HAD_THAAR
ID HAD_THAAR Reviewed; 368 AA.
AC O87871;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase {ECO:0000303|PubMed:9746358};
DE EC=1.1.1.368 {ECO:0000269|PubMed:10406950};
GN Name=had {ECO:0000303|PubMed:9746358};
OS Thauera aromatica.
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=59405 {ECO:0000312|EMBL:CAA12244.2};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 15-23, FUNCTION, AND
RP PATHWAY.
RC STRAIN=DSM 6984 / CIP 107765 / K172;
RX PubMed=9746358; DOI=10.1046/j.1432-1327.1998.2560148.x;
RA Breese K., Boll M., Alt-Moerbe J., Schaegger H., Fuchs G.;
RT "Genes coding for the benzoyl-CoA pathway of anaerobic aromatic metabolism
RT in the bacterium Thauera aromatica.";
RL Eur. J. Biochem. 256:148-154(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=DSM 6984 / CIP 107765 / K172;
RX PubMed=10406950; DOI=10.1046/j.1432-1327.1999.00504.x;
RA Laempe D., Jahn M., Fuchs G.;
RT "6-Hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase and 6-oxocyclohex-1-
RT ene-1-carbonyl-CoA hydrolase, enzymes of the benzoyl-CoA pathway of
RT anaerobic aromatic metabolism in the denitrifying bacterium Thauera
RT aromatica.";
RL Eur. J. Biochem. 263:420-429(1999).
CC -!- FUNCTION: Involved in the central benzoyl-CoA catabolism. Catalyzes the
CC oxidation of 6-hydroxycyclohex-1-ene-1-carbonyl-CoA to 6-oxocyclohex-1-
CC ene-1-carbonyl-CoA. It is specific to NAD and is also able to oxidize
CC 2-hydroxycyclohexane-1-carbonyl-CoA. {ECO:0000269|PubMed:10406950,
CC ECO:0000305|PubMed:9746358}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD(+) = 6-
CC oxocyclohex-1-ene-1-carbonyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:18265,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57361, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:76526; EC=1.1.1.368;
CC Evidence={ECO:0000269|PubMed:10406950};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:10406950};
CC Note=Binds 2 Zn(2+) ions per subunit. One of the Zn(2+) is essential
CC for catalytic activity while the other has a structural function.
CC {ECO:0000305|PubMed:10406950};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60 uM for 6-hydroxycyclohex-1-ene-1-carbonyl-CoA (with 3.5 mM NAD
CC at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:10406950};
CC Vmax=11.8 umol/min/mg enzyme with 6-hydroxycyclohex-1-ene-1-carbonyl-
CC CoA as substrate (with 3.5 mM NAD at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:10406950};
CC pH dependence:
CC Optimum pH is 7.2-7.4. {ECO:0000269|PubMed:10406950};
CC -!- PATHWAY: Aromatic compound metabolism; benzoyl-CoA degradation.
CC {ECO:0000305|PubMed:9746358}.
CC -!- SUBUNIT: Homodimer. {ECO:0000303|PubMed:10406950}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AJ224959; CAA12244.2; -; Genomic_DNA.
DR AlphaFoldDB; O87871; -.
DR SMR; O87871; -.
DR KEGG; ag:CAA12244; -.
DR BioCyc; MetaCyc:HADTHAUERA-MON; -.
DR BRENDA; 1.1.1.368; 6271.
DR UniPathway; UPA00739; -.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1901788; P:benzoyl-CoA catabolic process; IDA:UniProtKB.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR017614; Dearomat_deydrogenase.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03201; dearomat_had; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..368
FT /note="6-hydroxycyclohex-1-ene-1-carbonyl-CoA
FT dehydrogenase"
FT /id="PRO_0000430708"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q7SI09"
FT BINDING 56..60
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q52078"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q7SI09"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q7SI09"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q7SI09"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q7SI09"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000250|UniProtKB:Q7SI09"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q52078"
FT BINDING 173
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q52078"
FT BINDING 196..197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q7SI09"
FT BINDING 216..217
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q52078"
FT BINDING 216
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q7SI09"
FT BINDING 221
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00327"
FT BINDING 290..292
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q52078"
FT BINDING 308..310
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q7SI09"
FT BINDING 314..316
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q52078"
FT BINDING 363
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00327"
SQ SEQUENCE 368 AA; 38572 MW; 16A2A40B060A4CA6 CRC64;
MAAKSSVSSW RSEMSSNPHR WMMTSPGAPM VRAEFEIGEL SADQVVVAVA GCGVCHTDLG
YYYDSVRTNH ALPLALGHEI SGRVVQAGAN AAQWLGRAVI VPAVMPCGTC ELCTSGHGTI
CRDQVMPGND IQGGFASHVV VPARGLCPVD EARLAAAGLQ LADVSVVADA VTTPYQAVLQ
AGVEPGDVAV VIGVGGVGGY AVQIANAFGA SVVAIDVDPA KLEMMSKHGA ALTLNAREIS
GRDLKKAIEA HAKANGLRLT RWKIFECSGT GAGQTSAYGL LTHGATLAVV GFTMDKVEVR
LSNLMAFHAR ALGNWGCLPE YYPAALDLVL DKKIDLASFI ERHPLDQIGE VFAAAHAHKL
TRRAILTP
