CLOA_CLAFS
ID CLOA_CLAFS Reviewed; 511 AA.
AC A8C7R4;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Inactive cytochrome P450 monooxygenase cloA {ECO:0000303|PubMed:17720822};
DE AltName: Full=Ergot alkaloid synthesis protein cloA {ECO:0000303|PubMed:17720822};
DE AltName: Full=Inactive clavine oxidase {ECO:0000303|PubMed:17720822};
DE Short=CLOA {ECO:0000303|PubMed:17720822};
GN Name=cloA {ECO:0000303|PubMed:17720822};
OS Claviceps fusiformis (Ergot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=40602;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 26245 / DSM 2942 / CBS 164.59;
RX PubMed=17720822; DOI=10.1128/aem.01040-07;
RA Lorenz N., Wilson E.V., Machado C., Schardl C.L., Tudzynski P.;
RT "Comparison of ergot alkaloid biosynthesis gene clusters in Claviceps
RT species indicates loss of late pathway steps in evolution of C.
RT fusiformis.";
RL Appl. Environ. Microbiol. 73:7185-7191(2007).
CC -!- FUNCTION: Inactive cytochrome P450 monooxygenase; part of the gene
CC cluster that mediates the biosynthesis of fungal ergot alkaloid
CC (PubMed:17720822). DmaW catalyzes the first step of ergot alkaloid
CC biosynthesis by condensing dimethylallyl diphosphate (DMAP) and
CC tryptophan to form 4-dimethylallyl-L-tryptophan (By similarity). The
CC second step is catalyzed by the methyltransferase easF that methylates
CC 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-
CC methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By
CC similarity). The catalase easC and the FAD-dependent oxidoreductase
CC easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is
CC further oxidized by easD in the presence of NAD(+), resulting in the
CC formation of chanoclavine-I aldehyde (By similarity). Agroclavine
CC dehydrogenase easG then mediates the conversion of chanoclavine-I
CC aldehyde to agroclavine via a non-enzymatic adduct reaction: the
CC substrate is an iminium intermediate that is formed spontaneously from
CC chanoclavine-I aldehyde in the presence of glutathione (By similarity).
CC Further conversion of agroclavine to paspalic acid is a two-step
CC process involving oxidation of agroclavine to elymoclavine and of
CC elymoclavine to paspalic acid, the second step being performed by the
CC elymoclavine oxidase cloA (PubMed:17720822). However, cloA does not
CC encode a functional enzyme indicating that C.fusiformis terminates its
CC ergot alkaloid pathway at elymoclavine (PubMed:17720822).
CC {ECO:0000250|UniProtKB:Q2PBY6, ECO:0000269|PubMed:17720822}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Even when expressed, does not show any monooxygenase
CC activity (PubMed:17720822). {ECO:0000269|PubMed:17720822}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; EU006773; ABV57820.1; -; Genomic_DNA.
DR AlphaFoldDB; A8C7R4; -.
DR SMR; A8C7R4; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..511
FT /note="Inactive cytochrome P450 monooxygenase cloA"
FT /id="PRO_0000439117"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 450
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 511 AA; 57584 MW; D28AC165EB3DDE1A CRC64;
MLLLWLYQAL PTSLTRILLT AGLCVPCALV IHGIYNLYFH PLRNVPGPKL GALTDLYAFY
WNWIRGVGYS KQFDRWHKHY NSSVIRIGPN DVHTTQVELY DVIHKAGSTW LKDKSFYKHF
GGLDAMIDPR EYRTYRTHLA PLYSQRAVDG LVSKMDDDLA ICGQKTTKMA ENGKAVNMAR
VLTTLSTSMI LYNLFSMDIS LWECNDYHPF LEAFEHIMAQ IWLFLSYPRL ATCLSLIPGT
SLARLAPSWT TFMNSCAAWC DEDARKQRAS DDQSIRDSHS KRYYALKHTD ANDKKSIIPA
PLDELFSFIA GGTDTTAYTT GCAFFYILSS PSVCRKLVKE LDENASFIRN GLDYHKIQTL
PYLNAVIKET LRISVPVPGC LPRVVPEGGI TVGSFHLPAG TALSITQQAI SLNQDIFPSP
LCFSPERWIG PAAAGLDKWN VAFGRGSRQC IGTTLAYLEL RCVVAYFFSR FDMTLTAKNG
DGHRWVDRFV AVNLDTVEVL VLSDRWSGAR Y
