ID A0A097EIH7_9SPHN Unreviewed; 353 AA.
AC A0A097EIH7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 ORFNames=MC45_14490 {ECO:0000313|EMBL:AIT07380.1};
OS Sphingomonas taxi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1549858 {ECO:0000313|EMBL:AIT07380.1, ECO:0000313|Proteomes:UP000033200};
RN [1] {ECO:0000313|EMBL:AIT07380.1, ECO:0000313|Proteomes:UP000033200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55669 {ECO:0000313|EMBL:AIT07380.1,
RC ECO:0000313|Proteomes:UP000033200};
RA Zhou Y., Ma T., Liu T.;
RT "Using Illumina technology Improving SMRT sequencing Genome Assembly by
RT RASTools.";
RL Submitted (SEP-2014) 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; CP009571; AIT07380.1; -; Genomic_DNA.
DR RefSeq; WP_038664609.1; NZ_CP009571.1.
DR AlphaFoldDB; A0A097EIH7; -.
DR STRING; 1549858.MC45_14490; -.
DR KEGG; stax:MC45_14490; -.
DR eggNOG; COG0807; Bacteria.
DR HOGENOM; CLU_020273_1_2_5; -.
DR UniPathway; UPA00275; UER00400.
DR Proteomes; UP000033200; 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 NCBIfam; TIGR00505; ribA; 1.
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 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:UP000033200};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP-
KW Rule:MF_00179}; Zinc {ECO:0000256|HAMAP-Rule:MF_00179}.
FT DOMAIN 167..329
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
FT REGION 333..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT ACT_SITE 287
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 251..253
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 308
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT BINDING 313
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
SQ SEQUENCE 353 AA; 37165 MW; 04E2E27AAF07408A CRC64;
MSGARDVARA IDALRRGWPI AIHAPGEPPL PLLAVETADP CGRETFMTGG VGPLLISDGR
AATLKLTNQL AAADPDTPVV IEAAPWLDFS TAVALADPQF DLATPLKGPF RTTAVTRPAA
SLAAIRLARI AGLLPAFFID GSGPEVTIAP AAIDAHQDAR ALHLATRARL PVDGAEDAEI
VAFRAPDSSD EHVALLIGQP DGNPPLVRLH SECLTGDVLG SLKCDCGPQL RAAIAAIAAN
GWGILLYLRQ EGRGIGLVNK LRAYALQDQG FDTVDANVRL GFAIDSRDFG VAARMLDLLG
QRAVRLMTNN PAKVAGLEAA GVSVVERVPH QLPPNPHNAR YLATKRDRTG HQL
//
