ID V9R7V3_9RICK Unreviewed; 212 AA.
AC V9R7V3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|ARBA:ARBA00018836, ECO:0000256|RuleBase:RU003843};
DE Short=DHBP synthase {ECO:0000256|RuleBase:RU003843};
DE EC=4.1.99.12 {ECO:0000256|ARBA:ARBA00012153, ECO:0000256|RuleBase:RU003843};
GN ORFNames=EMUR_00345 {ECO:0000313|EMBL:AHC38924.1};
OS Ehrlichia muris AS145.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=1423892 {ECO:0000313|EMBL:AHC38924.1, ECO:0000313|Proteomes:UP000018689};
RN [1] {ECO:0000313|EMBL:AHC38924.1, ECO:0000313|Proteomes:UP000018689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS154 {ECO:0000313|Proteomes:UP000018689};
RX PubMed=24482514;
RA Thirumalapura N.R., Qin X., Kuriakose J.A., Walker D.H.;
RT "Complete Genome Sequence of Ehrlichia muris Strain AS145T, a Model
RT Monocytotropic Ehrlichia Strain.";
RL Genome Announc. 2:e01234-13(2014).
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, 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|ARBA:ARBA00004904, 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; CP006917; AHC38924.1; -; Genomic_DNA.
DR RefSeq; WP_024071713.1; NC_023063.1.
DR AlphaFoldDB; V9R7V3; -.
DR STRING; 1423892.EMUR_00345; -.
DR KEGG; emr:EMUR_00345; -.
DR PATRIC; fig|1423892.3.peg.68; -.
DR HOGENOM; CLU_020273_3_0_5; -.
DR OrthoDB; 9793111at2; -.
DR UniPathway; UPA00275; UER00399.
DR Proteomes; UP000018689; 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: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 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 212 AA; 23288 MW; 5B5792045B2DBB45 CRC64;
MGIIVSESSS FISPIEHIIE DAKQGKVFIL IDDEQRENEG DLVVLAEKIT SDVINFMITH
GSGIVCLSIT EDFMYKLGLE FMPKRHVNDN SASFATSIDA RYGITTGVSA HDRAHTILTA
VNENVTKDDF VTPGHIFPIV SKKGGVLERS GHTEASVEIA RIAGSAPIAV VCELMNPDGT
MSRMPDIIEF SQRHNIKVTS IDKLIQYVKA NW
//
