CHDH_AZOSP
ID CHDH_AZOSP Reviewed; 589 AA.
AC P0CH62;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Cyclohexane-1,2-dione hydrolase;
DE EC=3.7.1.11;
OS Azoarcus sp.
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus; unclassified Azoarcus.
OX NCBI_TaxID=29544;
RN [1]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=22Lin;
RX DOI=10.1016/j.molcatb.2009.03.021;
RA Fraas S., Steinbach A.K., Tabbert A., Harder J., Ermler U., Tittmann K.,
RA Meyer A., Kroneck P.M.H.;
RT "Cyclohexane-1,2-dione hydrolase: A new tool to degrade alicyclic
RT compounds.";
RL J. Mol. Catal., B Enzym. 61:47-49(2009).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH MAGNESIUM; FAD; TPP
RP AND SUBSTRATE ANALOG.
RA Steinbach A.K., Fraas S., Harder J., Warkentin E., Kroneck P.M.H.,
RA Ermler U.;
RT "The crystal structure of FAD and ThDP dependent cyclohexane-1,2-dione
RT hydrolase (CDH) from Azoarcus SP. strain 22Lin.";
RL Submitted (APR-2007) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the ring-opening cleavage of the alicyclic alcohol
CC cyclohexane-1,2-dione. {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclohexan-1,2-dione + H2O = 6-oxohexanoate + H(+);
CC Xref=Rhea:RHEA:26514, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18322, ChEBI:CHEBI:41674; EC=3.7.1.11;
CC Evidence={ECO:0000269|Ref.1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|Ref.1};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|Ref.1};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000269|Ref.1};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000269|Ref.1};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|Ref.1};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|Ref.1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.3 uM for cyclohexane-1,2-dione {ECO:0000269|Ref.1};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|Ref.1};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.1, ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR PDB; 2PGN; X-ray; 1.20 A; A/B=1-589.
DR PDB; 2PGO; X-ray; 1.26 A; A/B=1-589.
DR PDB; 4D5E; X-ray; 1.43 A; A/B=1-589.
DR PDB; 4D5G; X-ray; 2.00 A; A/B=1-589.
DR PDBsum; 2PGN; -.
DR PDBsum; 2PGO; -.
DR PDBsum; 4D5E; -.
DR PDBsum; 4D5G; -.
DR AlphaFoldDB; P0CH62; -.
DR SMR; P0CH62; -.
DR MINT; P0CH62; -.
DR BRENDA; 3.7.1.11; 604.
DR EvolutionaryTrace; P0CH62; -.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR18968; PTHR18968; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Hydrolase; Magnesium; Metal-binding;
KW Thiamine pyrophosphate.
FT CHAIN 1..589
FT /note="Cyclohexane-1,2-dione hydrolase"
FT /id="PRO_0000397839"
FT REGION 400..480
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:4D5E"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 139..150
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4D5E"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 214..219
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:4D5E"
FT TURN 240..244
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:4D5E"
FT TURN 284..292
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 322..332
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 350..368
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 377..386
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 402..408
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:4D5E"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 429..439
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 451..454
FT /evidence="ECO:0007829|PDB:4D5E"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 461..466
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 472..477
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 482..492
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 505..511
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:4D5E"
FT TURN 520..522
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 525..535
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 539..545
FT /evidence="ECO:0007829|PDB:4D5E"
FT STRAND 547..550
FT /evidence="ECO:0007829|PDB:4D5E"
FT TURN 551..553
FT /evidence="ECO:0007829|PDB:4D5E"
FT HELIX 582..586
FT /evidence="ECO:0007829|PDB:4D5E"
SQ SEQUENCE 589 AA; 63294 MW; 75FF57166BAEF014 CRC64;
MAIKRGADLI VEALEEYGTE QVVGFIGHTS HFVADAFSKS HLGKRVINPA TELGGAWMVN
GYNYVKDRSA AVGAWHCVGN LLLHAAMQEA RTGRIPAVHI GLNSDGRLAG RSEAAQQVPW
QSFTPIARST QRVERLDKVG EAIHEAFRVA EGHPAGPAYV DIPFDLTADQ IDDKALVPRG
ATRAKSVLHA PNEDVREAAA QLVAAKNPVI LAGGGVARSG GSEALLKLAE MVGVPVVTTS
TGAGVFPETH ALAMGSAGFC GWKSANDMMA AADFVLVLGS RLSDWGIAQG YITKMPKFVH
VDTDPAVLGT FYFPLLSVVA DAKTFMEQLI EVLPGTSGFK AVRYQERENF RQATEFRAAW
DGWVREQESG DGMPASMFRA MAEVRKVQRP EDIIVTDIGN HTLPMFGGAI LQRPRRLVTS
MAEGILGCGF PMALGAQLAE PNSRVFLGTG DGALYYHFNE FRVAVEHKLP VITMVFTNES
YGANWTLMNH QFGQNNWTEF MNPDWVGIAK AFGAYGESVR ETGDIAGALQ RAIDSGKPAL
IEIPVSKTQG LASDPVGGVG PNLLLKGREI PVDTGGSMYP GENLLHLKS
