ID F0WUY4_9STRA Unreviewed; 385 AA.
AC F0WUY4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=3,4-dihydroxy-2-butanone-4-phosphate synthase {ECO:0000256|ARBA:ARBA00012153};
DE EC=4.1.99.12 {ECO:0000256|ARBA:ARBA00012153};
GN Name=AlNc14C282G10131 {ECO:0000313|EMBL:CCA25220.1};
GN ORFNames=ALNC14_113640 {ECO:0000313|EMBL:CCA25220.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA25220.1};
RN [1] {ECO:0000313|EMBL:CCA25220.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA25220.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FR824327; CCA25220.1; -; Genomic_DNA.
DR AlphaFoldDB; F0WUY4; -.
DR EnsemblProtists; CCA25220; CCA25220; ALNC14_113640.
DR HOGENOM; CLU_020273_1_2_1; -.
DR UniPathway; UPA00275; -.
DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:InterPro.
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 HAMAP; MF_00180; RibB; 1.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR000422; DHBP_synthase_RibB.
DR InterPro; IPR036144; RibA-like_sf.
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 PIRSF; PIRSF001259; RibA; 2.
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 Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
SQ SEQUENCE 385 AA; 42257 MW; 38FE0D1AE632F437 CRC64;
MSVVNSSVAP LPSVLSTPLK AVNSVKEAFS PMHNTQVATI EQALEAIRKG ELVIVMDNED
RENEGDLIAA AEFATEERLA FMVRHSTGIV CVPIPEQRTM ELRLPAMVDD NTEAHKCKFT
ITVDLREGNT TGVSAADRAR TIRALADPSI SHDAYNRPGH IFPLKAKEGG VIARAGHTEA
AVDLARLAGC RPAGYICEIN DDNGKMLRRA DLHKFAAEHK LHLITISDMI RYRVCHETLL
HPLNTSNFKA METPFGSWKL FQYDALVCEL EIDLLVLGSV EKASKVPVFI AAGEALSTTV
DMQWAQKHIM SSSKLGVIIY MRKTANLIEV SGAFMGGQSI FGLAMQAVKQ LDVQSVRLMT
RTPYPFDTEG FGVCIDGTEE FPKCL
//
