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P32427

- PCAB_PSEPU

UniProt

P32427 - PCAB_PSEPU

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
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 3 (15 May 2007)
      Previous versions | rss
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    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

    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

    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

    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.

    Experimental Info

    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...
    MobiDBi 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: October 1, 2014
    This is version 83 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