P07097 (THIL_ZOORA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetyl-CoA acetyltransferase
EC=2.3.1.9

Alternative name(s):
Acetoacetyl-CoA thiolase

Gene names

Name:

phbA

Organism

Zoogloea ramigera

Taxonomic identifier

350 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Zoogloea

Protein attributes

Sequence length	392 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	2 acetyl-CoA = CoA + acetoacetyl-CoA.
Pathway	Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Biological process	PHB biosynthesis
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	poly-hydroxybutyrate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acetyl-CoA C-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

Chain

2 – 392

391

Acetyl-CoA acetyltransferase

PRO_0000206463

Sites

Active site

89

1

Acyl-thioester intermediate

Active site

348

1

Proton acceptor

Active site

378

1

Proton acceptor

Experimental info

Mutagenesis

64

1

Q → A: Slightly lower activity. Ref.6

Mutagenesis

89

1

C → A: Loss of activity. Ref.6

Mutagenesis

378

1

C → G: Loss of activity. Ref.3

Secondary structure

1

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392

Helix Strand Turn

Details...

Beta strand

6 – 12

7

Turn

21 – 24

4

Helix

27 – 42

16

Helix

46 – 48

3

Beta strand

51 – 55

5

Helix

66 – 73

8

Beta strand

80 – 86

7

Helix

88 – 90

3

Helix

91 – 104

14

Beta strand

111 – 119

9

Beta strand

124 – 126

3

Beta strand

133 – 135

3

Beta strand

137 – 141

5

Helix

142 – 147

6

Turn

151 – 153

3

Helix

157 – 168

12

Helix

172 – 192

21

Turn

193 – 198

6

Beta strand

202 – 204

3

Beta strand

211 – 213

3

Helix

225 – 229

5

Beta strand

234 – 236

3

Beta strand

243 – 246

4

Beta strand

250 – 260

11

Helix

261 – 267

7

Beta strand

272 – 282

11

Helix

285 – 290

6

Helix

292 – 303

12

Helix

307 – 309

3

Beta strand

311 – 315

5

Helix

320 – 330

11

Helix

334 – 336

3

Helix

343 – 346

4

Helix

350 – 352

3

Helix

353 – 368

16

Beta strand

371 – 379

9

Turn

380 – 382

3

Beta strand

383 – 390

8

Sequences

	Sequence		Length	Mass (Da)
	P07097 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 88A6298751A42B7E	FASTA	392	40,473
	10 20 30 40 50 60 MSTPSIVIAS ARTAVGSFNG AFANTPAHEL GATVISAVLE RAGVAAGEVN EVILGQVLPA 70 80 90 100 110 120 GEGQNPARQA AMKAGVPQEA TAWGMNQLCG SGLRAVALGM QQIATGDASI IVAGGMESMS 130 140 150 160 170 180 MAPHCAHLAG GVKMGDFKMI DTMIKDGLTD AFYGYHMGTT AENVAKQWQL SRDEQDAFAV 190 200 210 220 230 240 ASQNKAEAAQ KDGRFKDEIV PFIVKGRKGD ITVDADEYIR HGATLDSMAK LRPAFDKEGT 250 260 270 280 290 300 VTAGNASGLN DGAAAALLMS EAEASRRGIQ PLGRIVSWAT VGVDPKVMGT GPIPASRKAL 310 320 330 340 350 360 ERAGWKIGDL DLVEANEAFA AQACAVNKDL GWDPSIVNVN GGAIAIGHPI GASGARILNT 370 380 390 LLFEMKRRGA RKGLATLCIG GGMGVAMCIE SL

