ID A0A165PBY1_9GAMM Unreviewed; 369 AA.
AC A0A165PBY1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|ARBA:ARBA00018836};
DE EC=4.1.99.12 {ECO:0000256|ARBA:ARBA00012153};
GN ORFNames=A3709_10855 {ECO:0000313|EMBL:KZX51310.1};
OS Halioglobus sp. HI00S01.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Halioglobus.
OX NCBI_TaxID=1822214 {ECO:0000313|EMBL:KZX51310.1, ECO:0000313|Proteomes:UP000077184};
RN [1] {ECO:0000313|EMBL:KZX51310.1, ECO:0000313|Proteomes:UP000077184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI00S01 {ECO:0000313|EMBL:KZX51310.1,
RC ECO:0000313|Proteomes:UP000077184};
RA Sosa O.A.;
RT "Microbial cycling of marine high molecular weight dissolved organic
RT matter.";
RL Submitted (MAR-2016) 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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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 -!- SIMILARITY: In the C-terminal section; belongs to the GTP
CC cyclohydrolase II family. {ECO:0000256|ARBA:ARBA00008976}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP synthase
CC family. {ECO:0000256|ARBA:ARBA00005520}.
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:KZX51310.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LWEE01000387; KZX51310.1; -; Genomic_DNA.
DR RefSeq; WP_066059643.1; NZ_LWEE01000387.1.
DR AlphaFoldDB; A0A165PBY1; -.
DR OrthoDB; 9793111at2; -.
DR UniPathway; UPA00275; UER00399.
DR Proteomes; UP000077184; Unassembled WGS sequence.
DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.870.10; DHBP synthase; 1.
DR Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 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; IPR036144; RibA-like_sf.
DR NCBIfam; TIGR00506; ribB; 1.
DR PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR PANTHER; PTHR21327:SF48; RIBOFLAVIN BIOSYNTHESIS PROTEIN RIBBA; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000077184};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT DOMAIN 210..364
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
SQ SEQUENCE 369 AA; 39154 MW; 465BCCFD18337E50 CRC64;
MQVNTVDELI SDLRQGRMVV LLDDDADSHN EGVVMVAAEH VDADQVNFMA RKARGLVCLT
LTEERCRQLD LPPMVEDAMG EKSNFTLSIE ATVGIDTGIS AADRARTVHA AVAPHAVPGD
IVQPGHIFPL EALPGGVLTR AGHTEAGCDY ARLAGLLPAA VIADILTDDG TLADGPALAE
FAAKHGLKIG TVADLIHFRM VNERTIRKVR EGKVNTAHGE FNLTAYRDQT AGDVHLALSM
GEISEAEPTL VRVHVQSALR DLVGSEIEGQ PTWSMARCMQ TVAEAGKGVI VLLAREEGPE
QLLNSIDMAL GGEFTAGSGS AVYNTVGLGS QILRDLGVGK IHLMGAPIKY NALSGFDLEV
LDFVSPKAD
//
