Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 A0A0B7DCT3_PSEFL        Unreviewed;       369 AA.
A0A0B7DCT3;
01-APR-2015, integrated into UniProtKB/TrEMBL.
01-APR-2015, sequence version 1.
25-APR-2018, entry version 25.
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_1 {ECO:0000313|EMBL:CEL29708.1};
Synonyms=ribB {ECO:0000256|HAMAP-Rule:MF_00180};
ORFNames=SRM1_03062 {ECO:0000313|EMBL:CEL29708.1};
Pseudomonas fluorescens.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=294 {ECO:0000313|EMBL:CEL29708.1, ECO:0000313|Proteomes:UP000043897};
[1] {ECO:0000313|EMBL:CEL29708.1, ECO:0000313|Proteomes:UP000043897}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SRM1 {ECO:0000313|EMBL:CEL29708.1};
Lo R., Stanton-Cook M.J., Beatson S.A., Turner M.S., Bansal N.;
"Draft genome sequence of Pseudomonas fluorescens SRM1, an isolate
from spoiled raw milk.";
Genome Announc. 3:e00138-e00138(2015).
-!- 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}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; CDMF01000001; CEL29708.1; -; Genomic_DNA.
RefSeq; WP_042559515.1; NZ_CDMF01000001.1.
EnsemblBacteria; CEL29708; CEL29708; SRM1_03062.
eggNOG; ENOG4105C66; Bacteria.
eggNOG; COG0108; LUCA.
eggNOG; COG0807; LUCA.
UniPathway; UPA00275; UER00399.
Proteomes; UP000043897; 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:UP000043897};
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};
Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00180,
ECO:0000256|SAAS:SAAS00037880}.
DOMAIN 210 366 GTP_cyclohydro2.
{ECO:0000259|Pfam:PF00925}.
REGION 27 28 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00180}.
REGION 140 144 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00180}.
METAL 28 28 Magnesium or manganese 1.
{ECO:0000256|HAMAP-Rule:MF_00180}.
METAL 28 28 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_00180}.
METAL 143 143 Magnesium or manganese 2.
{ECO:0000256|HAMAP-Rule:MF_00180}.
BINDING 32 32 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00180}.
BINDING 164 164 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00180}.
SITE 126 126 Essential for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_00180}.
SITE 164 164 Essential for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_00180}.
SEQUENCE 369 AA; 40114 MW; F9CA4C25372C9E15 CRC64;
MAFNSIEEII ADYRLGKMVL LVDDEDRENE GDLLLAADCC TPEAISFMAR EARGLICLTL
TDEHCQRLGL EQMVPSNGSV FSTAFTVSIE AAVGVTTGIS AADRACTVAA AVAKDARAED
LVQPGHIFPL RAKEGGVLTR AGHTEAGCDL ARLAGFTPAS VIVEVMNDDG TMARRPDLEV
FARQHGIKIG TIADLIHHRL STEHTIERIG ERDLPTVHGT FRLITFEDRI EGGVHMAMVM
GDLRREEPTL VRVHVIDPLR DLVGADYSGP SNWTLWAALQ RVAAEGHGVV VVLANHESSQ
ALLERVPQLT QPPRQFSRSQ SRIYSEVGTG AQILQNLGVG KLRHLGPPLK YVGLTGYDLE
VVESIPFTE


Related products :

Catalog number Product name Quantity
EIAAB11775 Dolichol-phosphate mannose synthase,Dolichol-phosphate mannosyltransferase,Dolichyl-phosphate beta-D-mannosyltransferase,DPM synthase,DPM1,Homo sapiens,Human,Mannose-P-dolichol synthase,MPD synthase
EIAAB38426 Homo sapiens,Human,N-acetylneuraminate synthase,N-acetylneuraminate-9-phosphate synthase,N-acetylneuraminic acid phosphate synthase,N-acetylneuraminic acid synthase,NANS,SAS,Sialic acid synthase
EIAAB11774 Dolichol-phosphate mannose synthase,Dolichol-phosphate mannosyltransferase,Dolichyl-phosphate beta-D-mannosyltransferase,DPM synthase,Dpm1,Mannose-P-dolichol synthase,Mouse,MPD synthase,Mus musculus
