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

4-hydroxythreonine-4-phosphate dehydrogenase (EC 1.1.1.262) (4-(phosphohydroxy)-L-threonine dehydrogenase)

 J1IUB5_9RHIZ            Unreviewed;       337 AA.
J1IUB5;
03-OCT-2012, integrated into UniProtKB/TrEMBL.
03-OCT-2012, sequence version 1.
28-MAR-2018, entry version 37.
RecName: Full=4-hydroxythreonine-4-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00956571};
EC=1.1.1.262 {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00956565};
AltName: Full=4-(phosphohydroxy)-L-threonine dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00536};
Name=pdxA {ECO:0000256|HAMAP-Rule:MF_00536};
ORFNames=MEC_00663 {ECO:0000313|EMBL:EJF75187.1};
Bartonella alsatica IBS 382.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Bartonellaceae; Bartonella.
NCBI_TaxID=1094551 {ECO:0000313|EMBL:EJF75187.1, ECO:0000313|Proteomes:UP000008761};
[1] {ECO:0000313|EMBL:EJF75187.1, ECO:0000313|Proteomes:UP000008761}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IBS 382 {ECO:0000313|EMBL:EJF75187.1,
ECO:0000313|Proteomes:UP000008761};
The Broad Institute Genome Sequencing Platform;
The Broad Institute Genome Sequencing Center for Infectious Disease;
Feldgarden M., Kirby J., Kosoy M., Birtles R., Probert W.S.,
Chiaraviglio L., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.,
Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M.,
Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S.,
Wortman J., Nusbaum C., Birren B.;
"The Genome Sequence of Bartonella alsatica IBS 382.";
Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-
(phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-
(phosphohydroxy)butyric acid which spontaneously decarboxylates to
form 3-amino-2-oxopropyl phosphate (AHAP). {ECO:0000256|HAMAP-
Rule:MF_00536, ECO:0000256|SAAS:SAAS00956588}.
-!- CATALYTIC ACTIVITY: 4-phosphonooxy-L-threonine + NAD(+) = 3-amino-
2-oxopropyl phosphate + CO(2) + NADH. {ECO:0000256|HAMAP-
Rule:MF_00536, ECO:0000256|SAAS:SAAS00956547}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_00536};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00536};
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000256|HAMAP-Rule:MF_00536};
Note=Binds 1 divalent metal cation per subunit. Can use ions such
as Zn(2+), Mg(2+) or Co(2+). {ECO:0000256|HAMAP-Rule:MF_00536};
-!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
phosphate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00536,
ECO:0000256|SAAS:SAAS00956575}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00536,
ECO:0000256|SAAS:SAAS00956582}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536,
ECO:0000256|SAAS:SAAS00956573}.
-!- MISCELLANEOUS: The active site is located at the dimer interface.
{ECO:0000256|HAMAP-Rule:MF_00536}.
-!- SIMILARITY: Belongs to the PdxA family. {ECO:0000256|HAMAP-
Rule:MF_00536, ECO:0000256|SAAS:SAAS00701249}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EJF75187.1}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AIME01000004; EJF75187.1; -; Genomic_DNA.
RefSeq; WP_005865649.1; NZ_JH725020.1.
EnsemblBacteria; EJF75187; EJF75187; MEC_00663.
PATRIC; fig|1094551.3.peg.740; -.
OrthoDB; POG091H03XD; -.
UniPathway; UPA00244; UER00312.
Proteomes; UP000008761; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0050570; F:4-hydroxythreonine-4-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule.
GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
HAMAP; MF_00536; PdxA; 1.
InterPro; IPR037510; PdxA.
InterPro; IPR005255; PdxA_fam.
PANTHER; PTHR30004; PTHR30004; 1.
Pfam; PF04166; PdxA; 1.
TIGRFAMs; TIGR00557; pdxA; 1.
3: Inferred from homology;
Cobalt {ECO:0000256|HAMAP-Rule:MF_00536};
Complete proteome {ECO:0000313|Proteomes:UP000008761};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00536,
ECO:0000256|SAAS:SAAS00956585};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00536};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00536,
ECO:0000256|SAAS:SAAS00701256};
NAD {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00701266};
NADP {ECO:0000256|HAMAP-Rule:MF_00536, ECO:0000256|SAAS:SAAS00956572};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00536,
ECO:0000256|SAAS:SAAS00701261};
Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00536,
ECO:0000256|SAAS:SAAS00956552};
Zinc {ECO:0000256|HAMAP-Rule:MF_00536}.
METAL 170 170 Divalent metal cation; shared with
dimeric partner. {ECO:0000256|HAMAP-
Rule:MF_00536}.
METAL 215 215 Divalent metal cation; shared with
dimeric partner. {ECO:0000256|HAMAP-
Rule:MF_00536}.
METAL 270 270 Divalent metal cation; shared with
dimeric partner. {ECO:0000256|HAMAP-
Rule:MF_00536}.
BINDING 135 135 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00536}.
BINDING 136 136 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00536}.
BINDING 278 278 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00536}.
BINDING 287 287 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00536}.
BINDING 296 296 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00536}.
SEQUENCE 337 AA; 36867 MW; 85B731CB4BF41F6E CRC64;
MAVLVVSGGD PAGIGPEIAI KAWSLRVTHQ VPPFVLLADP DIICSCARFL QIDVEVESVF
INNPIKNFQT ALPIIPLENR QSDQRGLPSP QNTAGIIEAI KRSVQLIQSG HASALVTCPI
AKKNLYDAGF KFPGHTEFLA DLAHQTSNKC YHPVMMLSGP RLKTVPITVH VPFKEVPLQL
TRHLIIQTAL ITEHDLRKRF KITSPRLAVA GLNPHAGEKG AMGKEDIEII TPAIEYLKKK
GLNIVGPLPA DTMFHERTRK IYDVALCMYH DQALIPVKTL DFNSTVNVTL GLPFIRTSPD
HGTAFDIADK GIASPKSFIA ALKLANYLAE NSLISCQ


