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Protein

3-carboxy-cis,cis-muconate cycloisomerase

Gene

pcaB

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: 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

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 cycloisomerasePRO_0000161349Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

3D structure databases

ProteinModelPortaliP32427.
SMRiP32427. Positions 3-422.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-II fumarase/aspartase family.Curated

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

        10         20         30         40         50
MTNQLFDAYF TAPAMREIFS DRGRLQGMLD FEAALARAEA AAGLVPHSAV
60 70 80 90 100
AAIEAACKAE RYDVGALANA IATAGNSAIP LVKALGKVIA SGVPEAERYV
110 120 130 140 150
HLGATSQDAM DTGLVLQLRD ALDLIEADLG KLADTLSQQA LKHADTPMVG
160 170 180 190 200
RTWLQHATPV TLGMKLAGVL GALTRHRQRL QELGPPCWCC SSGGASGSLA
210 220 230 240 250
ALGSKAMPVA EALAEQLKLS LPEQPWHTQR DRLVEFASVL GLVAGSLGKF
260 270 280 290 300
GRDVSLLMQT EAGEVFEPSA PGKGGSSTMP HKRNPVGAAV LIGAATRVPG
310 320 330 340 350
LVSTLFAAMP QEHERSLGLW HAEWETLPDI CCLVSGALRQ AQVIAEGIEV
360 370 380 390 400
DAARMRRNLD LTQGLVLAEA VSIVLARTLG RDRAHHLLEQ CCQRAVAEQR
410 420
HLRAVLGDDP QVSAELSAEE LD
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. Curated

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L17082 Genomic DNA. Translation: AAA25920.1. Frameshift.
PIRiA44374.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L17082 Genomic DNA. Translation: AAA25920.1. Frameshift.
PIRiA44374.

3D structure databases

ProteinModelPortaliP32427.
SMRiP32427. Positions 3-422.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00157; UER00265.
BioCyciMetaCyc:MONOMER-3222.

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]
ProtoNetiSearch...

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: January 7, 2015
This is version 85 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

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.