ID Q2S2E8_SALRD Unreviewed; 455 AA.
AC Q2S2E8;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
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 OrderedLocusNames=SRU_1510 {ECO:0000313|EMBL:ABC44791.1};
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC44791.1, ECO:0000313|Proteomes:UP000008674};
RN [1] {ECO:0000313|EMBL:ABC44791.1, ECO:0000313|Proteomes:UP000008674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31
RC {ECO:0000313|Proteomes:UP000008674};
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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}.
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DR EMBL; CP000159; ABC44791.1; -; Genomic_DNA.
DR RefSeq; WP_011404259.1; NC_007677.1.
DR RefSeq; YP_445633.1; NC_007677.1.
DR AlphaFoldDB; Q2S2E8; -.
DR STRING; 309807.SRU_1510; -.
DR EnsemblBacteria; ABC44791; ABC44791; SRU_1510.
DR KEGG; sru:SRU_1510; -.
DR eggNOG; COG0807; Bacteria.
DR eggNOG; COG1985; Bacteria.
DR HOGENOM; CLU_047828_0_0_10; -.
DR OrthoDB; 9793111at2; -.
DR UniPathway; UPA00275; UER00400.
DR Proteomes; UP000008674; Chromosome.
DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:InterPro.
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:0050661; F:NADP binding; IEA:InterPro.
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; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 1.
DR HAMAP; MF_00179; RibA; 1.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR032677; GTP_cyclohydro_II.
DR InterPro; IPR000926; RibA.
DR InterPro; IPR036144; RibA-like_sf.
DR InterPro; IPR011549; RibD_C.
DR InterPro; IPR002734; RibDG_C.
DR NCBIfam; TIGR00505; ribA; 1.
DR NCBIfam; TIGR00227; ribD_Cterm; 1.
DR PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR PANTHER; PTHR21327:SF29; GTP CYCLOHYDROLASE-2; 1.
DR Pfam; PF00925; GTP_cyclohydro2; 1.
DR Pfam; PF01872; RibD_C; 1.
DR SUPFAM; SSF53597; Dihydrofolate reductase-like; 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}; Reference proteome {ECO:0000313|Proteomes:UP000008674};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP-
KW Rule:MF_00179}; Zinc {ECO:0000256|HAMAP-Rule:MF_00179}.
FT DOMAIN 8..172
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
FT DOMAIN 232..443
FT /note="Bacterial bifunctional deaminase-reductase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01872"
FT ACT_SITE 129
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT ACT_SITE 131
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 52..56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 95..97
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 117
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 152
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 157
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
SQ SEQUENCE 455 AA; 49656 MW; 0384A719578E78AE CRC64;
MEIPSVERLT SARIPTVDGE FSLSLYENSK DDKDHLALAC GDVADGEDVL VRVHSECFTG
DVLGSLRCDC GEQLDASMRR IAKNGRGILL YLRQEGRGIG LLSKLRAYNL QDDGYDTVEA
NRILGHGADE RDYAIAARIL DDLGVSSARL LTNNPQKIES LAEHGVEITE RISLEPHVNR
HNAEYLRTKV NRMRHILDLG PANGHAQGNA HGTSLRDLKQ RIDRYFAEKG RPFVTLTYAQ
SLDGSIASTS GTPLPISSEQ ALRFTHQLRA LHDGILVGIG TVLADDPRLT VRHNDGTHPV
PIVLDSSLRF PSDAQLLAGD GPDPLIVTSP NADPDRKERL EAHGGTVIEL SCGPEGGICV
KTLLRTLGER DFSSVMVEGG TSILTSFLRR QCAQRVIVTV APMFVGGTAA LSSLAPEDQD
THARSDFPRL DNIQQRWYGE DLVLEGDPVW PVASE
//
