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Database: UniProt
Entry: A0A1R3XEJ8_9MICO
LinkDB: A0A1R3XEJ8_9MICO
Original site: A0A1R3XEJ8_9MICO 
ID   A0A1R3XEJ8_9MICO        Unreviewed;       428 AA.
AC   A0A1R3XEJ8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=SAMN05880545_2992 {ECO:0000313|EMBL:SIT88383.1};
OS   Microbacterium sp. RU33B.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1907390 {ECO:0000313|EMBL:SIT88383.1, ECO:0000313|Proteomes:UP000187047};
RN   [1] {ECO:0000313|EMBL:SIT88383.1, ECO:0000313|Proteomes:UP000187047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU33B {ECO:0000313|EMBL:SIT88383.1,
RC   ECO:0000313|Proteomes:UP000187047};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate
CC       and 3,4-dihydroxy-2-butanone 4-phosphate.
CC       {ECO:0000256|ARBA:ARBA00002284}.
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=D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate +
CC         formate + H(+); Xref=Rhea:RHEA:18457, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:58121, ChEBI:CHEBI:58830;
CC         EC=4.1.99.12; Evidence={ECO:0000256|ARBA:ARBA00000141};
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; 2-hydroxy-3-
CC       oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004904}.
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}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the DHBP synthase
CC       family. {ECO:0000256|ARBA:ARBA00005520}.
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DR   EMBL; FTPO01000003; SIT88383.1; -; Genomic_DNA.
DR   RefSeq; WP_076683249.1; NZ_FTPO01000003.1.
DR   AlphaFoldDB; A0A1R3XEJ8; -.
DR   STRING; 1907390.SAMN05880545_2992; -.
DR   OrthoDB; 9793111at2; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000187047; Unassembled WGS sequence.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-EC.
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; 3.90.870.10; DHBP synthase; 1.
DR   Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 1.
DR   HAMAP; MF_00179; RibA; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR000422; DHBP_synthase_RibB.
DR   InterPro; IPR032677; GTP_cyclohydro_II.
DR   InterPro; IPR000926; RibA.
DR   InterPro; IPR036144; RibA-like_sf.
DR   NCBIfam; TIGR00505; ribA; 1.
DR   NCBIfam; TIGR00506; ribB; 1.
DR   PANTHER; PTHR21327:SF18; 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR   Pfam; PF00926; DHBP_synthase; 1.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   PIRSF; PIRSF001259; RibA; 1.
DR   SUPFAM; SSF142695; RibA-like; 1.
DR   SUPFAM; SSF55821; YrdC/RibB; 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|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00179};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00179}; Reference proteome {ECO:0000313|Proteomes:UP000187047};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP-
KW   Rule:MF_00179};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00179}.
FT   DOMAIN          222..384
FT                   /note="GTP cyclohydrolase II"
FT                   /evidence="ECO:0000259|Pfam:PF00925"
FT   ACT_SITE        340
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT   ACT_SITE        342
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT   BINDING         263..267
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT   BINDING         279
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT   BINDING         281
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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         306..308
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT   BINDING         328
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT   BINDING         363
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
FT   BINDING         368
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00179"
SQ   SEQUENCE   428 AA;  45554 MW;  455C6A9B0EE2F225 CRC64;
     MSLATIPDAL DALRAGRPVI VADDENRENE GDVILSAELA TPEWIAWTVR WSSGFICAPM
     PADWADNLDL PPMVAMNEDA RGTAYTVSVD AADRVSTGIS ASDRAHTLNV LANPESTPSS
     VIRPGHILPL RAVDGGVRER GGHTEAAVDL MRLAGLQPVG AIAEVVAEDG SMMRLPGLIE
     LGERDGVLVI TIEQLIAYLD ETEPVDVPHA HAVHKRRVSL RAEAQVPTSH GDFRFLAYKD
     RVTGTDHLAV VSGDLTEDAP LVRVHSECLT GEAFGSLKCE CGPQLDAALD AIETDGGVVI
     YMRGHEGRGI GLINKLRAYS LQERGLDTVD ANLALGLPAD ARDYAAAAGI LADLGVDRIR
     LLTNNTDKVN QLRGLGLDIV EQVPLLVGVG PNNHQYLATK AERMGHIIAE QDLSDALNSS
     RLTEGAGA
//
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