RIBA_HELPY
ID RIBA_HELPY Reviewed; 192 AA.
AC O08315;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 120.
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=HP_0802;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RX PubMed=9574900; DOI=10.1007/s004300050062;
RA Bereswill S., Fassbinder F., Voelzing C., Covacci A., Haas R., Kist M.;
RT "Hemolytic properties and riboflavin synthesis of Helicobacter pylori:
RT cloning and functional characterization of the ribA gene encoding GTP-
RT cyclohydrolase II that confers hemolytic activity to Escherichia coli.";
RL Med. Microbiol. Immunol. 186:177-187(1998).
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:0000305|PubMed:9574900}.
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 -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family.
CC {ECO:0000255|HAMAP-Rule:MF_00179}.
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DR EMBL; AE000511; AAD07851.1; -; Genomic_DNA.
DR EMBL; Y12062; CAA72785.1; -; Genomic_DNA.
DR PIR; B64620; B64620.
DR RefSeq; NP_207595.1; NC_000915.1.
DR RefSeq; WP_000825074.1; NC_018939.1.
DR PDB; 4RL4; X-ray; 2.20 A; A/B=1-192.
DR PDBsum; 4RL4; -.
DR AlphaFoldDB; O08315; -.
DR SMR; O08315; -.
DR DIP; DIP-3449N; -.
DR IntAct; O08315; 1.
DR MINT; O08315; -.
DR STRING; 85962.C694_04110; -.
DR PaxDb; O08315; -.
DR EnsemblBacteria; AAD07851; AAD07851; HP_0802.
DR KEGG; hpy:HP_0802; -.
DR PATRIC; fig|85962.47.peg.854; -.
DR eggNOG; COG0807; Bacteria.
DR OMA; GQGFILY; -.
DR PhylomeDB; O08315; -.
DR BRENDA; 3.5.4.25; 2604.
DR UniPathway; UPA00275; UER00400.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW Reference proteome; Riboflavin biosynthesis; Zinc.
FT CHAIN 1..192
FT /note="GTP cyclohydrolase-2"
FT /id="PRO_0000151761"
FT ACT_SITE 126
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT ACT_SITE 128
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT BINDING 50..54
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT BINDING 66
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="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT BINDING 92..94
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT BINDING 114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT BINDING 149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT BINDING 154
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00179"
FT CONFLICT 38
FT /note="V -> I (in Ref. 2; CAA72785)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="S -> P (in Ref. 2; CAA72785)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="L -> F (in Ref. 2; CAA72785)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="A -> P (in Ref. 2; CAA72785)"
FT /evidence="ECO:0000305"
FT CONFLICT 98..100
FT /note="LFN -> YLT (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="V -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="R -> H (in Ref. 2; CAA72785)"
FT /evidence="ECO:0000305"
FT STRAND 1..14
FT /evidence="ECO:0007829|PDB:4RL4"
FT STRAND 17..26
FT /evidence="ECO:0007829|PDB:4RL4"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:4RL4"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:4RL4"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:4RL4"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:4RL4"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:4RL4"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:4RL4"
FT TURN 92..96
FT /evidence="ECO:0007829|PDB:4RL4"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:4RL4"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:4RL4"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:4RL4"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:4RL4"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:4RL4"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:4RL4"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:4RL4"
SQ SEQUENCE 192 AA; 21715 MW; 1F34B0E1FC3A73A4 CRC64;
MKRLEVSNQA KLPTQFGEFY IQCFREKGSN GSKDHLVVFT PNFSQNPLVR LHSECLTGDA
LGSQKCDCGG ALQMALERIS KEGGLVIYLR QEGRGIGLFN KVNAYALQDK GYDTIQANEM
IGFKDDERDY SVAGEILEYY RIKKMRLLTN NPKKIAALEK YAEVTRESLI VCANEHNQGY
LEVKKLKMGH LL
