CHCA_STRCU
ID CHCA_STRCU Reviewed; 280 AA.
AC P95727;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=1-cyclohexenylcarbonyl-CoA reductase {ECO:0000303|PubMed:1597409};
DE EC=1.3.1.120 {ECO:0000269|PubMed:10973220, ECO:0000269|PubMed:1597409, ECO:0000269|PubMed:8955309};
DE AltName: Full=Cyclohexane-1-carbonyl-CoA reductase (NADP(+)) {ECO:0000305};
GN Name=chcA {ECO:0000303|PubMed:8955309};
OS Streptomyces collinus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=42684;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=Tu 1892;
RX PubMed=8955309; DOI=10.1128/jb.178.23.6873-6881.1996;
RA Wang P., Denoya C.D., Morgenstern M.R., Skinner D.D., Wallace K.K.,
RA Digate R., Patton S., Banavali N., Schuler G., Speedie M.K., Reynolds K.A.;
RT "Cloning and characterization of the gene encoding 1-cyclohexenylcarbonyl
RT coenzyme A reductase from Streptomyces collinus.";
RL J. Bacteriol. 178:6873-6881(1996).
RN [2]
RP PROTEIN SEQUENCE OF 106-117 AND 143-153, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=Tu 1892;
RX PubMed=1597409; DOI=10.1128/jb.174.12.3850-3854.1992;
RA Reynolds K.A., Wang P., Fox K.M., Speedie M.K., Lam Y., Floss H.G.;
RT "Purification and characterization of a novel enoyl coenzyme A reductase
RT from Streptomyces collinus.";
RL J. Bacteriol. 174:3850-3854(1992).
RN [3]
RP PATHWAY, AND GENE CLUSTER.
RC STRAIN=Tu 1892;
RX PubMed=10103039; DOI=10.1046/j.1432-1327.1999.00244.x;
RA Chen S., von Bamberg D., Hale V., Breuer M., Hardt B., Mueller R.,
RA Floss H.G., Reynolds K.A., Leistner E.;
RT "Biosynthesis of ansatrienin (mycotrienin) and naphthomycin. Identification
RT and analysis of two separate biosynthetic gene clusters in Streptomyces
RT collinus Tue 1892.";
RL Eur. J. Biochem. 261:98-107(1999).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10973220; DOI=10.1038/79479;
RA Cropp T.A., Wilson D.J., Reynolds K.A.;
RT "Identification of a cyclohexylcarbonyl CoA biosynthetic gene cluster and
RT application in the production of doramectin.";
RL Nat. Biotechnol. 18:980-983(2000).
CC -!- FUNCTION: Involved in the biosynthesis of the antifungal antibiotic
CC ansatrienin A (mycotrienin I) (PubMed:1597409, PubMed:8955309).
