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

UDP-glucose 4-epimerase (EC 5.1.3.2) (Galactowaldenase) (UDP-N-acetylgalactosamine 4-epimerase) (UDP-GalNAc 4-epimerase) (UDP-N-acetylglucosamine 4-epimerase) (UDP-GlcNAc 4-epimerase) (EC 5.1.3.7) (UDP-galactose 4-epimerase)

 GALE_CAEEL              Reviewed;         349 AA.
Q564Q1; O62107;
30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 1.
25-OCT-2017, entry version 108.
RecName: Full=UDP-glucose 4-epimerase {ECO:0000250|UniProtKB:Q14376};
EC=5.1.3.2 {ECO:0000305|PubMed:25298520};
AltName: Full=Galactowaldenase {ECO:0000305};
AltName: Full=UDP-N-acetylgalactosamine 4-epimerase {ECO:0000250|UniProtKB:Q14376};
Short=UDP-GalNAc 4-epimerase {ECO:0000250|UniProtKB:Q14376};
AltName: Full=UDP-N-acetylglucosamine 4-epimerase {ECO:0000250|UniProtKB:Q14376};
Short=UDP-GlcNAc 4-epimerase {ECO:0000250|UniProtKB:Q14376};
EC=5.1.3.7 {ECO:0000305|PubMed:25298520};
AltName: Full=UDP-galactose 4-epimerase {ECO:0000303|PubMed:25298520};
Name=gale-1 {ECO:0000312|WormBase:C47B2.6b};
ORFNames=C47B2.6 {ECO:0000312|WormBase:C47B2.6b};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND MUTAGENESIS OF PRO-314.
PubMed=25298520; DOI=10.1534/genetics.114.170084;
Brokate-Llanos A.M., Monje J.M., Murdoch P., Munoz M.J.;
"Developmental defects in a Caenorhabditis elegans model for type III
galactosemia.";
Genetics 198:1559-1569(2014).
-!- FUNCTION: Catalyzes two distinct but analogous reactions: the
reversible epimerization of UDP-glucose to UDP-galactose and the
reversible epimerization of UDP-N-acetylglucosamine to UDP-N-
acetylgalactosamine. The reaction with UDP-Gal plays a critical
role in the Leloir pathway of galactose catabolism in which
galactose is converted to the glycolytic intermediate glucose 6-
phosphate. It contributes to the catabolism of dietary galactose
and enables the endogenous biosynthesis of both UDP-Gal and UDP-
GalNAc when exogenous sources are limited. Both UDP-sugar
interconversions are important for the synthesis of glycoproteins
and glycolipids. {ECO:0000269|PubMed:25298520}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose = UDP-alpha-D-galactose.
{ECO:0000305|PubMed:25298520}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine = UDP-N-
acetyl-alpha-D-galactosamine. {ECO:0000305|PubMed:25298520}.
-!- COFACTOR:
Name=NAD(+); Xref=ChEBI:CHEBI:57540;
Evidence={ECO:0000255|RuleBase:RU003508};
-!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
{ECO:0000269|PubMed:25298520}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=b {ECO:0000312|WormBase:C47B2.6b};
IsoId=Q564Q1-1; Sequence=Displayed;
Note=No experimental confirmation available. {ECO:0000305};
Name=a {ECO:0000312|WormBase:C47B2.6a};
IsoId=Q564Q1-2; Sequence=VSP_059051;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in gonads, vulva, intestine,
hypdermis and nervous system. {ECO:0000269|PubMed:25298520}.
-!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and adults.
{ECO:0000269|PubMed:25298520}.
-!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
family. {ECO:0000255|RuleBase:RU003508}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; BX284601; CAB16861.1; -; Genomic_DNA.
EMBL; BX284601; CAI79146.1; -; Genomic_DNA.
PIR; T19989; T19989.
RefSeq; NP_001021051.1; NM_001025880.2. [Q564Q1-2]
RefSeq; NP_001021052.1; NM_001025881.3. [Q564Q1-1]
UniGene; Cel.6687; -.
ProteinModelPortal; Q564Q1; -.
SMR; Q564Q1; -.
DIP; DIP-26300N; -.
IntAct; Q564Q1; 1.
MINT; MINT-1079276; -.
STRING; 6239.C47B2.6b; -.
World-2DPAGE; 0020:O62107; -.
EPD; Q564Q1; -.
PaxDb; Q564Q1; -.
PeptideAtlas; Q564Q1; -.
EnsemblMetazoa; C47B2.6a; C47B2.6a; WBGene00008132. [Q564Q1-2]
EnsemblMetazoa; C47B2.6b; C47B2.6b; WBGene00008132. [Q564Q1-1]
GeneID; 173171; -.
KEGG; cel:CELE_C47B2.6; -.
UCSC; C47B2.6b; c. elegans. [Q564Q1-1]
CTD; 173171; -.
