ID A0A139H2Y5_9PEZI Unreviewed; 403 AA.
AC A0A139H2Y5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=GTP cyclohydrolase II {ECO:0000256|ARBA:ARBA00012762};
DE EC=3.5.4.25 {ECO:0000256|ARBA:ARBA00012762};
GN ORFNames=AC578_5349 {ECO:0000313|EMBL:KXS96781.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS96781.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXS96781.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS96781.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-
CC pyrimidine + formate + 3 H(+) + 2 phosphate; Xref=Rhea:RHEA:23704,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58614; EC=3.5.4.25;
CC Evidence={ECO:0000256|ARBA:ARBA00029293};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005104}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family.
CC {ECO:0000256|ARBA:ARBA00008131}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXS96781.1}.
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DR EMBL; LFZN01000163; KXS96781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139H2Y5; -.
DR STRING; 321146.A0A139H2Y5; -.
DR OrthoDB; 1328905at2759; -.
DR Proteomes; UP000070133; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:InterPro.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00641; GTP_cyclohydro2; 1.
DR Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 1.
DR InterPro; IPR032677; GTP_cyclohydro_II.
DR InterPro; IPR000926; RibA.
DR InterPro; IPR036144; RibA-like_sf.
DR PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR PANTHER; PTHR21327:SF29; GTP CYCLOHYDROLASE-2; 1.
DR Pfam; PF00925; GTP_cyclohydro2; 1.
DR SUPFAM; SSF142695; RibA-like; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000070133};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT DOMAIN 212..366
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 403 AA; 44469 MW; A2F4D4CAE0068405 CRC64;
MPDFPSLASP AFTPIELASP KAERHEQNNV SELQLDTDFS TNTAPPLISP AFTPPRSPLV
DGQRHDRLPR SVPTEPPDAS TEHSQPKLLE QLPHVTCEVR ARIPTTTGQE MWLHLYHNNV
DNKEHMAIVF GPHIRSKSLD APRPGETERD RMIRGAYTGT LYPGRMHSRL EQIRSDAGVS
ARPQSPHTNG ASSPERSSSD AESISSTHSS YPPELGPPLV RIHSECYTGE TVWSARCDCG
EQLDEAARLM SLPVATPAGT PDTEHPQPRL QSAGGVIVYL RQEGRGIGLL SKLKAYNLQD
LGHDTMEANI LLRHPGDARS YGLATAILID LGLDGERGIK LLTNNPEKVR AVEGPHREVR
VVERVPMIPL AWQTKGEKGF TSPEVEKYIS TKIEKFKHMF SST
//
