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Protein

Cyclohexane-1,2-dione hydrolase

Gene
N/A
Organism
Azoarcus sp.
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ring-opening cleavage of the alicyclic alcohol cyclohexane-1,2-dione.1 Publication

Catalytic activityi

Cyclohexane-1,2-dione + H2O = 6-oxohexanoate.1 Publication

Cofactori

Protein has several cofactor binding sites:

Kineticsi

  1. KM=12.3 µM for cyclohexane-1,2-dione1 Publication

    pH dependencei

    Optimum pH is 8.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei52 – 521Thiamine pyrophosphateBy similarity
    Metal bindingi451 – 4511MagnesiumBy similarity
    Metal bindingi478 – 4781MagnesiumBy similarity

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    FAD, Flavoprotein, Magnesium, Metal-binding, Thiamine pyrophosphate

    Enzyme and pathway databases

    BRENDAi3.7.1.11. 604.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclohexane-1,2-dione hydrolase (EC:3.7.1.11)
    OrganismiAzoarcus sp.
    Taxonomic identifieri29544 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAzoarcus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 589589Cyclohexane-1,2-dione hydrolasePRO_0000397839Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    MINTiMINT-8305294.

    Structurei

    Secondary structure

    1
    589
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53Combined sources
    Helixi6 – 1611Combined sources
    Beta strandi21 – 255Combined sources
    Helixi28 – 303Combined sources
    Helixi31 – 388Combined sources
    Helixi41 – 444Combined sources
    Beta strandi45 – 473Combined sources
    Helixi52 – 6615Combined sources
    Beta strandi71 – 766Combined sources
    Helixi77 – 826Combined sources
    Helixi84 – 929Combined sources
    Beta strandi97 – 1048Combined sources
    Helixi106 – 1083Combined sources
    Helixi120 – 1234Combined sources
    Turni124 – 1263Combined sources
    Beta strandi127 – 1326Combined sources
    Helixi136 – 1383Combined sources
    Helixi139 – 15012Combined sources
    Beta strandi152 – 1543Combined sources
    Beta strandi157 – 1637Combined sources
    Helixi165 – 1684Combined sources
    Beta strandi170 – 1723Combined sources
    Turni174 – 1763Combined sources
    Helixi192 – 20413Combined sources
    Beta strandi206 – 2127Combined sources
    Helixi214 – 2196Combined sources
    Helixi222 – 23211Combined sources
    Beta strandi236 – 2383Combined sources
    Turni240 – 2445Combined sources
    Beta strandi253 – 2564Combined sources
    Helixi263 – 2719Combined sources
    Beta strandi273 – 2797Combined sources
    Turni284 – 2929Combined sources
    Beta strandi297 – 3037Combined sources
    Helixi305 – 3073Combined sources
    Beta strandi310 – 3123Combined sources
    Beta strandi315 – 3195Combined sources
    Helixi322 – 33211Combined sources
    Helixi333 – 3353Combined sources
    Helixi344 – 3463Combined sources
    Helixi350 – 36819Combined sources
    Beta strandi372 – 3754Combined sources
    Helixi377 – 38610Combined sources
    Beta strandi393 – 3964Combined sources
    Helixi402 – 4087Combined sources
    Beta strandi417 – 4193Combined sources
    Turni421 – 4233Combined sources
    Helixi429 – 43911Combined sources
    Beta strandi445 – 4506Combined sources
    Helixi451 – 4544Combined sources
    Turni455 – 4573Combined sources
    Helixi458 – 4603Combined sources
    Helixi461 – 4666Combined sources
    Beta strandi472 – 4776Combined sources
    Helixi482 – 49211Combined sources
    Helixi505 – 5117Combined sources
    Beta strandi515 – 5184Combined sources
    Turni520 – 5223Combined sources
    Helixi525 – 53511Combined sources
    Beta strandi539 – 5457Combined sources
    Beta strandi547 – 5504Combined sources
    Turni551 – 5533Combined sources
    Helixi582 – 5865Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PGNX-ray1.20A/B1-589[»]
    2PGOX-ray1.26A/B1-589[»]
    4D5EX-ray1.43A/B1-589[»]
    4D5GX-ray2.00A/B1-589[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0CH62.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni400 – 48081Thiamine pyrophosphate bindingBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TPP enzyme family.Curated