References

[1]	"Biosynthetic thiolase from Zoogloea ramigera. III. Isolation and characterization of the structural gene." Peoples O.P., Masamune S., Walsh C.T., Sinskey A.J. J. Biol. Chem. 262:97-102(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 19623 / I-16-M / NCIB 10340 / NCTC 10482.
[2]	"Poly-beta-hydroxybutyrate biosynthesis in Alcaligenes eutrophus H16. Characterization of the genes encoding beta-ketothiolase and acetoacetyl-CoA reductase." Peoples O.P., Sinskey A.J. J. Biol. Chem. 264:15293-15297(1989) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 131.
[3]	"Biosynthetic thiolase from Zoogloea ramigera. Evidence for a mechanism involving Cys-378 as the active site base." Palmer M.A.J., Differding E., Gamboni R., Williams S.F., Peoples O.P., Walsh C.T., Sinskey S.J., Masamune S. J. Biol. Chem. 266:8369-8375(1991) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-378.
[4]	"Crystallographic analysis of the reaction pathway of Zoogloea ramigera biosynthetic thiolase." Modis Y., Wierenga R.K. J. Mol. Biol. 297:1171-1182(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
[5]	"A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism." Modis Y., Wierenga R.K. Structure 7:1279-1290(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF THE THIOESTER INTERMEDIATE AND OF COMPLEX WITH SUBSTRATE.
[6]	"The catalytic cycle of biosynthetic thiolase: a conformational journey of an acetyl group through four binding modes and two oxyanion holes." Kursula P., Ojala J., Lambeir A.-M., Wierenga R.K. Biochemistry 41:15543-15556(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF THE THIOESTER INTERMEDIATE; OF COMPLEX WITH SUBSTRATE AND OF MUTANTS ALA-64 AND ALA-89, MUTAGENESIS OF GLN-64 AND CYS-89.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J02631 Genomic DNA. Translation: AAA27706.1. Sequence problems.

PIR

XXGZAC. A26121.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DLU	X-ray	2.25	A/B/C/D	11-392	[»]
1DLV	X-ray	2.29	A/B/C/D	11-392	[»]
1DM3	X-ray	2.00	A/B/C/D	11-392	[»]
1M1O	X-ray	1.95	A/B/C/D	11-392	[»]
1M1T	X-ray	1.94	A/B/C/D	11-392	[»]
1M3K	X-ray	1.70	A/B/C/D	11-392	[»]
1M3Z	X-ray	1.87	A/B/C/D	11-392	[»]
1M4S	X-ray	1.87	A/B/C/D	11-392	[»]
1M4T	X-ray	1.77	A/B/C/D	11-392	[»]
1NL7	X-ray	1.90	A/B/C/D	11-391	[»]
1OU6	X-ray	2.07	A/B/C/D	11-391	[»]
1QFL	X-ray	1.92	A/B/C/D	11-392	[»]
2VTZ	X-ray	2.30	A/B/C/D	2-392	[»]
2VU0	X-ray	1.87	A/B/C/D	11-392	[»]
2VU1	X-ray	1.51	A/B/C/D	2-392	[»]
2VU2	X-ray	2.65	A/B/C/D	2-392	[»]
2WKT	X-ray	2.00	A/B/C/D	11-392	[»]
2WKU	X-ray	2.30	A/B/C/D	11-392	[»]
2WKV	X-ray	2.50	A/B/C/D	11-392	[»]
2WL4	X-ray	1.80	A/B/C/D	11-392	[»]
2WL5	X-ray	1.80	A/B/C/D	11-392	[»]
2WL6	X-ray	2.98	A/B/C/D	11-392	[»]

ProteinModelPortal

P07097.

SMR

P07097. Positions 5-392.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P07097.

UniPathway

UPA00058; UER00101.

Family and domain databases

Gene3D

3.40.47.10. 4 hits.

InterPro

IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]

PANTHER

PTHR18919. PTHR18919. 1 hit.

Pfam

PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000429. Ac-CoA_Ac_transf. 1 hit.

SUPFAM

SSF53901. Thiolase-like. 2 hits.

TIGRFAMs

TIGR01930. AcCoA-C-Actrans. 1 hit.

PROSITE

PS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07097.

Entry information

Entry name

THIL_ZOORA

Accession

Primary (citable) accession number: P07097

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 100 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program