CC Catalyzes three of the reductive steps involved in the formation of the
CC cyclohexanecarboxylic acid (CHC) moiety of ansatrienin from shikimic
CC acid (PubMed:8955309). Can use 3,4-dihydroxycyclohexa-1,5-diene-1-
CC carbonyl-CoA, 5-hydroxycyclohex-1-ene-1-carbonyl-CoA and cyclohex-1-
CC ene-1-carbonyl-CoA as substrates (PubMed:8955309, PubMed:1597409,
CC PubMed:10973220). {ECO:0000269|PubMed:10973220,
CC ECO:0000269|PubMed:1597409, ECO:0000269|PubMed:8955309}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4R,5R)-4,5-dihydroxycyclohex-2-ene-1-carbonyl-CoA + NADP(+) =
CC (3R,4R)-3,4-dihydroxycyclohexa-1,5-diene-1-carbonyl-CoA + H(+) +
CC NADPH; Xref=Rhea:RHEA:61576, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:144823, ChEBI:CHEBI:144824;
CC EC=1.3.1.120; Evidence={ECO:0000269|PubMed:8955309};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:61578;
CC Evidence={ECO:0000269|PubMed:8955309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-3-hydroxycyclohexane-1-carbonyl-CoA + NADP(+) = (5S)-5-
CC hydroxycyclohex-1-ene-1-carbonyl-CoA + H(+) + NADPH;
CC Xref=Rhea:RHEA:61580, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:144830, ChEBI:CHEBI:144831;
CC EC=1.3.1.120; Evidence={ECO:0000269|PubMed:8955309};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:61582;
CC Evidence={ECO:0000269|PubMed:8955309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclohexane-1-carbonyl-CoA + NADP(+) = cyclohex-1-ene-1-
CC carbonyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:59988, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:76270,
CC ChEBI:CHEBI:76271; EC=1.3.1.120;
CC Evidence={ECO:0000269|PubMed:10973220, ECO:0000269|PubMed:1597409,
CC ECO:0000269|PubMed:8955309};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:59990;
CC Evidence={ECO:0000269|PubMed:10973220, ECO:0000269|PubMed:1597409,
CC ECO:0000269|PubMed:8955309};
CC -!- ACTIVITY REGULATION: Inhibited by the thiol inhibitors p-
CC chloromercuribenzoate, N-ethylmaleimide and iodoacetamide. Also
CC inhibited by various divalent cations. {ECO:0000269|PubMed:1597409}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for NADPH {ECO:0000269|PubMed:1597409};
CC KM=30 uM for 5-hydroxycyclohex-1-ene-1-carbonyl-CoA
CC {ECO:0000269|PubMed:8955309};
CC KM=25 uM for cyclohex-1-ene-1-carbonyl-CoA
CC {ECO:0000269|PubMed:1597409, ECO:0000269|PubMed:8955309};
CC Vmax=5.3 umol/min/mg enzyme with 5-hydroxycyclohex-1-ene-1-carbonyl-
CC CoA as substrate {ECO:0000269|PubMed:8955309};
CC Vmax=7.5 umol/min/mg enzyme with cyclohex-1-ene-1-carbonyl-CoA as
CC substrate {ECO:0000269|PubMed:8955309};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:1597409};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:1597409};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:8955309,
CC ECO:0000305|PubMed:10103039}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1597409,
CC ECO:0000269|PubMed:8955309}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant loses the ability to synthesize
CC either cyclohexanecarboxylic acid or ansatrienin.
CC {ECO:0000269|PubMed:8955309}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U72144; AAC44655.1; -; Genomic_DNA.
DR AlphaFoldDB; P95727; -.
DR SMR; P95727; -.
DR KEGG; ag:AAC44655; -.
DR BioCyc; MetaCyc:MON-20782; -.
DR BRENDA; 1.3.1.120; 6000.
DR SABIO-RK; P95727; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Direct protein sequencing; NADP; Oxidoreductase.
FT CHAIN 1..280
FT /note="1-cyclohexenylcarbonyl-CoA reductase"
FT /id="PRO_0000450124"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P71079"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P71079"
FT BINDING 22..25
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P71079"
FT BINDING 71..72
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P71079"
FT BINDING 98
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P71079"
FT BINDING 165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P71079"
FT BINDING 194..196
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P71079"
SQ SEQUENCE 280 AA; 29849 MW; 20F8B51A21E76135 CRC64;
MNSPHQQQTA DRRQVSLITG ASRGIGRTLA LTLARRGGTV VVNYKKNADL AQKTVAEVEE
AGGQGFAVQA DVETTEGVTA LFDEVAQRCG RLDHFVSNAA ASAFKNIVDL GPHHLDRSYA
MNLRPFVLGA QQAVKLMDNG GRIVALSSYG SVRAYPTYAM LGGMKAAIES WVRYMAVEFA
PYGINVNAVN GGLIDSDSLE FFYNVEGMPP MQGVLDRIPA RRPGTVQEMA DTIAFLLGDG
AGYITGQTLV VDGGLSIVAP PFFADAGEAL ELPPRPTRDA
