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RIBA_BUCAI
ID   RIBA_BUCAI              Reviewed;         194 AA.
AC   P57359;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=GTP cyclohydrolase-2 {ECO:0000255|HAMAP-Rule:MF_00179};
DE            EC=3.5.4.25 {ECO:0000255|HAMAP-Rule:MF_00179};
DE   AltName: Full=GTP cyclohydrolase II {ECO:0000255|HAMAP-Rule:MF_00179};
GN   Name=ribA {ECO:0000255|HAMAP-Rule:MF_00179}; OrderedLocusNames=BU271;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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:0000255|HAMAP-Rule:MF_00179}.
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:0000255|HAMAP-Rule:MF_00179};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00179};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00179};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC       ribitylamino)uracil from GTP: step 1/4. {ECO:0000255|HAMAP-
CC       Rule:MF_00179}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00179}.
CC   -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family.
CC       {ECO:0000255|HAMAP-Rule:MF_00179}.
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DR   EMBL; BA000003; BAB12981.1; -; Genomic_DNA.
DR   RefSeq; NP_240095.1; NC_002528.1.
DR   RefSeq; WP_009874225.1; NC_002528.1.
DR   AlphaFoldDB; P57359; -.
DR   SMR; P57359; -.
DR   STRING; 107806.10038946; -.
DR   EnsemblBacteria; BAB12981; BAB12981; BAB12981.
DR   KEGG; buc:BU271; -.
DR   PATRIC; fig|107806.10.peg.281; -.
DR   eggNOG; COG0807; Bacteria.
DR   HOGENOM; CLU_020273_2_1_6; -.
DR   OMA; GQGFILY; -.
DR   UniPathway; UPA00275; UER00400.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00641; GTP_cyclohydro2; 1.
DR   Gene3D; 3.40.50.10990; -; 1.
DR   HAMAP; MF_00179; RibA; 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..194
FT                   /note="GTP cyclohydrolase-2"
FT                   /id="PRO_0000151750"
FT   ACT_SITE        124
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT   ACT_SITE        126
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT   BINDING         47..51
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT   BINDING         52
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT   BINDING         68
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT   BINDING         90..92
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT   BINDING         112
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT   BINDING         147
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT   BINDING         152
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
SQ   SEQUENCE   194 AA;  21893 MW;  DA45422AFEFEF0B8 CRC64;
     MQLIEKAMLP TPWGNFLIFG FEEKKNGKNH VALVYGDIKT NTPTLSRVHS ECLTGDAFFS
     LRCDCGSQLE MSMKRISQEG SGVLIYHRQE GRNIGLLNKI KAYALQDRGL DTVQANQKLG
     FSADERDFSL CADIFNILNI KKIRLLTNNP FKVQMLSDAG INIVERVPLI VKKNPKNAYY
     LKTKAEKMGH LLSE
 
 
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