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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei89 – 891Acyl-thioester intermediate
Active sitei348 – 3481Proton acceptor
Active sitei378 – 3781Proton acceptor

GO - Molecular functioni

  1. acetyl-CoA C-acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. poly-hydroxybutyrate biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

PHB biosynthesis

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-4110-MONOMER.
RETL1328306-WGS:GSTH-6457-MONOMER.
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

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi64 – 641Q → A: Slightly lower activity. 1 Publication
Mutagenesisi89 – 891C → A: Loss of activity. 1 Publication
Mutagenesisi378 – 3781C → G: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 392391Acetyl-CoA acetyltransferasePRO_0000206463Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
392
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127Combined sources
Turni21 – 244Combined sources
Helixi27 – 4216Combined sources
Helixi46 – 483Combined sources
Beta strandi51 – 555Combined sources
Helixi66 – 738Combined sources
Beta strandi80 – 867Combined sources
Helixi88 – 903Combined sources
Helixi91 – 10414Combined sources
Beta strandi111 – 1199Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi137 – 1415Combined sources
Helixi142 – 1476Combined sources
Turni151 – 1533Combined sources
Helixi157 – 16812Combined sources
Helixi172 – 19221Combined sources
Turni193 – 1986Combined sources
Beta strandi202 – 2043Combined sources
Beta strandi211 – 2133Combined sources
Helixi225 – 2295Combined sources
Beta strandi233 – 2353Combined sources
Beta strandi243 – 2464Combined sources
Beta strandi250 – 26011Combined sources
Helixi261 – 2677Combined sources
Beta strandi272 – 28211Combined sources
Helixi285 – 2906Combined sources
Helixi292 – 30312Combined sources
Helixi307 – 3093Combined sources
Beta strandi311 – 3155Combined sources
Helixi320 – 33011Combined sources
Helixi334 – 3363Combined sources
Helixi343 – 3464Combined sources
Helixi350 – 3523Combined sources
Helixi353 – 36816Combined sources
Beta strandi371 – 3799Combined sources
Turni380 – 3823Combined sources
Beta strandi383 – 3908Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 5-392.
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.
IPR016038. Thiolase-like_subgr.
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
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. Positions 5-392.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00058; UER00101.
BioCyciRETL1328306-WGS:GSTH-4110-MONOMER.
RETL1328306-WGS:GSTH-6457-MONOMER.
SABIO-RKP07097.

Miscellaneous databases

EvolutionaryTraceiP07097.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. 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]
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...

Publicationsi

  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.

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: January 7, 2015
This is version 108 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

External Data

Dasty 3

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 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.