RIB1_PICGU
ID RIB1_PICGU Reviewed; 332 AA.
AC P50139; A5DL76;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=GTP cyclohydrolase-2;
DE EC=3.5.4.25;
DE AltName: Full=GTP cyclohydrolase II;
GN Name=RIB1; ORFNames=PGUG_04027;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8533469; DOI=10.1002/yea.320111005;
RA Liauta-Teglivets O.Y., Hasslacher M., Boretsky Y.R., Kohlwein S.D.,
RA Shavlovskii G.M.;
RT "Molecular cloning of the GTP-cyclohydrolase structural gene RIB1 of Pichia
RT guilliermondii involved in riboflavin biosynthesis.";
RL Yeast 11:945-952(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6-
CC ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and
CC pyrophosphate. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC ribitylamino)uracil from GTP: step 1/4.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA88916.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z49093; CAA88916.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CH408159; EDK39929.1; -; Genomic_DNA.
DR PIR; S57373; S57373.
DR RefSeq; XP_001483298.1; XM_001483248.1.
DR AlphaFoldDB; P50139; -.
DR SMR; P50139; -.
DR STRING; 4929.XP_001483298.1; -.
DR PRIDE; P50139; -.
DR EnsemblFungi; EDK39929; EDK39929; PGUG_04027.
DR GeneID; 5125322; -.
DR KEGG; pgu:PGUG_04027; -.
DR VEuPathDB; FungiDB:PGUG_04027; -.
DR eggNOG; KOG1284; Eukaryota.
DR HOGENOM; CLU_020273_2_4_1; -.
DR InParanoid; P50139; -.
DR OMA; RLPNVEC; -.
DR OrthoDB; 1101017at2759; -.
DR UniPathway; UPA00275; UER00400.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00641; GTP_cyclohydro2; 1.
DR Gene3D; 3.40.50.10990; -; 1.
DR InterPro; IPR032677; GTP_cyclohydro_II.
DR InterPro; IPR000926; RibA.
DR InterPro; IPR036144; RibA-like_sf.
DR Pfam; PF00925; GTP_cyclohydro2; 1.
DR SUPFAM; SSF142695; SSF142695; 1.
DR TIGRFAMs; TIGR00505; ribA; 1.
PE 3: Inferred from homology;
KW GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Riboflavin biosynthesis; Zinc.
FT CHAIN 1..332
FT /note="GTP cyclohydrolase-2"
FT /id="PRO_0000151785"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 25..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 250
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 171..175
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 214..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 147
FT /note="L -> V (in Ref. 1; CAA88916)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="E -> V (in Ref. 1; CAA88916)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="A -> S (in Ref. 1; CAA88916)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="A -> P (in Ref. 1; CAA88916)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="S -> T (in Ref. 1; CAA88916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 37147 MW; 964E7D0F41FBA448 CRC64;
MASKDIVHPQ PERRHGSETH EFTMPLLSPT LTPSHIPSQT PQIPPEVPAE VRDRLPLPET
LPVVKCMARA RIPTTQGPEI FLHLYENNVD NKEHLAIVFG EDVRSKTLYQ KRPNETQQDR
MTRGAYVGRL FPGRTEADYD SESNLRLNFD ENGQLIRDPS TTCSGEPILA RIHSECYTGE
TAWSARCDCG EQFDEAGRLM GEAGHGCIVY LRQEGRGIGL GEKLKAYNLQ DLGADTVQAN
LMLRHPADAR SFSLATAILL DLGLNEIKLL TNNPDKIAAV EGRNREVKVV ERVPMVPLAW
RSENGIKSKE IEGYLSAKIE RMGHLLEKPL KI
