for: MUTAGENESIS.
[3]	"Crystal structure of phosphotransacetylase from the methanogenic archaeon Methanosarcina thermophila." Iyer P.P., Lawrence S.H., Luther K.B., Rajashankar K.R., Yennawar H.P., Ferry J.G., Schindelin H. Structure 12:559-567(2004) [PubMed: 15062079] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L23147 Unassigned DNA. Translation: AAA72041.1.

PIR

A49338.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QZT	X-ray	2.70	A/B/C/D	1-333	[»]
2AF3	X-ray	2.60	C/D	1-333	[»]
2AF4	X-ray	2.15	C/D	1-333	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

2.3.1.8. 8918.

Family and domain databases

InterPro

IPR012147. P_Ac_Bu_trans.
IPR004614. P_AcTrfase.
IPR002505. PTA_PTB.
[Graphical view]

Pfam

PF01515. PTA_PTB. 1 hit.
[Graphical view]

PIRSF

PIRSF000428. P_Ac_trans. 1 hit.

TIGRFAMs

TIGR00651. pta. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PTA_METTE

Accession

Primary (citable) accession number: P38503

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 64 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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