ID A0A2D6EBA5_9SPHN Unreviewed; 357 AA.
AC A0A2D6EBA5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:MAL27577.1};
GN ORFNames=CL820_17140 {ECO:0000313|EMBL:MAL27577.1};
OS Croceicoccus sp.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceicoccus.
OX NCBI_TaxID=1927144 {ECO:0000313|EMBL:MAL27577.1, ECO:0000313|Proteomes:UP000231504};
RN [1] {ECO:0000313|Proteomes:UP000231504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Graham E.D., Heidelberg J.F.;
RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT Global Oceans.";
RL Submitted (SEP-2017) 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|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: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|HAMAP-
CC Rule:MF_00179}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family.
CC {ECO:0000256|HAMAP-Rule:MF_00179}.
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:MAL27577.1}.
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DR EMBL; NZMY01000053; MAL27577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D6EBA5; -.
DR UniPathway; UPA00275; UER00400.
DR Proteomes; UP000231504; Unassembled WGS sequence.
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 NCBIfam; TIGR00505; ribA; 1.
DR PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR PANTHER; PTHR21327:SF48; RIBOFLAVIN BIOSYNTHESIS PROTEIN RIBBA; 1.
DR Pfam; PF00925; GTP_cyclohydro2; 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 165..332
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT ACT_SITE 291
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 208..212
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 229
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 255..257
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 277
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 312
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 317
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
SQ SEQUENCE 357 AA; 37850 MW; 7C7D916835F4346F CRC64;
MTAPSPSRRT AQAVDALRHG WPVRVSGGDG ALLLLPAETG HDAGGSAARR LLISAARAAT
LKLINQKDAA VPDAPALIRA AEPFTLQAAR ELADPSRDLA NPLSGPFRAD PLEASEAAKA
AMALARIAGI LPAFLVAPEP AGEAVELSAS DIAAFEDPAR LTIQARAHLP THAAEQAEIV
AFRAPDDLRE HVALVIGRQN GERVPLVRLH SECLTGDVLG SLKCDCGPQL DAALAAMADE
AAGGGWGVLL YLRQEGRGIG LINKLRAYRL QDQGFDTVDA NNRLGLPTDA RDFPVAARML
ELLGVRRIRL LTNNPMKVET LDALGIEVAE RVAHALPANP HNARYLDTKR DRTGHLL
//
