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Protein

3-oxoadipate CoA-transferase subunit A

Gene

catI

Organism
Pseudomonas sp. (strain B13)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the CoA transfer from succinate to 3-oxoadipate (beta-ketoadipate).

Catalytic activityi

Succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA.1 Publication

Kineticsi

  1. KM=0.4 mM for 3-oxoadipate1 Publication
  2. KM=0.2 mM for succinyl-CoA1 Publication

pH dependencei

Optimum pH is 8.4.1 Publication

Pathwayi

GO - Molecular functioni

  1. 3-oxoadipate CoA-transferase activity Source: UniProtKB-EC

GO - Biological processi

  1. beta-ketoadipate pathway Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Enzyme and pathway databases

SABIO-RKQ8VPF3.
UniPathwayiUPA00157; UER00262.

Names & Taxonomyi

Protein namesi
Recommended name:
3-oxoadipate CoA-transferase subunit A (EC:2.8.3.6)
Alternative name(s):
3-oxoadipate:succinyl-CoA transferase subunit A
Beta-ketoadipate:succinyl-CoA transferase subunit A
Gene namesi
Name:catI
OrganismiPseudomonas sp. (strain B13)
Taxonomic identifieri65741 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 2822813-oxoadipate CoA-transferase subunit APRO_0000337673Add
BLAST

Interactioni

Subunit structurei

Heterotetramer composed of 2 A and 2 B subunits.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ8VPF3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR004165. CoA_trans_fam_I.
[Graphical view]
PANTHERiPTHR13707. PTHR13707. 1 hit.
PfamiPF01144. CoA_trans. 1 hit.
[Graphical view]
SMARTiSM00882. CoA_trans. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8VPF3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAELLTLREA VERFVNDGDT VALEGFTHLI PTAASHEIIR QGKKDLHLVR
60 70 80 90 100
MTPDLVYDLL IGAGCARKLT FSWGGNPGVG SLHRLRDAVE KGWPNALEID
110 120 130 140 150
EHSHADLANS YVAGASGLPF AVLRAYAGSD LPKVNPNIKF INCPFTGEQL
160 170 180 190 200
AAVPSVRPDV TVIHAQKADR KGNVLLWGIL GVQKEAALAA KRCIVTVEEI
210 220 230 240 250
VDDLNAPMNS CVLPTWALSA VCHVPGGSHP SYAHGYYERD NRFYQAWDPI
260 270 280
ARDRETFTAW IDEYIRGTKD FSEFQAKIAE GK
Length:282
Mass (Da):30,973
Last modified:March 1, 2002 - v1
Checksum:iEFC6A128C8F8CB34
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY044272 Genomic DNA. Translation: AAL02405.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY044272 Genomic DNA. Translation: AAL02405.1.

3D structure databases

ProteinModelPortaliQ8VPF3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00157; UER00262.
SABIO-RKQ8VPF3.

Family and domain databases

InterProiIPR004165. CoA_trans_fam_I.
[Graphical view]
PANTHERiPTHR13707. PTHR13707. 1 hit.
PfamiPF01144. CoA_trans. 1 hit.
[Graphical view]
SMARTiSM00882. CoA_trans. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: cloning, characterization, and analysis of sequences encoding 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase."
    Goebel M., Kassel-Cati K., Schmidt E., Reineke W.
    J. Bacteriol. 184:216-223(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: purification and characterization of 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase."
    Kaschabek S.R., Kuhn B., Mueller D., Schmidt E., Reineke W.
    J. Bacteriol. 184:207-215(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-31, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Entry informationi

Entry nameiCATI_PSESB
AccessioniPrimary (citable) accession number: Q8VPF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 1, 2002
Last modified: October 1, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.