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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)DescriptionActionsGraphical viewLength
    Binding sitei52Thiamine pyrophosphateBy similarity1
    Metal bindingi451MagnesiumBy similarity1
    Metal bindingi478MagnesiumBy similarity1

    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)DescriptionActionsGraphical viewLength
    ChainiPRO_00003978391 – 589Cyclohexane-1,2-dione hydrolaseAdd BLAST589

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    MINTiMINT-8305294.

    Structurei

    Secondary structure

    1589
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 5Combined sources3
    Helixi6 – 16Combined sources11
    Beta strandi21 – 25Combined sources5
    Helixi28 – 30Combined sources3
    Helixi31 – 38Combined sources8
    Helixi41 – 44Combined sources4
    Beta strandi45 – 47Combined sources3
    Helixi52 – 66Combined sources15
    Beta strandi71 – 76Combined sources6
    Helixi77 – 82Combined sources6
    Helixi84 – 92Combined sources9
    Beta strandi97 – 104Combined sources8
    Helixi106 – 108Combined sources3
    Helixi120 – 123Combined sources4
    Turni124 – 126Combined sources3
    Beta strandi127 – 132Combined sources6
    Helixi136 – 138Combined sources3
    Helixi139 – 150Combined sources12
    Beta strandi152 – 154Combined sources3
    Beta strandi157 – 163Combined sources7
    Helixi165 – 168Combined sources4
    Beta strandi170 – 172Combined sources3
    Turni174 – 176Combined sources3
    Helixi192 – 204Combined sources13
    Beta strandi206 – 212Combined sources7
    Helixi214 – 219Combined sources6
    Helixi222 – 232Combined sources11
    Beta strandi236 – 238Combined sources3
    Turni240 – 244Combined sources5
    Beta strandi253 – 256Combined sources4
    Helixi263 – 271Combined sources9
    Beta strandi273 – 279Combined sources7
    Turni284 – 292Combined sources9
    Beta strandi297 – 303Combined sources7
    Helixi305 – 307Combined sources3
    Beta strandi310 – 312Combined sources3
    Beta strandi315 – 319Combined sources5
    Helixi322 – 332Combined sources11
    Helixi333 – 335Combined sources3
    Helixi344 – 346Combined sources3
    Helixi350 – 368Combined sources19
    Beta strandi372 – 375Combined sources4
    Helixi377 – 386Combined sources10
    Beta strandi393 – 396Combined sources4
    Helixi402 – 408Combined sources7
    Beta strandi417 – 419Combined sources3
    Turni421 – 423Combined sources3
    Helixi429 – 439Combined sources11
    Beta strandi445 – 450Combined sources6
    Helixi451 – 454Combined sources4
    Turni455 – 457Combined sources3
    Helixi458 – 460Combined sources3
    Helixi461 – 466Combined sources6
    Beta strandi472 – 477Combined sources6
    Helixi482 – 492Combined sources11
    Helixi505 – 511Combined sources7
    Beta strandi515 – 518Combined sources4
    Turni520 – 522Combined sources3
    Helixi525 – 535Combined sources11
    Beta strandi539 – 545Combined sources7
    Beta strandi547 – 550Combined sources4
    Turni551 – 553Combined sources3
    Helixi582 – 586Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2PGNX-ray1.20A/B1-589[»]
    2PGOX-ray1.26A/B1-589[»]
    4D5EX-ray1.43A/B1-589[»]
    4D5GX-ray2.00A/B1-589[»]
    SMRiP0CH62.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0CH62.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni400 – 480Thiamine pyrophosphate bindingBy similarityAdd BLAST81

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2PGNX-ray1.20A/B1-589[»]
    2PGOX-ray1.26A/B1-589[»]
    4D5EX-ray1.43A/B1-589[»]
    4D5GX-ray2.00A/B1-589[»]
    SMRiP0CH62.
    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...

    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: November 2, 2016
    This is version 14 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.