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Database: UniProt
Entry: A0A0L0QK47_VIRPA
LinkDB: A0A0L0QK47_VIRPA
Original site: A0A0L0QK47_VIRPA 
ID   A0A0L0QK47_VIRPA        Unreviewed;       251 AA.
AC   A0A0L0QK47;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=GTP cyclohydrolase II {ECO:0000256|ARBA:ARBA00012762};
DE            EC=3.5.4.25 {ECO:0000256|ARBA:ARBA00012762};
GN   ORFNames=AFK71_10560 {ECO:0000313|EMBL:KNE19005.1};
OS   Virgibacillus pantothenticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=1473 {ECO:0000313|EMBL:KNE19005.1, ECO:0000313|Proteomes:UP000036780};
RN   [1] {ECO:0000313|Proteomes:UP000036780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26 {ECO:0000313|Proteomes:UP000036780};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-10053 dsm26.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00043932}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC       ribitylamino)uracil from GTP: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004853}.
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:KNE19005.1}.
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DR   EMBL; LGTO01000007; KNE19005.1; -; Genomic_DNA.
DR   RefSeq; WP_050351503.1; NZ_LGTO01000007.1.
DR   AlphaFoldDB; A0A0L0QK47; -.
DR   GeneID; 66872007; -.
DR   PATRIC; fig|1473.5.peg.625; -.
DR   OrthoDB; 9793111at2; -.
DR   UniPathway; UPA00275; -.
DR   Proteomes; UP000036780; 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:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; GTP cyclohydrolase II; 1.
DR   InterPro; IPR032677; GTP_cyclohydro_II.
DR   InterPro; IPR000926; RibA.
DR   InterPro; IPR036144; RibA-like_sf.
DR   PANTHER; PTHR21327:SF18; 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   SUPFAM; SSF142695; RibA-like; 1.
PE   4: Predicted;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KNE19005.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036780};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT   DOMAIN          78..220
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000259|Pfam:PF00925"
SQ   SEQUENCE   251 AA;  28488 MW;  4334A4AD0C048144 CRC64;
     MEQQIKLDPQ VLSILQDKIQ RIDTEYDSIY LVGPIQLPVN LGGKTTLFHW YCWWNYEEVT
     EDYEAIIAKL SSANLAEYQQ SSVLVYGDFA TADHALVRMH SICHTGDIFG SKRCDCGFQL
     REAMERIKEN GSGALFYLAN HEGRGIGLFS KAMAYILQEN GYDTVEANER LGFVNDSRNY
     QNALHVLKKL RQKPVTVITN NPEKLVAFKD AGISINGRTP LWGDVSEYNR KYLQTKVTKS
     GHFQPEGALL Q
//
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