    Family and domain databases

    Gene3Di3.40.50.1220. 1 hit.
    3.40.50.970. 2 hits.
    InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR029061. THDP-binding.
    IPR012000. Thiamin_PyroP_enz_cen_dom.
    IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
    IPR011766. TPP_enzyme-bd_C.
    [Graphical view]
    PfamiPF02775. TPP_enzyme_C. 1 hit.
    PF00205. TPP_enzyme_M. 1 hit.
    PF02776. TPP_enzyme_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF52467. SSF52467. 1 hit.
    SSF52518. SSF52518. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    P0CH62-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAIKRGADLI VEALEEYGTE QVVGFIGHTS HFVADAFSKS HLGKRVINPA
    60 70 80 90 100
    TELGGAWMVN GYNYVKDRSA AVGAWHCVGN LLLHAAMQEA RTGRIPAVHI
    110 120 130 140 150
    GLNSDGRLAG RSEAAQQVPW QSFTPIARST QRVERLDKVG EAIHEAFRVA
    160 170 180 190 200
    EGHPAGPAYV DIPFDLTADQ IDDKALVPRG ATRAKSVLHA PNEDVREAAA
    210 220 230 240 250
    QLVAAKNPVI LAGGGVARSG GSEALLKLAE MVGVPVVTTS TGAGVFPETH
    260 270 280 290 300
    ALAMGSAGFC GWKSANDMMA AADFVLVLGS RLSDWGIAQG YITKMPKFVH
    310 320 330 340 350
    VDTDPAVLGT FYFPLLSVVA DAKTFMEQLI EVLPGTSGFK AVRYQERENF
    360 370 380 390 400
    RQATEFRAAW DGWVREQESG DGMPASMFRA MAEVRKVQRP EDIIVTDIGN
    410 420 430 440 450
    HTLPMFGGAI LQRPRRLVTS MAEGILGCGF PMALGAQLAE PNSRVFLGTG
    460 470 480 490 500
    DGALYYHFNE FRVAVEHKLP VITMVFTNES YGANWTLMNH QFGQNNWTEF
    510 520 530 540 550
    MNPDWVGIAK AFGAYGESVR ETGDIAGALQ RAIDSGKPAL IEIPVSKTQG
    560 570 580
    LASDPVGGVG PNLLLKGREI PVDTGGSMYP GENLLHLKS
    Length:589
    Mass (Da):63,294
    Last modified:October 5, 2010 - v1
    Checksum:i75FF57166BAEF014
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PGNX-ray1.20A/B1-589[»]
    2PGOX-ray1.26A/B1-589[»]
    4D5EX-ray1.43A/B1-589[»]
    4D5GX-ray2.00A/B1-589[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    MINTiMINT-8305294.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.7.1.11. 604.

    Miscellaneous databases

    EvolutionaryTraceiP0CH62.

    Family and domain databases

    Gene3Di3.40.50.1220. 1 hit.
    3.40.50.970. 2 hits.
    InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR029061. THDP-binding.
    IPR012000. Thiamin_PyroP_enz_cen_dom.
    IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
    IPR011766. TPP_enzyme-bd_C.
    [Graphical view]
    PfamiPF02775. TPP_enzyme_C. 1 hit.
    PF00205. TPP_enzyme_M. 1 hit.
    PF02776. TPP_enzyme_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF52467. SSF52467. 1 hit.
    SSF52518. SSF52518. 2 hits.
    ProtoNetiSearch...

    Publicationsi

    1. "Cyclohexane-1,2-dione hydrolase: A new tool to degrade alicyclic compounds."
      Fraas S., Steinbach A.K., Tabbert A., Harder J., Ermler U., Tittmann K., Meyer A., Kroneck P.M.H.
      J. Mol. Catal., B Enzym. 61:47-49(2009)
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: 22Lin.
    2. "The crystal structure of FAD and ThDP dependent cyclohexane-1,2-dione hydrolase (CDH) from Azoarcus SP. strain 22Lin."
      Steinbach A.K., Fraas S., Harder J., Warkentin E., Kroneck P.M.H., Ermler U.
      Submitted (APR-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH MAGNESIUM; FAD; TPP AND SUBSTRATE ANALOG.

    Entry informationi

    Entry nameiCHDH_AZOSP
    AccessioniPrimary (citable) accession number: P0CH62
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: October 5, 2010
    Last modified: May 27, 2015
    This is version 13 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

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    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 one 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.