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P32427

- PCAB_PSEPU

UniProt

P32427 - PCAB_PSEPU

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Protein
3-carboxy-cis,cis-muconate cycloisomerase
Gene
pcaB
Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes an anti cycloisomerization.

Catalytic activityi

2-carboxy-2,5-dihydro-5-oxofuran-2-acetate = cis,cis-butadiene-1,2,4-tricarboxylate.

Pathwayi

GO - Molecular functioni

  1. 3-carboxy-cis,cis-muconate cycloisomerase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. beta-ketoadipate pathway Source: UniProtKB-UniPathway
  2. protocatechuate catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-3222.
UniPathwayiUPA00157; UER00265.

Names & Taxonomyi

Protein namesi
Recommended name:
3-carboxy-cis,cis-muconate cycloisomerase (EC:5.5.1.2)
Alternative name(s):
3-carboxymuconate lactonizing enzyme
Short name:
CMLE
Gene namesi
Name:pcaB
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›422›4223-carboxy-cis,cis-muconate cycloisomerase
PRO_0000161349Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

3D structure databases

ProteinModelPortaliP32427.
SMRiP32427. Positions 3-422.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR012789. Protocat_PcaB.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SMARTiSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR02426. protocat_pcaB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P32427-1 [UniParc]FASTAAdd to Basket

« Hide

MTNQLFDAYF TAPAMREIFS DRGRLQGMLD FEAALARAEA AAGLVPHSAV    50
AAIEAACKAE RYDVGALANA IATAGNSAIP LVKALGKVIA SGVPEAERYV 100
HLGATSQDAM DTGLVLQLRD ALDLIEADLG KLADTLSQQA LKHADTPMVG 150
RTWLQHATPV TLGMKLAGVL GALTRHRQRL QELGPPCWCC SSGGASGSLA 200
ALGSKAMPVA EALAEQLKLS LPEQPWHTQR DRLVEFASVL GLVAGSLGKF 250
GRDVSLLMQT EAGEVFEPSA PGKGGSSTMP HKRNPVGAAV LIGAATRVPG 300
LVSTLFAAMP QEHERSLGLW HAEWETLPDI CCLVSGALRQ AQVIAEGIEV 350
DAARMRRNLD LTQGLVLAEA VSIVLARTLG RDRAHHLLEQ CCQRAVAEQR 400
HLRAVLGDDP QVSAELSAEE LD 422
Length:422
Mass (Da):44,676
Last modified:May 15, 2007 - v3
Checksum:iDCB0C1E9E90DB03B
GO

Sequence cautioni

The sequence AAA25920.1 differs from that shown. Reason: Frameshift at position 379.

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei422 – 4221

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L17082 Genomic DNA. Translation: AAA25920.1. Frameshift.
PIRiA44374.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L17082 Genomic DNA. Translation: AAA25920.1 . Frameshift.
PIRi A44374.

3D structure databases

ProteinModelPortali P32427.
SMRi P32427. Positions 3-422.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00157 ; UER00265 .
BioCyci MetaCyc:MONOMER-3222.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
InterProi IPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR012789. Protocat_PcaB.
[Graphical view ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SMARTi SM00998. ADSL_C. 1 hit.
[Graphical view ]
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR02426. protocat_pcaB. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida is homologous to the class II fumarase family: a new reaction in the evolution of a mechanistic motif."
    Williams S.E., Woolridge E.M., Ransom S.C., Landro J.A., Babbitt P.C., Kozarich J.W.
    Biochemistry 31:9768-9776(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15.
    Strain: PRS2000.

Entry informationi

Entry nameiPCAB_PSEPU
AccessioniPrimary (citable) accession number: P32427
Secondary accession number(s): Q59703
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: May 15, 2007
Last modified: September 3, 2014
This is version 82 of the entry and version 3 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

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