ID K0B9G3_9ARCH Unreviewed; 221 AA.
AC K0B9G3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
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 ORFNames=NKOR_08795 {ECO:0000313|EMBL:AFS81610.1};
OS Candidatus Nitrosopumilus koreensis AR1.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=1229908 {ECO:0000313|EMBL:AFS81610.1, ECO:0000313|Proteomes:UP000006101};
RN [1] {ECO:0000313|EMBL:AFS81610.1, ECO:0000313|Proteomes:UP000006101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR1 {ECO:0000313|EMBL:AFS81610.1,
RC ECO:0000313|Proteomes:UP000006101};
RX PubMed=23209206; DOI=10.1128/JB.01857-12;
RA Park S.J., Kim J.G., Jung M.Y., Kim S.J., Cha I.T., Kwon K., Lee J.H.,
RA Rhee S.K.;
RT "Draft Genome Sequence of an Ammonia-Oxidizing Archaeon, "Candidatus
RT Nitrosopumilus koreensis" AR1, from Marine Sediment.";
RL J. Bacteriol. 194:6940-6941(2012).
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; CP003842; AFS81610.1; -; Genomic_DNA.
DR RefSeq; WP_014963988.1; NC_018655.1.
DR AlphaFoldDB; K0B9G3; -.
DR STRING; 1229908.NKOR_08795; -.
DR GeneID; 13724596; -.
DR KEGG; nkr:NKOR_08795; -.
DR PATRIC; fig|1229908.8.peg.1900; -.
DR HOGENOM; CLU_020273_3_2_2; -.
DR UniPathway; UPA00275; UER00399.
DR Proteomes; UP000006101; Chromosome.
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 Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW ECO:0000256|RuleBase:RU003843}.
SQ SEQUENCE 221 AA; 24425 MW; DBAD8548FD28BA51 CRC64;
MSLESALQSL KRGEFVLLFD SAGRENEIDM VVAAEFVTPE HVARMRQHAG GLLCIAIDNN
FANSLELKYM HEILSDSSIP NKEMIMGLAP YGDHPTFSLS VNHYQTYTGI TDNDRSLTIR
EMANIYNVEN KQKKFASSFK TPGHVPLLIA SKGLLAARQG HTEMSVYLAQ IAGLTPVTAI
CEMMDAETYT ALSVDKAEKF GKQNGIPLID GKELLEYAKV H
//
