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Protein

Acetyl-CoA acetyltransferase

Gene

phaA

Organism
Zoogloea ramigera
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: poly-(R)-3-hydroxybutanoate biosynthesis

This protein is involved in the pathway poly-(R)-3-hydroxybutanoate biosynthesis, which is part of Biopolymer metabolism.Curated
View all proteins of this organism that are known to be involved in the pathway poly-(R)-3-hydroxybutanoate biosynthesis and in Biopolymer metabolism.

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 (phaA)
  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

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processPHB biosynthesis

Enzyme and pathway databases

BRENDAi2.3.1.9 6758
SABIO-RKiP07097
UniPathwayiUPA00058; UER00101
UPA00917

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA acetyltransferase (EC:2.3.1.9)
Alternative name(s):
Acetoacetyl-CoA thiolase
Beta-ketothiolase1 Publication
Gene namesi
Name:phaA1 Publication
Synonyms:phbA1 Publication
OrganismiZoogloea ramigera
Taxonomic identifieri350 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesZoogloeaceaeZoogloea

Subcellular locationi

GO - Cellular componenti

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

Chemistry databases

DrugBankiDB03059 Acetoacetyl-Coenzyme A
DB01992 Coenzyme A
DB08328 PANTOTHENYL-AMINOETHANOL-11-PIVALIC ACID
DB03045 Pantothenyl-Aminoethanol-Acetate Pivalic Acid
DB02039 S-Acetyl-Cysteine
DB02160 S-Butyryl-Cystein
DB01915 S-Hydroxycysteine

PTM / Processingi

Molecule processing

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

Interactioni

Subunit structurei

Homotetramer.3 Publications

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
Beta strandi28 – 33Combined sources6
Beta strandi40 – 43Combined sources4
Turni44 – 47Combined sources4
Helixi48 – 59Combined sources12
Helixi60 – 62Combined sources3
Beta strandi65 – 69Combined sources5
Helixi80 – 87Combined sources8
Helixi88 – 90Combined sources3
Beta strandi95 – 101Combined sources7
Helixi107 – 120Combined sources14
Beta strandi124 – 126Combined sources3
Beta strandi128 – 131Combined sources4
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

ProteinModelPortaliP07097
SMRiP07097
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07097

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Family and domain databases

CDDicd00751 thiolase, 1 hit
Gene3Di3.40.47.10, 4 hits
InterProiView protein in InterPro
IPR002155 Thiolase
IPR016039 Thiolase-like
IPR020615 Thiolase_acyl_enz_int_AS
IPR020610 Thiolase_AS
IPR020617 Thiolase_C
IPR020613 Thiolase_CS
IPR020616 Thiolase_N
PfamiView protein in Pfam
PF02803 Thiolase_C, 1 hit
PF00108 Thiolase_N, 1 hit
PIRSFiPIRSF000429 Ac-CoA_Ac_transf, 1 hit
SUPFAMiSSF53901 SSF53901, 2 hits
TIGRFAMsiTIGR01930 AcCoA-C-Actrans, 1 hit
PROSITEiView protein in PROSITE
PS00098 THIOLASE_1, 1 hit
PS00737 THIOLASE_2, 1 hit
PS00099 THIOLASE_3, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiTHIL_ZOORA
AccessioniPrimary (citable) accession number: P07097
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 127 of the entry and version 4 of the sequence. See 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

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