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Database: UniProt
Entry: B9LSB3_HALLT
LinkDB: B9LSB3_HALLT
Original site: B9LSB3_HALLT 
ID   B9LSB3_HALLT            Unreviewed;       236 AA.
AC   B9LSB3;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|RuleBase:RU003843};
DE            Short=DHBP synthase {ECO:0000256|RuleBase:RU003843};
DE            EC=4.1.99.12 {ECO:0000256|RuleBase:RU003843};
GN   OrderedLocusNames=Hlac_0354 {ECO:0000313|EMBL:ACM55958.1};
OS   Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS   34).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=416348 {ECO:0000313|EMBL:ACM55958.1, ECO:0000313|Proteomes:UP000000740};
RN   [1] {ECO:0000313|EMBL:ACM55958.1, ECO:0000313|Proteomes:UP000000740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34
RC   {ECO:0000313|Proteomes:UP000000740};
RX   PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA   Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA   Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA   Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA   Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA   Woese C.R., Kyrpides N.C.;
RT   "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT   strain ACAM 34.";
RL   Stand. Genomic Sci. 11:70-70(2016).
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate
CC       and 3,4-dihydroxy-2-butanone 4-phosphate.
CC       {ECO:0000256|RuleBase:RU003843}.
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|RuleBase:RU003843};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU003843};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU003843};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000256|RuleBase:RU003843};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-
CC       oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
CC       {ECO:0000256|RuleBase:RU003843}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU003843}.
CC   -!- SIMILARITY: Belongs to the DHBP synthase family.
CC       {ECO:0000256|RuleBase:RU003843}.
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DR   EMBL; CP001365; ACM55958.1; -; Genomic_DNA.
DR   RefSeq; WP_012659599.1; NC_012029.1.
DR   AlphaFoldDB; B9LSB3; -.
DR   GeneID; 7399746; -.
DR   KEGG; hla:Hlac_0354; -.
DR   eggNOG; arCOG01320; Archaea.
DR   HOGENOM; CLU_020273_3_2_2; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000000740; Chromosome 1.
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   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR000422; DHBP_synthase_RibB.
DR   NCBIfam; TIGR00506; ribB; 1.
DR   PANTHER; PTHR21327:SF46; 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR   Pfam; PF00926; DHBP_synthase; 1.
DR   SUPFAM; SSF55821; YrdC/RibB; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|RuleBase:RU003843};
KW   Magnesium {ECO:0000256|RuleBase:RU003843};
KW   Manganese {ECO:0000256|RuleBase:RU003843};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003843};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000740};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW   ECO:0000256|RuleBase:RU003843}.
SQ   SEQUENCE   236 AA;  24745 MW;  30C31D76C3A7452F CRC64;
     MRADADTDVD AVPGSDADSV NRALDAFRAG DPVCVHDFAD REGETDIIYP AGAVDEAAVA
     HMRNDAGGLI CVAVADSVAD AFGLPFLADA LDHPAVNDDP EYDDRSSFSL PVNHRETFTG
     ITDEDRARTI VELAVSAAAV DADPAGYDPD DFAAEFRAPG HVHVLRGAHD GLRGRTGHTE
     LGLAMAEAVD AAPAAVVCEM LDDETGAALT PADAEAYARR RQIPYVEGAA LVEAFK
//
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