WormBase; C47B2.6a; CE17566; WBGene00008132; gale-1.
WormBase; C47B2.6b; CE38295; WBGene00008132; gale-1.
eggNOG; KOG1371; Eukaryota.
eggNOG; COG1087; LUCA.
GeneTree; ENSGT00530000063128; -.
HOGENOM; HOG000168001; -.
InParanoid; Q564Q1; -.
KO; K01784; -.
OMA; SCTVYGQ; -.
OrthoDB; EOG091G0ACI; -.
PhylomeDB; Q564Q1; -.
Reactome; R-CEL-70370; Galactose catabolism.
UniPathway; UPA00214; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00008132; -.
ExpressionAtlas; Q564Q1; baseline and differential.
GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IMP:UniProtKB.
GO; GO:0003974; F:UDP-N-acetylglucosamine 4-epimerase activity; IMP:UniProtKB.
GO; GO:0042335; P:cuticle development; IMP:WormBase.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
GO; GO:0006012; P:galactose metabolic process; IMP:UniProtKB.
GO; GO:0035262; P:gonad morphogenesis; IMP:UniProtKB.
GO; GO:1900102; P:negative regulation of endoplasmic reticulum unfolded protein response; IMP:UniProtKB.
GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
GO; GO:0040026; P:positive regulation of vulval development; IMP:UniProtKB.
GO; GO:1903354; P:regulation of distal tip cell migration; IMP:UniProtKB.
CDD; cd05247; UDP_G4E_1_SDR_e; 1.
InterPro; IPR016040; NAD(P)-bd_dom.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR005886; UDP_G4E.
Pfam; PF16363; GDP_Man_Dehyd; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01179; galE; 1.
1: Evidence at protein level;
Alternative splicing; Carbohydrate metabolism; Complete proteome;
Galactose metabolism; Isomerase; NAD; Reference proteome.
CHAIN 1 349 UDP-glucose 4-epimerase.
/FTId=PRO_0000441236.
NP_BIND 10 12 NAD. {ECO:0000250|UniProtKB:Q14376}.
NP_BIND 31 35 NAD. {ECO:0000250|UniProtKB:Q14376}.
NP_BIND 66 67 NAD. {ECO:0000250|UniProtKB:Q14376}.
REGION 132 134 Substrate binding.
{ECO:0000250|UniProtKB:Q14376}.
REGION 186 188 Substrate binding.
{ECO:0000250|UniProtKB:Q14376}.
REGION 207 209 Substrate binding.
{ECO:0000250|UniProtKB:Q14376}.
REGION 225 227 Substrate binding.
{ECO:0000250|UniProtKB:Q14376}.
REGION 303 306 Substrate binding.
{ECO:0000250|UniProtKB:Q14376}.
ACT_SITE 158 158 Proton acceptor.
{ECO:0000250|UniProtKB:Q14376}.
BINDING 92 92 NAD. {ECO:0000250|UniProtKB:Q14376}.
BINDING 162 162 NAD. {ECO:0000250|UniProtKB:Q14376}.
BINDING 186 186 NAD. {ECO:0000250|UniProtKB:Q14376}.
BINDING 240 240 Substrate.
{ECO:0000250|UniProtKB:Q14376}.
VAR_SEQ 39 40 Missing (in isoform a). {ECO:0000305}.
/FTId=VSP_059051.
MUTAGEN 314 314 P->L: In pv18; at the restrictive
temperature of 25 degrees Celsius,
embryos have cell-cell adhesion defects
and die before hatching. The few
surviving animals are arrested at the L1
larval stage. At the permissive
temperature of 16-20 degrees Celsius,
causes a developmental delay. Distal tip
cell migration is impaired due to a
reduced localization of metalloprotease
mig-17 to the gonad basement membrane.
Vulva lumen is smaller at the L4 larval
stage. Accumulation of UDP-galactose
(Gal) and reduction in UDP-N-
acetylgalactosamine (GalNAc) levels.
Hypersensitivity to a galactose-rich diet
characterized by a slow development often
resulting in an arrest at the L1 larval
stage. Up-regulation of ER stress
response protein hsp-4; expression is
suppressed in an xbp-1 RNAi-mediated
knockdown animals. Reduced survival upon
E.faecalis or S.aureus-mediated
infection. {ECO:0000269|PubMed:25298520}.
SEQUENCE 349 AA; 37883 MW; 0B0FC906186E2105 CRC64;
MHILVTGAAG FIGSHTVLEL LNSGYTVLCI DNFANAISVT DEHGNAISLK RVAQLTGKDV
PFQNVDVCDE AALEKVFSEN KFDGIIHLAA LKAVGESVAK PLQYYSNNLV ASLNLIQMCL
KYNVKNFVFS SSATVYGPPS ELPITEKSQT GQGITNPYGQ TKYMMEQILI DVGKANPEWN
VVLLRYFNPV GAHKSGLIGE DPKGVPNNLM PYVSQVAIGK LPVLTIYGDQ FDTVDGTGVR
DYIHVVDLAK GHVKAFDRIK TVGNIGTEIY NLGTGVGYSV RQMVDALKKV SGRDIPVKIG
VPRPGDVASV YCDPSLAQEK LGWRAETGLE EMCADLWNWQ TKNPQGFSA