Related products :

Catalog number Product name Quantity
201-20-2466 H6PD{hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase)}rabbit.pAb 0.2ml
HAB1 H6PD Gene hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase)
GS-0939a hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase) primary antibody, Host: Rabbit 200ul
EIAAB11131 2DD,DHDH,Dimeric dihydrodiol dehydrogenase,D-xylose 1-dehydrogenase,D-xylose-NADP dehydrogenase,Ory2DD,Oryctolagus cuniculus,Rabbit,Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
EIAAB11132 2DD,DHDH,Dimeric dihydrodiol dehydrogenase,D-xylose 1-dehydrogenase,D-xylose-NADP dehydrogenase,Homo sapiens,Hum2DD,Human,Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
EIAAB11135 Bos taurus,Bovine,DHDH,Dimeric dihydrodiol dehydrogenase,D-xylose 1-dehydrogenase,D-xylose-NADP dehydrogenase,Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
EIAAB11134 Dhdh,Dimeric dihydrodiol dehydrogenase,D-xylose 1-dehydrogenase,D-xylose-NADP dehydrogenase,Mouse,Mus musculus,Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
EIAAB11133 2DD,DHDH,Dimeric dihydrodiol dehydrogenase,D-xylose 1-dehydrogenase,D-xylose-NADP dehydrogenase,Pig,Sus scrofa,Sus2DD,Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
CSB-EL010111MO Mouse hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase) (H6PD) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL010111HU Human hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase) (H6PD) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL010111RB Rabbit hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase) (H6PD) ELISA kit, Species Rabbit, Sample Type serum, plasma 96T
U2012p CLIA DHPDHase,Dihydropyrimidine dehydrogenase [NADP+],Dihydrothymine dehydrogenase,Dihydrouracil dehydrogenase,DPD,DPYD,Pig,Sus scrofa 96T
E2012p ELISA DHPDHase,Dihydropyrimidine dehydrogenase [NADP+],Dihydrothymine dehydrogenase,Dihydrouracil dehydrogenase,DPD,DPYD,Pig,Sus scrofa 96T
U2012p CLIA kit DHPDHase,Dihydropyrimidine dehydrogenase [NADP+],Dihydrothymine dehydrogenase,Dihydrouracil dehydrogenase,DPD,DPYD,Pig,Sus scrofa 96T
E2012p ELISA kit DHPDHase,Dihydropyrimidine dehydrogenase [NADP+],Dihydrothymine dehydrogenase,Dihydrouracil dehydrogenase,DPD,DPYD,Pig,Sus scrofa 96T
U2012b CLIA Bos taurus,Bovine,DHPDHase,Dihydropyrimidine dehydrogenase [NADP+],Dihydrothymine dehydrogenase,Dihydrouracil dehydrogenase,DPD,DPYD 96T
U2012r CLIA kit DHPDHase,Dihydropyrimidine dehydrogenase [NADP+],Dihydrothymine dehydrogenase,Dihydrouracil dehydrogenase,DPD,DPD,Dpyd,Rat,Rattus norvegicus 96T
E2012b ELISA kit Bos taurus,Bovine,DHPDHase,Dihydropyrimidine dehydrogenase [NADP+],Dihydrothymine dehydrogenase,Dihydrouracil dehydrogenase,DPD,DPYD 96T
U2012m CLIA DHPDHase,Dihydropyrimidine dehydrogenase [NADP+],Dihydrothymine dehydrogenase,Dihydrouracil dehydrogenase,DPD,Dpyd,Mouse,Mus musculus 96T
U2012m CLIA kit DHPDHase,Dihydropyrimidine dehydrogenase [NADP+],Dihydrothymine dehydrogenase,Dihydrouracil dehydrogenase,DPD,Dpyd,Mouse,Mus musculus 96T
U2012b CLIA kit Bos taurus,Bovine,DHPDHase,Dihydropyrimidine dehydrogenase [NADP+],Dihydrothymine dehydrogenase,Dihydrouracil dehydrogenase,DPD,DPYD 96T
E2012m ELISA DHPDHase,Dihydropyrimidine dehydrogenase [NADP+],Dihydrothymine dehydrogenase,Dihydrouracil dehydrogenase,DPD,Dpyd,Mouse,Mus musculus 96T
U2012r CLIA DHPDHase,Dihydropyrimidine dehydrogenase [NADP+],Dihydrothymine dehydrogenase,Dihydrouracil dehydrogenase,DPD,DPD,Dpyd,Rat,Rattus norvegicus 96T
E2012b ELISA Bos taurus,Bovine,DHPDHase,Dihydropyrimidine dehydrogenase [NADP+],Dihydrothymine dehydrogenase,Dihydrouracil dehydrogenase,DPD,DPYD 96T
E2012r ELISA DHPDHase,Dihydropyrimidine dehydrogenase [NADP+],Dihydrothymine dehydrogenase,Dihydrouracil dehydrogenase,DPD,DPD,Dpyd,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