TCPK_CLAP2
ID TCPK_CLAP2 Reviewed; 222 AA.
AC M1W855;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Gamma-glutamyl cyclotransferase gliK {ECO:0000250|UniProtKB:E9R9Y3};
DE Short=GGCT gliK {ECO:0000250|UniProtKB:E9R9Y3};
DE EC=4.3.2.9 {ECO:0000305|PubMed:27390873};
DE AltName: Full=Thiocalpurine biosynthesis protein K {ECO:0000303|PubMed:27390873};
GN Name=tcpK {ECO:0000303|PubMed:27390873}; ORFNames=CPUR_02674;
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1;
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
RN [2]
RP FUNCTION, AND INDUCTION.
RX PubMed=27390873; DOI=10.1371/journal.pone.0158945;
RA Dopstadt J., Neubauer L., Tudzynski P., Humpf H.U.;
RT "The epipolythiodiketopiperazine gene cluster in Claviceps purpurea:
RT dysfunctional cytochrome P450 enzyme prevents formation of the previously
RT unknown clapurines.";
RL PLoS ONE 11:E0158945-E0158945(2016).
CC -!- FUNCTION: Gamma-glutamyl cyclotransferase; part of the gene cluster
CC that mediates the biosynthesis of an unusual class of
CC epipolythiodioxopiperazines (ETPs) lacking the reactive thiol group
CC important for toxicity (PubMed:27390873). Firstly, L-tyrosine is
CC prenylated by tcpD, before undergoing condensation with L-glycine in a
CC reaction catalyzed by the NRPS tcpP leading to the diketopiperazine
CC (DKP) backbone (PubMed:27390873). Afterwards the alpha-carbon of
CC tyrosine is oxidized by the cytochrome P450 tcpC to form a hydroxyl
CC group (PubMed:27390873). However, in contrast other ETP biosynthesis
CC pathways studied so far, tcpC is not able to bishydroxylate the DKP at
CC both alpha-carbon positions, but hydroxylates the alpha-carbon of the
CC tyrosine part and the nitrogen of the glycine part (PubMed:27390873).
CC The next steps involve an alpha,beta-elimination reaction catalyzed by
CC tcpI, a methylation by the methyltransferase tcpN the action of the
CC four enzyme cascade tcpG/K/J/I (PubMed:27390873). Due to a
CC dysfunctional cytochrome P450 monooxygenase tcpC, the pathway leads to
CC the biosynthesis of probable non-toxic metabolites lacking the reactive
CC thiol group (PubMed:27390873). {ECO:0000269|PubMed:27390873}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-(gamma-L-glutamyl)-L-amino acid = 5-oxo-L-proline +
CC an L-alpha-amino acid; Xref=Rhea:RHEA:20505, ChEBI:CHEBI:58402,
CC ChEBI:CHEBI:59869, ChEBI:CHEBI:71304; EC=4.3.2.9;
CC Evidence={ECO:0000305|PubMed:27390873};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:27390873}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by the thioclapurine
CC cluster-specific transcription factor tcpZ (PubMed:27390873).
CC {ECO:0000269|PubMed:27390873}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; CAGA01000011; CCE28983.1; -; Genomic_DNA.
DR AlphaFoldDB; M1W855; -.
DR SMR; M1W855; -.
DR STRING; 1111077.M1W855; -.
DR EnsemblFungi; CCE28983; CCE28983; CPUR_02674.
DR VEuPathDB; FungiDB:CPUR_02674; -.
DR eggNOG; ENOG502SBD2; Eukaryota.
DR HOGENOM; CLU_030506_0_0_1; -.
DR OrthoDB; 1484710at2759; -.
DR Proteomes; UP000016801; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003839; F:gamma-glutamylcyclotransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR017939; G-Glutamylcylcotransferase.
DR PANTHER; PTHR12935; PTHR12935; 1.
PE 2: Evidence at transcript level;
KW Lyase; Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..222
FT /note="Gamma-glutamyl cyclotransferase gliK"
FT /id="PRO_0000437728"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 222 AA; 24889 MW; BE7888ED08C6B39C CRC64;
MSASVFIERR KIRPLRTEAA CIPTHALCFN VLGIPYMDPG NGGIRPLNPD DSDATACVHG
VAYLLTSDDL KKVILSEGGG IAYQVARLNA KLLLDDSPIV VDTLIGRHNV DASNERLPSA
RYIGVLTRGA NELNLPLSYQ RRLAEQPIYQ PKSGWWFQLG VALFLWPWTR AAIITERLVY
KHQGPDGHVP AWFLFIFDCL LWLMWAQHDY IHGPIFGRGD GR