Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P27099

- TCBD_PSESQ

UniProt

P27099 - TCBD_PSESQ

Protein

Chloromuconate cycloisomerase

Gene

tcbD

Organism
Pseudomonas sp. (strain P51)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    2-chloro-2,5-dihydro-5-oxofuran-2-acetate = 3-chloro-cis,cis-muconate.

    Cofactori

    Manganese.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei165 – 1651Proton acceptor
    Metal bindingi194 – 1941Manganese
    Metal bindingi220 – 2201Manganese
    Metal bindingi245 – 2451Manganese
    Active sitei323 – 3231Proton donor

    GO - Molecular functioni

    1. chloromuconate cycloisomerase activity Source: UniProtKB
    2. manganese ion binding Source: InterPro
    3. muconate cycloisomerase activity Source: InterPro

    GO - Biological processi

    1. 2,4-dichlorophenoxyacetic acid catabolic process Source: UniProtKB
    2. cellular amino acid catabolic process Source: InterPro

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14405.
    UniPathwayiUPA00083.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chloromuconate cycloisomerase (EC:5.5.1.7)
    Alternative name(s):
    Muconate cycloisomerase II
    Gene namesi
    Name:tcbD
    Encoded oniPlasmid pP510 Publication
    OrganismiPseudomonas sp. (strain P51)
    Taxonomic identifieri65067 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceae

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 370370Chloromuconate cycloisomerasePRO_0000171254Add
    BLAST

    Structurei

    Secondary structure

    1
    370
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 2120
    Beta strandi24 – 3815
    Beta strandi41 – 477
    Turni51 – 555
    Helixi60 – 6910
    Helixi71 – 755
    Helixi83 – 9311
    Helixi98 – 11518
    Helixi120 – 1245
    Beta strandi130 – 1345
    Beta strandi136 – 1383
    Helixi143 – 15513
    Beta strandi160 – 1656
    Beta strandi167 – 1693
    Helixi171 – 18515
    Helixi186 – 1883
    Beta strandi190 – 1945
    Helixi201 – 21414
    Beta strandi218 – 2203
    Helixi228 – 23710
    Beta strandi239 – 2457
    Helixi251 – 2599
    Beta strandi264 – 2685
    Helixi270 – 2734
    Helixi276 – 28914
    Beta strandi292 – 2954
    Helixi302 – 31211
    Helixi326 – 3294
    Beta strandi330 – 3323
    Beta strandi334 – 3374
    Beta strandi345 – 3473
    Beta strandi351 – 3533
    Helixi360 – 3667

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NU5X-ray1.95A1-370[»]
    ProteinModelPortaliP27099.
    SMRiP27099. Positions 1-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27099.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    InterProiIPR013370. Chloromuconate_cycloisomerase.
    IPR029065. Enolase_C-like.
    IPR029017. Enolase_N_like.
    IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
    IPR013342. Mandelate_racemase_C.
    IPR013341. Mandelate_racemase_N.
    IPR001354. MR_MLE.
    [Graphical view]
    PANTHERiPTHR13794. PTHR13794. 1 hit.
    PfamiPF02746. MR_MLE_N. 1 hit.
    [Graphical view]
    SMARTiSM00922. MR_MLE. 1 hit.
    [Graphical view]
    SUPFAMiSSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    TIGRFAMsiTIGR02534. mucon_cyclo. 1 hit.
    PROSITEiPS00908. MR_MLE_1. 1 hit.
    PS00909. MR_MLE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P27099-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKIEAISTTI VDVPTRRPLQ MSFTTVHKQS YVIVQVKAGG LVGIGEGGSV    50
    GGPTWGSESA ETIKVIIDNY LAPLLVGKDA SNLSQARVLM DRAVTGNLSA 100
    KAAIDIALHD LKARALNLSI ADLIGGTMRT SIPIAWTLAS GDTARDIDSA 150
    LEMIETRRHN RFKVKLGART PAQDLEHIRS IVKAVGDRAS VRVDVNQGWD 200
    EQTASIWIPR LEEAGVELVE QPVPRANFGA LRRLTEQNGV AILADESLSS 250
    LSSAFELARD HAVDAFSLKL CNMGGIANTL KVAAVAEAAG ISSYGGTMLD 300
    STVGTAAALH VYATLPSLPY GCELIGPWVL GDRLTQQDLE IKDFEVHLPL 350
    GSGLGVDLDH DKVRHYTRAA 370
    Length:370
    Mass (Da):39,487
    Last modified:August 1, 1992 - v1
    Checksum:i8C6ADA522C63508A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57629 Genomic DNA. Translation: AAD13626.1.
    PIRiB43673.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57629 Genomic DNA. Translation: AAD13626.1 .
    PIRi B43673.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NU5 X-ray 1.95 A 1-370 [» ]
    ProteinModelPortali P27099.
    SMRi P27099. Positions 1-369.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00083 .
    BioCyci MetaCyc:MONOMER-14405.

    Miscellaneous databases

    EvolutionaryTracei P27099.

    Family and domain databases

    Gene3Di 3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    InterProi IPR013370. Chloromuconate_cycloisomerase.
    IPR029065. Enolase_C-like.
    IPR029017. Enolase_N_like.
    IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
    IPR013342. Mandelate_racemase_C.
    IPR013341. Mandelate_racemase_N.
    IPR001354. MR_MLE.
    [Graphical view ]
    PANTHERi PTHR13794. PTHR13794. 1 hit.
    Pfami PF02746. MR_MLE_N. 1 hit.
    [Graphical view ]
    SMARTi SM00922. MR_MLE. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    TIGRFAMsi TIGR02534. mucon_cyclo. 1 hit.
    PROSITEi PS00908. MR_MLE_1. 1 hit.
    PS00909. MR_MLE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence analysis of the Pseudomonas sp. strain P51 tcb gene cluster, which encodes metabolism of chlorinated catechols: evidence for specialization of catechol 1,2-dioxygenases for chlorinated substrates."
      van der Meer J.R., Eggen R.I., Zehnder A.J., de Vos W.M.
      J. Bacteriol. 173:2425-2434(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The structure of Pseudomonas P51 Cl-muconate lactonizing enzyme: co-evolution of structure and dynamics with the dehalogenation function."
      Kajander T., Lehtioe L., Schloemann M., Goldman A.
      Protein Sci. 12:1855-1864(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), COFACTOR.

    Entry informationi

    Entry nameiTCBD_PSESQ
    AccessioniPrimary (citable) accession number: P27099
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Chloromuconate cycloisomerase II is highly active toward chlorinated substrates but retains diminished activity toward the non-chlorinated substrates.

    Keywords - Technical termi

    3D-structure, Plasmid

    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

    External Data

    Dasty 3