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Protein

Acetyl-CoA acetyltransferase

Gene

phbA

Organism
Zoogloea ramigera
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 acetyl-CoA = CoA + acetoacetyl-CoA.PROSITE-ProRule annotation

Pathwayi: (R)-mevalonate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (R)-mevalonate from acetyl-CoA.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Acetyl-CoA acetyltransferase (phbA)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway (R)-mevalonate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-mevalonate from acetyl-CoA, the pathway (R)-mevalonate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei89Acyl-thioester intermediate1
Active sitei348Proton acceptor1
Active sitei378Proton acceptor1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

PHB biosynthesis

Enzyme and pathway databases

BRENDAi2.3.1.9. 6758.
SABIO-RKP07097.
UniPathwayiUPA00058; UER00101.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA acetyltransferase (EC:2.3.1.9)
Alternative name(s):
Acetoacetyl-CoA thiolase
Gene namesi
Name:phbA
OrganismiZoogloea ramigera
Taxonomic identifieri350 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeZoogloea

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi64Q → A: Slightly lower activity. 1 Publication1
Mutagenesisi89C → A: Loss of activity. 1 Publication1
Mutagenesisi378C → G: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00002064632 – 392Acetyl-CoA acetyltransferaseAdd BLAST391

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1392
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 12Combined sources7
Turni21 – 24Combined sources4
Helixi27 – 42Combined sources16
Helixi46 – 48Combined sources3
Beta strandi51 – 55Combined sources5
Helixi66 – 73Combined sources8
Beta strandi80 – 86Combined sources7
Helixi88 – 90Combined sources3
Helixi91 – 104Combined sources14
Beta strandi111 – 119Combined sources9
Beta strandi124 – 126Combined sources3
Beta strandi133 – 135Combined sources3
Beta strandi137 – 141Combined sources5
Helixi142 – 147Combined sources6
Turni151 – 153Combined sources3
Helixi157 – 168Combined sources12
Helixi172 – 192Combined sources21
Turni193 – 198Combined sources6
Beta strandi202 – 204Combined sources3
Beta strandi211 – 213Combined sources3
Helixi225 – 229Combined sources5
Beta strandi233 – 235Combined sources3
Beta strandi243 – 246Combined sources4
Beta strandi250 – 260Combined sources11
Helixi261 – 267Combined sources7
Beta strandi272 – 282Combined sources11
Helixi285 – 290Combined sources6
Helixi292 – 303Combined sources12
Helixi307 – 309Combined sources3
Beta strandi311 – 315Combined sources5
Helixi320 – 330Combined sources11
Helixi334 – 336Combined sources3
Helixi343 – 346Combined sources4
Helixi350 – 352Combined sources3
Helixi353 – 368Combined sources16
Beta strandi371 – 379Combined sources9
Turni380 – 382Combined sources3
Beta strandi383 – 390Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DLUX-ray2.25A/B/C/D5-392[»]
1DLVX-ray2.29A/B/C/D5-392[»]
1DM3X-ray2.00A/B/C/D5-392[»]
1M1OX-ray1.95A/B/C/D2-392[»]
1M1TX-ray1.94A/B/C/D2-392[»]
1M3KX-ray1.70A/B/C/D2-392[»]
1M3ZX-ray1.87A/B/C/D2-392[»]
1M4SX-ray1.87A/B/C/D2-392[»]
1M4TX-ray1.77A/B/C/D2-392[»]
1NL7X-ray1.90A/B/C/D2-392[»]
1OU6X-ray2.07A/B/C/D2-392[»]
1QFLX-ray1.92A/B/C/D5-392[»]
2VTZX-ray2.30A/B/C/D2-392[»]
2VU0X-ray1.87A/B/C/D2-392[»]
2VU1X-ray1.51A/B/C/D12-392[»]
2VU2X-ray2.65A/B/C/D2-392[»]
2WKTX-ray2.00A/B/C/D2-392[»]
2WKUX-ray2.30A/B/C/D2-392[»]
2WKVX-ray2.50A/B/C/D2-392[»]
2WL4X-ray1.80A/B/C/D2-392[»]
2WL5X-ray1.80A/B/C/D2-392[»]
2WL6X-ray2.98A/B/C/D2-392[»]
ProteinModelPortaliP07097.
SMRiP07097.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07097.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07097-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTPSIVIAS ARTAVGSFNG AFANTPAHEL GATVISAVLE RAGVAAGEVN
60 70 80 90 100
EVILGQVLPA GEGQNPARQA AMKAGVPQEA TAWGMNQLCG SGLRAVALGM
110 120 130 140 150
QQIATGDASI IVAGGMESMS MAPHCAHLAG GVKMGDFKMI DTMIKDGLTD
160 170 180 190 200
AFYGYHMGTT AENVAKQWQL SRDEQDAFAV ASQNKAEAAQ KDGRFKDEIV
210 220 230 240 250
PFIVKGRKGD ITVDADEYIR HGATLDSMAK LRPAFDKEGT VTAGNASGLN
260 270 280 290 300
DGAAAALLMS EAEASRRGIQ PLGRIVSWAT VGVDPKVMGT GPIPASRKAL
310 320 330 340 350
ERAGWKIGDL DLVEANEAFA AQACAVNKDL GWDPSIVNVN GGAIAIGHPI
360 370 380 390
GASGARILNT LLFEMKRRGA RKGLATLCIG GGMGVAMCIE SL
Length:392
Mass (Da):40,473
Last modified:January 23, 2007 - v4
Checksum:i88A6298751A42B7E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02631 Genomic DNA. Translation: AAA27706.1. Sequence problems.
PIRiA26121. XXGZAC.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02631 Genomic DNA. Translation: AAA27706.1. Sequence problems.
PIRiA26121. XXGZAC.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DLUX-ray2.25A/B/C/D5-392[»]
1DLVX-ray2.29A/B/C/D5-392[»]
1DM3X-ray2.00A/B/C/D5-392[»]
1M1OX-ray1.95A/B/C/D2-392[»]
1M1TX-ray1.94A/B/C/D2-392[»]
1M3KX-ray1.70A/B/C/D2-392[»]
1M3ZX-ray1.87A/B/C/D2-392[»]
1M4SX-ray1.87A/B/C/D2-392[»]
1M4TX-ray1.77A/B/C/D2-392[»]
1NL7X-ray1.90A/B/C/D2-392[»]
1OU6X-ray2.07A/B/C/D2-392[»]
1QFLX-ray1.92A/B/C/D5-392[»]
2VTZX-ray2.30A/B/C/D2-392[»]
2VU0X-ray1.87A/B/C/D2-392[»]
2VU1X-ray1.51A/B/C/D12-392[»]
2VU2X-ray2.65A/B/C/D2-392[»]
2WKTX-ray2.00A/B/C/D2-392[»]
2WKUX-ray2.30A/B/C/D2-392[»]
2WKVX-ray2.50A/B/C/D2-392[»]
2WL4X-ray1.80A/B/C/D2-392[»]
2WL5X-ray1.80A/B/C/D2-392[»]
2WL6X-ray2.98A/B/C/D2-392[»]
ProteinModelPortaliP07097.
SMRiP07097.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00058; UER00101.
BRENDAi2.3.1.9. 6758.
SABIO-RKP07097.

Miscellaneous databases

EvolutionaryTraceiP07097.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHIL_ZOORA
AccessioniPrimary (citable) accession number: P07097
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 114 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.