Related products :

Catalog number Product name Quantity
EIAAB34262 AGE,GlcNAc 2-epimerase,N-acetyl-D-glucosamine 2-epimerase,N-acylglucosamine 2-epimerase,Pig,RENBP,Renin-binding protein,RnBP,Sus scrofa
EIAAB34259 AGE,GlcNAc 2-epimerase,N-acetyl-D-glucosamine 2-epimerase,N-acylglucosamine 2-epimerase,Rat,Rattus norvegicus,Renbp,Renin-binding protein,RnBP
EIAAB34260 AGE,GlcNAc 2-epimerase,Mouse,Mus musculus,N-acetyl-D-glucosamine 2-epimerase,N-acylglucosamine 2-epimerase,Renbp,Renin-binding protein,RnBP
EIAAB34257 AGE,Bos taurus,Bovine,GlcNAc 2-epimerase,N-acetyl-D-glucosamine 2-epimerase,N-acylglucosamine 2-epimerase,RENBP,Renin-binding protein,RnBP
EIAAB34261 AGE,GlcNAc 2-epimerase,Homo sapiens,Human,N-acetyl-D-glucosamine 2-epimerase,N-acylglucosamine 2-epimerase,RENBP,Renin-binding protein,RnBP
EIAAB11961 Bos taurus,Bovine,Chondroitin-glucuronate 5-epimerase,Dermatan-sulfate epimerase,DS epimerase,DSE
EIAAB11962 Chondroitin-glucuronate 5-epimerase,Dermatan-sulfate epimerase,DS epimerase,Dse,Mouse,Mus musculus,Sart2,SART-2,Squamous cell carcinoma antigen recognized by T-cells 2
EIAAB34258 AGE,Canis familiaris,Canis lupus familiaris,Dog,GlcNAc 2-epimerase,N-acetyl-D-glucosamine 2-epimerase,N-acylglucosamine 2-epimerase,RENBP,Renin-binding protein,RnBP
EIAAB11963 Chondroitin-glucuronate 5-epimerase,Dermatan-sulfate epimerase,DS epimerase,DSE,Homo sapiens,Human,SART2,SART-2,Squamous cell carcinoma antigen recognized by T-cells 2
29-593 HSD17B6 has both oxidoreductase and epimerase activities and is involved in androgen catabolism. The oxidoreductase activity can convert 3 alpha-adiol to dihydrotestosterone, while the epimerase activ 0.1 mg
EIAAB35839 Homo sapiens,Human,HUSSY-17,Ribulose-5-phosphate-3-epimerase,Ribulose-phosphate 3-epimerase,RPE
26-862 GALE is an UDP-galactose-4-epimerase which catalyzes two distinct but analogous reactions the epimerization of UDP-glucose to UDP-galactose, and the epimerization of UDP-N-acetylglucosamine to UDP-N- 0.05 mg
EIAAB35838 Mouse,Mus musculus,Ribulose-5-phosphate-epimerase,Ribulose-phosphate 3-epimerase,Rpe
REN-537 Recombinant Human UDP-Galactose-4-Epimerase 5
enz-537 Recombinant Human UDP-Galactose-4-Epimerase 5
enz-537 Recombinant Human UDP-Galactose-4-Epimerase 1mg
enz-537 Recombinant Human UDP-Galactose-4-Epimerase 25
OETENZ-537 UDP-Galactose-4-Epimerase Human Recombinant 5
7-02791 Recombinant Human UDP-Galactose-4-Epimerase 5
enz-537 Recombinant Human UDP-Galactose-4-Epimerase ENZYMES 25
OETENZ-537 UDP-Galactose-4-Epimerase Human Recombinant 25
enz-537 Recombinant Human UDP-Galactose-4-Epimerase ENZYMES 1mg
GALK2 GALE Gene UDP-galactose-4-epimerase
enz-537 Recombinant Human UDP-Galactose-4-Epimerase ENZYMES 5
enz-537 Recombinant Human UDP-Galactose-4-Epimerase GALE 25


 

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