ID F8MF20_NEUT8 Unreviewed; 410 AA.
AC F8MF20;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=GTP cyclohydrolase II {ECO:0000256|ARBA:ARBA00012762};
DE EC=3.5.4.25 {ECO:0000256|ARBA:ARBA00012762};
GN ORFNames=NEUTE1DRAFT_74839 {ECO:0000313|EMBL:EGO60072.1};
OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO60072.1};
RN [1] {ECO:0000313|EMBL:EGO60072.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO60072.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Submitted (APR-2011) 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}.
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DR EMBL; GL891302; EGO60072.1; -; Genomic_DNA.
DR RefSeq; XP_009847440.1; XM_009849138.1.
DR AlphaFoldDB; F8MF20; -.
DR GeneID; 20829748; -.
DR KEGG; nte:NEUTE1DRAFT74839; -.
DR VEuPathDB; FungiDB:NEUTE1DRAFT_74839; -.
DR HOGENOM; CLU_020273_2_4_1; -.
DR OrthoDB; 1328905at2759; -.
DR Proteomes; UP000008065; 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 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 Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT DOMAIN 241..370
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 44454 MW; D51EA12907994822 CRC64;
MCPAPTSDAQ SSQADNATTS QLPSFYSPKR SENTSEQSRD NGDVESVDLS STSAQPTTTP
AITLDTSDNL STHSSVPSTP LSQPPPPSLL SPSFTPPQTP GTATPSTSIT SLSLSEPRGI
PVDSSIPTGG CGTKKPKLLE SLPHVECIVR ARIPTTNGAE MFLHLYTNDV DNKEHLAIVF
GNNIRSESLD RVREGETEMD RLVRGAYTGR LYPGRTTSRE PGVGETKKED QEEKAEEKKQ
VPLVRIHSEC YTGETVWSAR CDCGEQLDEA ARLMSLPSNT AGGIIIYLRQ EGRGIGLGEK
LKAYNLQDLG SDTVEANLLL RHPADARSYG LATAMLRDLG QKEIRLLTNN PDKIRAVEGP
NREIVVTERV AMVPLSWKGK GGFRAPEVEG YLKTKIEKMG HMLDMGALPQ
//
