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3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (EC 4.1.99.12)

 A0A165YHB0_9RHOB        Unreviewed;       451 AA.
A0A165YHB0;
06-JUL-2016, integrated into UniProtKB/TrEMBL.
06-JUL-2016, sequence version 1.
25-APR-2018, entry version 14.
RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00180};
Short=DHBP synthase {ECO:0000256|HAMAP-Rule:MF_00180};
EC=4.1.99.12 {ECO:0000256|HAMAP-Rule:MF_00180};
Name=ribBA {ECO:0000313|EMBL:KZL18843.1};
Synonyms=ribB {ECO:0000256|HAMAP-Rule:MF_00180};
ORFNames=PsAD2_02359 {ECO:0000313|EMBL:KZL18843.1};
Pseudovibrio axinellae.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae; Pseudovibrio.
NCBI_TaxID=989403 {ECO:0000313|EMBL:KZL18843.1, ECO:0000313|Proteomes:UP000076577};
[1] {ECO:0000313|EMBL:KZL18843.1, ECO:0000313|Proteomes:UP000076577}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Ad2 {ECO:0000313|EMBL:KZL18843.1,
ECO:0000313|Proteomes:UP000076577};
PubMed=27065959; DOI=10.3389/fmicb.2016.00387;
Romano S., Fernandez-Guerra A., Reen F.J., Glockner F.O.,
Crowley S.P., O'Sullivan O., Cotter P.D., Adams C., Dobson A.D.,
O'Gara F.;
"Comparative Genomic Analysis Reveals a Diverse Repertoire of Genes
Involved in Prokaryote-Eukaryote Interactions within the Pseudovibrio
Genus.";
Front. Microbiol. 7:387-387(2016).
-!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to
formate and 3,4-dihydroxy-2-butanone 4-phosphate.
{ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|SAAS:SAAS00661634}.
-!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4-
dihydroxybutan-2-one 4-phosphate. {ECO:0000256|HAMAP-
Rule:MF_00180, ECO:0000256|SAAS:SAAS00661651}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00180};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|HAMAP-Rule:MF_00180};
Note=Binds 2 divalent metal cations per subunit. Magnesium or
manganese. {ECO:0000256|HAMAP-Rule:MF_00180};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|SAAS:SAAS00661637};
-!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-
hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step
1/1. {ECO:0000256|HAMAP-Rule:MF_00180,
ECO:0000256|SAAS:SAAS00661665}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00180}.
-!- SIMILARITY: Belongs to the DHBP synthase family.
{ECO:0000256|HAMAP-Rule:MF_00180}.
-!- SIMILARITY: In the N-terminal section; belongs to the DHBP
synthase family. {ECO:0000256|SAAS:SAAS00534513}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KZL18843.1}.
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EMBL; LMCB01000017; KZL18843.1; -; Genomic_DNA.
EnsemblBacteria; KZL18843; KZL18843; PsAD2_02359.
PATRIC; fig|989403.3.peg.2515; -.
UniPathway; UPA00275; UER00399.
Proteomes; UP000076577; Unassembled WGS sequence.
GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
HAMAP; MF_00180; RibB; 1.
InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
InterPro; IPR000422; DHBP_synthase_RibB.
InterPro; IPR032677; GTP_cyclohydro_II.
InterPro; IPR036144; RibA-like_sf.
Pfam; PF00926; DHBP_synthase; 1.
Pfam; PF00925; GTP_cyclohydro2; 1.
SUPFAM; SSF142695; SSF142695; 1.
SUPFAM; SSF55821; SSF55821; 1.
TIGRFAMs; TIGR00506; ribB; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000076577};
Lyase {ECO:0000256|HAMAP-Rule:MF_00180,
ECO:0000256|SAAS:SAAS01036014};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00180,
ECO:0000256|SAAS:SAAS00661654};
Manganese {ECO:0000256|HAMAP-Rule:MF_00180};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00180,
ECO:0000256|SAAS:SAAS00037896};
Reference proteome {ECO:0000313|Proteomes:UP000076577};
Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00180,
ECO:0000256|SAAS:SAAS00037880}.
DOMAIN 292 445 GTP_cyclohydro2.
{ECO:0000259|Pfam:PF00925}.
REGION 109 110 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00180}.
REGION 222 226 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00180}.
METAL 110 110 Magnesium or manganese 1.
{ECO:0000256|HAMAP-Rule:MF_00180}.
METAL 110 110 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_00180}.
METAL 225 225 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_00180}.
BINDING 114 114 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00180}.
BINDING 246 246 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00180}.
SITE 208 208 Essential for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_00180}.
SITE 246 246 Essential for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_00180}.
SEQUENCE 451 AA; 49158 MW; 65875E72ACD0BDD4 CRC64;
MILKFYGKGD KAMRLTEWLE KTGESRSAFA RRACLSPASV TALCNDPSAW ISREMAQKIA
VATDHQVTPN DFLGLKENKE YVVSQSRVAE ALRAFEKGEM VVVTDDDDRE NEGDLIVAAS
LITPEQMGFI VRHTSGIVCA PMTPKEAKRL HLDPMVGSND APLATAFTVS VDYAPGLTTG
ISAEQRCATV RGLANPNASS GDFVRPGHVF PLVAKEGGVL MRSGHTEAAV DLCKLTGLPE
VGVISELVND DGTVKQGEQV EEFAREHNLK KVSVADLIAW RQRHENLVKR TDEFDVDTPA
GKARAIVYST PFDNIGHLAL VYGDIRDGQN IPVRLHLENV LDAVTGQVKP IEKTLEDFAK
RGRGIFVYLR EGAVGVASKP HRQRDNLEAA EDEQHVSAQG RSEDWREVGL GAQILKDLGA
NSIRVIASRA RHYVGLEGFG LKVEATESLA D


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