ID V4YAQ7_9ARCH Unreviewed; 251 AA.
AC V4YAQ7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=A07HR60_01027 {ECO:0000313|EMBL:ESS12088.1};
OS uncultured archaeon A07HR60.
OC Archaea; environmental samples.
OX NCBI_TaxID=1412874 {ECO:0000313|EMBL:ESS12088.1, ECO:0000313|Proteomes:UP000030679};
RN [1] {ECO:0000313|Proteomes:UP000030679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24335829;
RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S.,
RA Heidelberg K.B., Banfield J.F., Allen E.E.;
RT "Seasonal fluctuations in ionic concentrations drive microbial succession
RT in a hypersaline lake community.";
RL ISME J. 0:0-0(2013).
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; KI543229; ESS12088.1; -; Genomic_DNA.
DR AlphaFoldDB; V4YAQ7; -.
DR STRING; 1412874.A07HR60_01027; -.
DR PATRIC; fig|1412874.3.peg.1170; -.
DR UniPathway; UPA00275; UER00399.
DR Proteomes; UP000030679; Unassembled WGS sequence.
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, ECO:0000313|EMBL:ESS12088.1};
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:UP000030679};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW ECO:0000256|RuleBase:RU003843}.
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 251 AA; 26921 MW; D933709064C182B9 CRC64;
MRTNANSPRK TPGREANQTK PARSDAVPIE DTAVEDALEA FRDGDPVLVH DFADREGETD
IVYPAAAVGP EAIARLRNDA GGLICVAVPD RIADVFELPF LATELDHPAT DDHPAYDDRS
AFSLPVNHRD TYTGITDRDR SRTVIELAEA AQSADDDPEY NIDEFAAEFR SPGHVHILRG
APGLLADRAG HTELGLAIAQ AAGLRPAVVV CEMLDDATGE ALSPSDAQGY ADRHGFAYLE
GEILVDALSP Q
//
