ID Q5UY63_HALMA Unreviewed; 224 AA.
AC Q5UY63;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
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 Name=ribA {ECO:0000313|EMBL:AAV47790.1};
GN Synonyms=ribB {ECO:0000313|EMBL:QCP92470.1};
GN OrderedLocusNames=rrnAC3073 {ECO:0000313|EMBL:AAV47790.1};
GN ORFNames=E6P14_17000 {ECO:0000313|EMBL:QCP92470.1};
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569 {ECO:0000313|EMBL:AAV47790.1, ECO:0000313|Proteomes:UP000001169};
RN [1] {ECO:0000313|EMBL:AAV47790.1, ECO:0000313|Proteomes:UP000001169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:AAV47790.1}, and ATCC 43049 / DSM
RC 3752 / JCM 8966 / VKM B-1809 {ECO:0000313|Proteomes:UP000001169};
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [2] {ECO:0000313|EMBL:QCP92470.1, ECO:0000313|Proteomes:UP000298722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:QCP92470.1,
RC ECO:0000313|Proteomes:UP000298722};
RA DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA Roberts R.J.;
RT "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT mediterranei.";
RL Submitted (APR-2019) 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|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; AY596297; AAV47790.1; -; Genomic_DNA.
DR EMBL; CP039138; QCP92470.1; -; Genomic_DNA.
DR RefSeq; WP_011224602.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5UY63; -.
DR STRING; 272569.rrnAC3073; -.
DR PaxDb; 272569-rrnAC3073; -.
DR EnsemblBacteria; AAV47790; AAV47790; rrnAC3073.
DR GeneID; 40153890; -.
DR KEGG; hma:rrnAC3073; -.
DR PATRIC; fig|272569.17.peg.3619; -.
DR eggNOG; arCOG01320; Archaea.
DR HOGENOM; CLU_020273_3_2_2; -.
DR UniPathway; UPA00275; UER00399.
DR Proteomes; UP000001169; Chromosome I.
DR Proteomes; UP000298722; Chromosome.
DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:AAV47790.1};
KW Lyase {ECO:0000256|RuleBase:RU003843, ECO:0000313|EMBL:QCP92470.1};
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:UP000001169};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW ECO:0000256|RuleBase:RU003843}.
SQ SEQUENCE 224 AA; 23598 MW; AB74DD105F12BB0C CRC64;
MSRSEETAVD ADSVADAVAA FARGEPVLIH DAADREGETD LVYPAGAVSP DAVARMRNDA
GGLVCVALSD RVAEALELPF MQEVLSHPTA ADHDLAYDER SSFSLTVNHR DTFTGITDDD
RSLTIQELAA VAADPDPDAF SDAFRSPGHV HLLRAAPDGL ADREGHTELA LALAAAADQP
EAAVVCEMLD DETGAALPPA AARAYAEREG LVYVEGASLL ERFD
//
