ID I2GYD9_TETBL Unreviewed; 316 AA.
AC I2GYD9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=GTP cyclohydrolase II {ECO:0000256|ARBA:ARBA00012762};
DE EC=3.5.4.25 {ECO:0000256|ARBA:ARBA00012762};
GN Name=TBLA0B02990 {ECO:0000313|EMBL:CCH59141.1};
GN ORFNames=TBLA_0B02990 {ECO:0000313|EMBL:CCH59141.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH59141.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH59141.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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}.
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DR EMBL; HE806317; CCH59141.1; -; Genomic_DNA.
DR RefSeq; XP_004178660.1; XM_004178612.1.
DR AlphaFoldDB; I2GYD9; -.
DR STRING; 1071380.I2GYD9; -.
DR GeneID; 14494282; -.
DR KEGG; tbl:TBLA_0B02990; -.
DR eggNOG; KOG1284; Eukaryota.
DR HOGENOM; CLU_020273_2_4_1; -.
DR InParanoid; I2GYD9; -.
DR OMA; RLPNVEC; -.
DR OrthoDB; 1328905at2759; -.
DR Proteomes; UP000002866; Chromosome 2.
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 NCBIfam; TIGR00505; ribA; 1.
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:UP000002866};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT DOMAIN 108..241
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
SQ SEQUENCE 316 AA; 35656 MW; DE7EFB8F1422BF5D CRC64;
MTNQLPVVQC VARARIPTTK NGPDIFLHLY ANDRDNKEHL AIVFGEDIRS RSLFKQRPND
NQQSRMIRGA YVGKLYPGRT EADYDDRLNM KLEFDPVTGD LLVDHDHKTV WDPENNTLVR
IHSECYTGEN AWSARCDCGE QFDRAGELIS SEFDSQFPKV KGGNGHGVIV YLRQEGRGIG
LGEKLKAYNL QDLGADTVQA NLLLKHPADG RDFSIGKSIL IDLGIQNIRL LTNNPDKIST
VTYPPYLNCI ERVPMIPINW TDESKGIHSK EIDGYLRTKV ERMGHLLSQP LKLHSETSTL
HAHAHAHDQT TLPLVQ
//
