ID CHADH_ASPFM Reviewed; 261 AA.
AC D3J0Z1;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Chanoclavine-I dehydrogenase;
DE Short=ChaDH;
DE EC=1.1.1.332;
GN Name=fgaDH;
OS Aspergillus fumigatus (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=746128;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PATHWAY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=NIH 5233 / ATCC 13073;
RX PubMed=20039019; DOI=10.1007/s00203-009-0536-1;
RA Wallwey C., Matuschek M., Li S.M.;
RT "Ergot alkaloid biosynthesis in Aspergillus fumigatus: conversion of
RT chanoclavine-I to chanoclavine-I aldehyde catalyzed by a short-chain
RT alcohol dehydrogenase FgaDH.";
RL Arch. Microbiol. 192:127-134(2010).
CC -!- FUNCTION: Oxidoreductase involved in the biosynthesis of ergot alkaloid
CC biosynthesis. Catalyzes the oxidation of chanoclavine-I in the presence
CC of NAD(+) resulting in the formation of chanoclavine-I aldehyde. Ergot
CC alkaloids, which are produced by endophyte fungi, can enhance plant
CC host fitness, but also cause livestock toxicosis to host plants.
CC {ECO:0000269|PubMed:20039019}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chanoclavine-I + NAD(+) = chanoclavine-I aldehyde + H(+) +
CC NADH; Xref=Rhea:RHEA:33891, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:71487, ChEBI:CHEBI:72949;
CC EC=1.1.1.332; Evidence={ECO:0000269|PubMed:20039019};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.27 mM for chanoclavine-I {ECO:0000269|PubMed:20039019};
CC KM=1.1 mM for NAD(+) {ECO:0000269|PubMed:20039019};
CC Vmax=186 nmol/min/mg enzyme {ECO:0000269|PubMed:20039019};
CC -!- PATHWAY: Alkaloid biosynthesis; ergot alkaloid biosynthesis.
CC {ECO:0000269|PubMed:20039019}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20039019}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; GQ413954; ADB93017.1; -; mRNA.
DR AlphaFoldDB; D3J0Z1; -.
DR SMR; D3J0Z1; -.
DR BRENDA; 1.1.1.332; 508.
DR SABIO-RK; D3J0Z1; -.
DR UniPathway; UPA00327; -.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0035837; P:ergot alkaloid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR CDD; cd05233; SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR24321; DEHYDROGENASES, SHORT CHAIN; 1.
DR PANTHER; PTHR24321:SF8; DEHYDROGENASES, SHORT CHAIN; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 1: Evidence at protein level;
KW Alkaloid metabolism; NADP; Oxidoreductase.
FT CHAIN 1..261
FT /note="Chanoclavine-I dehydrogenase"
FT /id="PRO_0000421746"
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT ACT_SITE 170
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 18
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT BINDING 66
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT BINDING 132
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:L0E2Z4"
FT BINDING 166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 170
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 201
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:L0E2Z4"
SQ SEQUENCE 261 AA; 27796 MW; 4D8824EB115CA636 CRC64;
MASVESRIIA ITGGASGIGA ATCRLLAERG AAVLCVCDIS PKNFDDLKIS IKKINPSTKV
HCATVDVTSS VEVRQWIEGI ISDFGDLHGA VNAAGIAQGA GMRNTPTIAE EVDEEWTRIM
NTNLNGVFYC TREEVRAMKG LPATDRSIVN VGSIASVSHM PDVYAYGTSK GACAYFTTCV
AADAFPLGIR INNVSPGVTN TPMLPQFAPM AKTFEEIEES YKKEGLSLIE AEDVARTIVW
LLSEDSRPVF GANINVGACM P
//
