ID A0A0G3LNM0_XANCT Unreviewed; 374 AA.
AC A0A0G3LNM0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=GTP cyclohydrolase-2 {ECO:0000256|HAMAP-Rule:MF_00179};
DE EC=3.5.4.25 {ECO:0000256|HAMAP-Rule:MF_00179};
DE AltName: Full=GTP cyclohydrolase II {ECO:0000256|HAMAP-Rule:MF_00179};
GN Name=ribA {ECO:0000256|HAMAP-Rule:MF_00179,
GN ECO:0000313|EMBL:QEO25230.1};
GN ORFNames=F0H32_02560 {ECO:0000313|EMBL:QEO25230.1}, FD63_02510
GN {ECO:0000313|EMBL:AKK66432.1};
OS Xanthomonas translucens pv. undulosa.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=487909 {ECO:0000313|EMBL:QEO25230.1, ECO:0000313|Proteomes:UP000324457};
RN [1] {ECO:0000313|Proteomes:UP000035194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xtu4699 {ECO:0000313|Proteomes:UP000035194};
RA Peng Z., Potnis N., Jones J., Liu Z., White F.F., Liu S.;
RT "A complete genome of Xanthomonas translucens and the full TAL effector
RT gene content using long read sequencing.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKK66432.1, ECO:0000313|Proteomes:UP000035194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xtu 4699 {ECO:0000313|EMBL:AKK66432.1}, and Xtu4699
RC {ECO:0000313|Proteomes:UP000035194};
RX PubMed=26729225; DOI=10.1186/s12864-015-2348-9;
RA Peng Z., Hu Y., Xie J., Potnis N., Akhunova A., Jones J., Liu Z.,
RA White F.F., Liu S.;
RT "Long read and single molecule DNA sequencing simplifies genome assembly
RT and TAL effector gene analysis of Xanthomonas translucens.";
RL BMC Genomics 17:21-21(2016).
RN [3] {ECO:0000313|EMBL:QEO25230.1, ECO:0000313|Proteomes:UP000324457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LW16 {ECO:0000313|EMBL:QEO25230.1,
RC ECO:0000313|Proteomes:UP000324457};
RA Peng Z., Huguet-Tapia J.C., White F.;
RT "Xanthomonas translucens pv. undulosa LW16.";
RL Submitted (AUG-2019) 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, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00029293, ECO:0000256|HAMAP-
CC Rule:MF_00179};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00179};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00179};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC ribitylamino)uracil from GTP: step 1/4. {ECO:0000256|ARBA:ARBA00004853,
CC ECO:0000256|HAMAP-Rule:MF_00179}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family.
CC {ECO:0000256|HAMAP-Rule:MF_00179}.
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DR EMBL; CP008714; AKK66432.1; -; Genomic_DNA.
DR EMBL; CP043540; QEO25230.1; -; Genomic_DNA.
DR RefSeq; WP_003467867.1; NZ_MADU01000086.1.
DR AlphaFoldDB; A0A0G3LNM0; -.
DR STRING; 487909.FD63_02510; -.
DR GeneID; 66888513; -.
DR KEGG; xtn:FD63_02510; -.
DR UniPathway; UPA00275; UER00400.
DR Proteomes; UP000035194; Chromosome.
DR Proteomes; UP000324457; 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; GTP cyclohydrolase II; 1.
DR HAMAP; MF_00179; RibA; 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 PIRSF; PIRSF001259; RibA; 1.
DR SUPFAM; SSF142695; RibA-like; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00179};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00179};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00179};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00179};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP-
KW Rule:MF_00179}; Zinc {ECO:0000256|HAMAP-Rule:MF_00179}.
FT DOMAIN 177..340
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
FT ACT_SITE 296
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 219..223
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 240
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 262..264
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 284
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 319
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 324
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
SQ SEQUENCE 374 AA; 39583 MW; FC3CB6D700005D91 CRC64;
MTSPAPLICT PPFGDPAAIR AERAASELRA GRPVVIEGGD GQARAVLALD SSTAQSYLSF
TQAAAQRHYL FLTPTRAQVL GLVAPQGARI ALAEQSYDAL AALAYLRSGT LPTHWLPGDA
LDAGAVEIAR LGLLLPAIVA VDLDADSTFQ GCQSLQLDDL KHGCATTTSG SYELVTRTQV
PLRDLGSSEF VVFRGGVAQR DQVAIVIGQP DLSVPVPVRV HSSCLTGDLF GSLKCDCGDQ
LRHGLAKLKE LGGGVLLYLD QEGRGTGIAT KLRAYGYQHD GLDTIDADAQ LGFGADERRY
GSAVAMLRGL GIQRVRLLTN NLSKAERLRA AGIDVVERIP ITGAITAENE RYLRTKATRA
GHALDVDALI HAAR
//