EIAAB11776 Bos taurus,Bovine,Dolichol-phosphate mannose synthase,Dolichol-phosphate mannosyltransferase,Dolichyl-phosphate beta-D-mannosyltransferase,DPM synthase,DPM1,Mannose-P-dolichol synthase,MPD synthase
EIAAB11773 Dolichol-phosphate mannose synthase,Dolichol-phosphate mannosyltransferase,Dolichyl-phosphate beta-D-mannosyltransferase,DPM synthase,DPM1,Mannose-P-dolichol synthase,MPD synthase,Pig,Sus scrofa
EIAAB30749 Bos taurus,Bovine,CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial,PGP synthase 1,PGS1,Phosphatidylglycerophosphate synthase 1
EIAAB30750 CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial,Homo sapiens,Human,PGP synthase 1,PGS1,Phosphatidylglycerophosphate synthase 1
EIAAB30751 CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial,Mouse,Mus musculus,PGP synthase 1,Pgs1,Phosphatidylglycerophosphate synthase 1,Saf,Silencer-associated factor
EIAAB11782 Dolichol-phosphate mannose synthase subunit 3,Dolichol-phosphate mannosyltransferase subunit 3,Dolichyl-phosphate beta-D-mannosyltransferase subunit 3,DPM synthase complex subunit 3,DPM3,Homo sapiens,
EIAAB06601 CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,CDS2,CTP phosphatidate cytidylyltransferase 2,Homo sapiens,Human
EIAAB06603 CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,Cds2,CTP phosphatidate cytidylyltransferase 2,Mouse,Mus musculus
EIAAB06600 Bos taurus,Bovine,CDP-DAG synthase 2,CDP-DG synthase 2,CDP-diacylglycerol synthase 2,CDP-diglyceride pyrophosphorylase 2,CDP-diglyceride synthase 2,CDS 2,CDS2,CTP phosphatidate cytidylyltransferase 2,
EIAAB06599 CDP-DAG synthase 1,CDP-DG synthase 1,CDP-diacylglycerol synthase 1,CDP-diglyceride pyrophosphorylase 1,CDP-diglyceride synthase 1,Cds,CDS 1,Cds1,CTP phosphatidate cytidylyltransferase 1,Mouse,Mus musc
EIAAB06597 CDP-DAG synthase 1,CDP-DG synthase 1,CDP-diacylglycerol synthase 1,CDP-diglyceride pyrophosphorylase 1,CDP-diglyceride synthase 1,CDS,CDS 1,CDS1,CTP phosphatidate cytidylyltransferase 1,Homo sapiens,H
E0167h ELISA kit Beta-trace protein,Cerebrin-28,Glutathione-independent PGD synthase,Homo sapiens,Human,Lipocalin-type prostaglandin-D synthase,PDS,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostag 96T
E0167h ELISA Beta-trace protein,Cerebrin-28,Glutathione-independent PGD synthase,Homo sapiens,Human,Lipocalin-type prostaglandin-D synthase,PDS,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandi 96T
EIAAB11783 Bos taurus,Bovine,Dolichol-phosphate mannose synthase subunit 3,Dolichol-phosphate mannosyltransferase subunit 3,Dolichyl-phosphate beta-D-mannosyltransferase subunit 3,DPM synthase complex subunit 3,
EIAAB28570 (2-5')oligo(A) synthase 1B,2-5A synthase 1B,2'-5'-oligoadenylate synthase 1B,2'-5'-oligoadenylate synthase-like protein 1,Mouse,Mus musculus,Oas1b,Oias2
E0167m ELISA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,L-PGDS,Mouse,Mus musculus,PGD2 synthase,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds 96T
E0167b ELISA kit Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
E0167b ELISA Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
E0167r ELISA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds,Rat,Rattus norvegicus 96T
U0167b CLIA Bos taurus,Bovine,Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS 96T
U0167m CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,L-PGDS,Mouse,Mus musculus,PGD2 synthase,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds 96T
E0167r ELISA kit Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,Ptgds,Rat,Rattus norvegicus 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur