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

Bifunctional polymyxin resistance protein ArnA (Polymyxin resistance protein PmrI) [Includes: UDP-4-amino-4-deoxy-L-arabinose formyltransferase (EC 2.1.2.13) (ArnAFT) (UDP-L-Ara4N formyltransferase); UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating (EC 1.1.1.305) (ArnADH) (UDP-GlcUA decarboxylase) (UDP-glucuronic acid dehydrogenase)]

 ARNA_ECOLI              Reviewed;         660 AA.
P77398; Q56VX0;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
22-NOV-2017, entry version 162.
RecName: Full=Bifunctional polymyxin resistance protein ArnA;
AltName: Full=Polymyxin resistance protein PmrI;
Includes:
RecName: Full=UDP-4-amino-4-deoxy-L-arabinose formyltransferase;
EC=2.1.2.13;
AltName: Full=ArnAFT;
AltName: Full=UDP-L-Ara4N formyltransferase;
Includes:
RecName: Full=UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating;
EC=1.1.1.305;
AltName: Full=ArnADH;
AltName: Full=UDP-GlcUA decarboxylase;
AltName: Full=UDP-glucuronic acid dehydrogenase;
Name=arnA; Synonyms=pmrI, yfbG; OrderedLocusNames=b2255, JW2249;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION OF C-TERMINAL DOMAIN, AND
CHARACTERIZATION.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=11706007; DOI=10.1074/jbc.M109377200;
Breazeale S.D., Ribeiro A.A., Raetz C.R.H.;
"Oxidative decarboxylation of UDP-glucuronic acid in extracts of
polymyxin-resistant Escherichia coli. Origin of lipid A species
modified with 4-amino-4-deoxy-L-arabinose.";
J. Biol. Chem. 277:2886-2896(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9205837; DOI=10.1093/dnares/4.2.91;
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
Yamagata S., Horiuchi T.;
"Construction of a contiguous 874-kb sequence of the Escherichia coli-
K12 genome corresponding to 50.0-68.8 min on the linkage map and
analysis of its sequence features.";
DNA Res. 4:91-113(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
INDUCTION BY BASR.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15569938; DOI=10.1073/pnas.0406038101;
Winfield M.D., Groisman E.A.;
"Phenotypic differences between Salmonella and Escherichia coli
resulting from the disparate regulation of homologous genes.";
Proc. Natl. Acad. Sci. U.S.A. 101:17162-17167(2004).
[6]
FUNCTION OF N-TERMINAL DOMAIN, CATALYTIC ACTIVITY, AND
CHARACTERIZATION.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=15695810; DOI=10.1074/jbc.M414265200;
Breazeale S.D., Ribeiro A.A., McClerren A.L., Raetz C.R.H.;
"A formyltransferase required for polymyxin resistance in Escherichia
coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose:
identification and function of UDP-4-deoxy-4-formamido-L-arabinose.";
J. Biol. Chem. 280:14154-14167(2005).
[7]
PATHWAY.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=17928292; DOI=10.1074/jbc.M706172200;
Yan A., Guan Z., Raetz C.R.H.;
"An undecaprenyl phosphate-aminoarabinose flippase required for
polymyxin resistance in Escherichia coli.";
J. Biol. Chem. 282:36077-36089(2007).
[8]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 306-660, CATALYTIC ACTIVITY
OF C-TERMINAL DOMAIN, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15491143; DOI=10.1021/bi048551f;
Gatzeva-Topalova P.Z., May A.P., Sousa M.C.;
"Crystal structure of Escherichia coli ArnA (PmrI) decarboxylase
domain. A key enzyme for lipid A modification with 4-amino-4-deoxy-L-
arabinose and polymyxin resistance.";
Biochemistry 43:13370-13379(2004).
[9]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-300, MUTAGENESIS OF
ASN-102; HIS-104 AND ASP-140, AND REACTION MECHASNISM.
PubMed=15807526; DOI=10.1021/bi047384g;
Gatzeva-Topalova P.Z., May A.P., Sousa M.C.;
"Crystal structure and mechanism of the Escherichia coli ArnA (PmrI)
transformylase domain. An enzyme for lipid A modification with 4-
amino-4-deoxy-L-arabinose and polymyxin resistance.";
Biochemistry 44:5328-5338(2005).
[10]
X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH UMP AND
N-5-FTHF, AND MUTAGENESIS OF SER-433 AND GLU-434.
PubMed=15809294; DOI=10.1074/jbc.M501534200;
Williams G.J., Breazeale S.D., Raetz C.R.H., Naismith J.H.;
"Structure and function of both domains of ArnA, a dual function
decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-
arabinose biosynthesis.";
J. Biol. Chem. 280:23000-23008(2005).
[11]
X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) IN COMPLEX WITH UDP-GLCUA AND
NAD ANALOG AND OF 306-660 OF MUTANTS ALA-433; GLU-619; MET-619 AND
TYR-619, MUTAGENESIS OF SER-433 AND ARG-619, SUBUNIT, AND REACTION
MECHANISM.
PubMed=15939024; DOI=10.1016/j.str.2005.03.018;
Gatzeva-Topalova P.Z., May A.P., Sousa M.C.;
"Structure and mechanism of ArnA: conformational change implies
ordered dehydrogenase mechanism in key enzyme for polymyxin
resistance.";
Structure 13:929-942(2005).
-!- FUNCTION: Bifunctional enzyme that catalyzes the oxidative
decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-
arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-
amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-
arabinose (UDP-L-Ara4FN). The modified arabinose is attached to
lipid A and is required for resistance to polymyxin and cationic
antimicrobial peptides. {ECO:0000269|PubMed:11706007,
ECO:0000269|PubMed:15695810}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucuronate + NAD(+) = UDP-beta-L-
threo-pentapyranos-4-ulose + CO(2) + NADH.
-!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + UDP-4-amino-4-
deoxy-beta-L-arabinose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-
formamido-beta-L-arabinose.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.76 mM for NAD {ECO:0000269|PubMed:15491143};
KM=0.086 mM for UDP-GlcUA {ECO:0000269|PubMed:15491143};
-!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-
beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-
arabinose from UDP-alpha-D-glucuronate: step 1/3.
{ECO:0000269|PubMed:17928292}.
-!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-
beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-
arabinose from UDP-alpha-D-glucuronate: step 3/3.
{ECO:0000269|PubMed:17928292}.
-!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
biosynthesis. {ECO:0000269|PubMed:17928292}.
-!- SUBUNIT: Homohexamer, formed by a dimer of trimers.
{ECO:0000269|PubMed:15809294, ECO:0000269|PubMed:15939024}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-545305, EBI-545305;
P76092:ynbC; NbExp=2; IntAct=EBI-545305, EBI-544837;
-!- INDUCTION: Induced by BasR. {ECO:0000269|PubMed:15569938}.
-!- SIMILARITY: In the N-terminal section; belongs to the Fmt family.
UDP-L-Ara4N formyltransferase subfamily. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the NAD(P)-
dependent epimerase/dehydratase family. UDP-glucuronic acid
decarboxylase subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY057445; AAL23678.1; -; Genomic_DNA.
EMBL; U00096; AAC75315.1; -; Genomic_DNA.
EMBL; AP009048; BAA16078.1; -; Genomic_DNA.
PIR; E64996; E64996.
RefSeq; NP_416758.1; NC_000913.3.
RefSeq; WP_000860273.1; NZ_LN832404.1.
PDB; 1U9J; X-ray; 2.40 A; A=306-660.
PDB; 1YRW; X-ray; 1.70 A; A=1-300.
PDB; 1Z73; X-ray; 2.50 A; A=306-660.
PDB; 1Z74; X-ray; 2.70 A; A=306-660.
PDB; 1Z75; X-ray; 2.40 A; A=306-660.
PDB; 1Z7B; X-ray; 2.31 A; A=306-660.
PDB; 1Z7E; X-ray; 3.00 A; A/B/C/D/E/F=1-660.
PDB; 2BLL; X-ray; 2.30 A; A=317-660.
PDB; 2BLN; X-ray; 1.20 A; A/B=1-305.
PDB; 4WKG; X-ray; 2.70 A; A/B/C/D/E/F=1-660.
PDBsum; 1U9J; -.
PDBsum; 1YRW; -.
PDBsum; 1Z73; -.
PDBsum; 1Z74; -.
PDBsum; 1Z75; -.
PDBsum; 1Z7B; -.
PDBsum; 1Z7E; -.
PDBsum; 2BLL; -.
PDBsum; 2BLN; -.
PDBsum; 4WKG; -.
ProteinModelPortal; P77398; -.
SMR; P77398; -.
BioGrid; 4260497; 259.
DIP; DIP-11961N; -.
IntAct; P77398; 15.
MINT; MINT-1257581; -.
STRING; 316385.ECDH10B_2415; -.
DrugBank; DB03256; (6R)-Folinic acid.
DrugBank; DB03685; Uridine-5'-Monophosphate.
PaxDb; P77398; -.
PRIDE; P77398; -.
EnsemblBacteria; AAC75315; AAC75315; b2255.
EnsemblBacteria; BAA16078; BAA16078; BAA16078.
GeneID; 947683; -.
KEGG; ecj:JW2249; -.
KEGG; eco:b2255; -.
PATRIC; fig|1411691.4.peg.4482; -.
EchoBASE; EB3844; -.
EcoGene; EG14091; arnA.
eggNOG; ENOG4105C3I; Bacteria.
eggNOG; COG0223; LUCA.
eggNOG; COG0451; LUCA.
HOGENOM; HOG000247761; -.
InParanoid; P77398; -.
KO; K10011; -.
PhylomeDB; P77398; -.
BioCyc; EcoCyc:G7168-MONOMER; -.
BioCyc; MetaCyc:G7168-MONOMER; -.
BRENDA; 1.1.1.305; 2026.
BRENDA; 2.1.2.13; 2026.
SABIO-RK; P77398; -.
UniPathway; UPA00030; -.
UniPathway; UPA00032; UER00492.
UniPathway; UPA00032; UER00494.
EvolutionaryTrace; P77398; -.
PRO; PR:P77398; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
GO; GO:0099619; F:UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity; IDA:EcoCyc.
GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; IDA:UniProtKB.
GO; GO:0099618; F:UDP-glucuronic acid dehydrogenase activity; IDA:EcoCyc.
GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0034214; P:protein hexamerization; IDA:EcoCyc.
GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
GO; GO:2001315; P:UDP-4-deoxy-4-formamido-beta-L-arabinopyranose biosynthetic process; IMP:EcoCyc.
GO; GO:0033320; P:UDP-D-xylose biosynthetic process; IDA:UniProtKB.
Gene3D; 3.10.25.10; -; 1.
Gene3D; 3.40.50.170; -; 1.
HAMAP; MF_01166; ArnA; 1.
InterPro; IPR021168; Bifun_polymyxin_resist_ArnA.
InterPro; IPR001509; Epimerase_deHydtase.
InterPro; IPR005793; Formyl_trans_C.
InterPro; IPR037022; Formyl_trans_C_sf.
InterPro; IPR002376; Formyl_transf_N.
InterPro; IPR036477; Formyl_transf_N_sf.
InterPro; IPR011034; Formyl_transferase-like_C_sf.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF01370; Epimerase; 1.
Pfam; PF02911; Formyl_trans_C; 1.
Pfam; PF00551; Formyl_trans_N; 1.
PIRSF; PIRSF036506; Bifun_polymyxin_resist_ArnA; 1.
SUPFAM; SSF50486; SSF50486; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF53328; SSF53328; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Complete proteome;
Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
Lipopolysaccharide biosynthesis; Multifunctional enzyme; NAD;
Oxidoreductase; Reference proteome; Transferase.
CHAIN 1 660 Bifunctional polymyxin resistance protein
ArnA.
/FTId=PRO_0000083098.
NP_BIND 368 369 NAD binding.
REGION 1 304 Formyltransferase ArnAFT.
REGION 86 88 10-formyltetrahydrofolate binding.
REGION 136 140 10-formyltetrahydrofolate binding.
REGION 314 660 Dehydrogenase ArnADH.
REGION 432 433 UDP-glucuronate binding.
REGION 526 535 UDP-glucuronate binding.
ACT_SITE 104 104 Proton donor; for formyltransferase
activity.
ACT_SITE 434 434 Proton acceptor; for decarboxylase
activity.
ACT_SITE 619 619 Proton donor; for decarboxylase activity.
BINDING 114 114 10-formyltetrahydrofolate.
BINDING 347 347 NAD.
BINDING 393 393 UDP-glucuronate; via carbonyl oxygen.
BINDING 398 398 UDP-glucuronate.
BINDING 460 460 UDP-glucuronate.
BINDING 492 492 UDP-glucuronate.
BINDING 613 613 UDP-glucuronate.
SITE 102 102 Transition state stabilizer.
SITE 140 140 Raises pKa of active site His.
MUTAGEN 102 102 N->A: No activity.
{ECO:0000269|PubMed:15807526}.
MUTAGEN 104 104 H->A: 25-fold lower activity.
{ECO:0000269|PubMed:15807526}.
MUTAGEN 104 104 H->K: Less than 1% residual activity.
{ECO:0000269|PubMed:15807526}.
MUTAGEN 140 140 D->A,N: Less than 1% residual activity.
{ECO:0000269|PubMed:15807526}.
MUTAGEN 433 433 S->A: 40-fold lower specific activity.
{ECO:0000269|PubMed:15809294,
ECO:0000269|PubMed:15939024}.
MUTAGEN 433 433 S->T: No activity.
{ECO:0000269|PubMed:15809294,
ECO:0000269|PubMed:15939024}.
MUTAGEN 434 434 E->A: 100-fold lower specific activity.
{ECO:0000269|PubMed:15809294}.
MUTAGEN 434 434 E->Q: No activity.
{ECO:0000269|PubMed:15809294}.
MUTAGEN 619 619 R->E,Y: No activity.
{ECO:0000269|PubMed:15939024}.
MUTAGEN 619 619 R->M: 400-fold lower activity.
{ECO:0000269|PubMed:15939024}.
STRAND 2 7 {ECO:0000244|PDB:2BLN}.
HELIX 9 21 {ECO:0000244|PDB:2BLN}.
STRAND 25 30 {ECO:0000244|PDB:2BLN}.
HELIX 45 52 {ECO:0000244|PDB:2BLN}.
HELIX 65 73 {ECO:0000244|PDB:2BLN}.
STRAND 77 83 {ECO:0000244|PDB:2BLN}.
HELIX 90 93 {ECO:0000244|PDB:2BLN}.
STRAND 100 106 {ECO:0000244|PDB:2BLN}.
TURN 108 111 {ECO:0000244|PDB:2BLN}.
STRAND 112 114 {ECO:0000244|PDB:2BLN}.
HELIX 116 122 {ECO:0000244|PDB:2BLN}.
STRAND 126 134 {ECO:0000244|PDB:2BLN}.
TURN 139 141 {ECO:0000244|PDB:1Z7E}.
STRAND 144 151 {ECO:0000244|PDB:2BLN}.
HELIX 158 181 {ECO:0000244|PDB:2BLN}.
HELIX 192 194 {ECO:0000244|PDB:2BLN}.
HELIX 203 206 {ECO:0000244|PDB:2BLN}.
HELIX 214 223 {ECO:0000244|PDB:2BLN}.
STRAND 231 235 {ECO:0000244|PDB:2BLN}.
STRAND 238 248 {ECO:0000244|PDB:2BLN}.
STRAND 258 261 {ECO:0000244|PDB:2BLN}.
TURN 262 264 {ECO:0000244|PDB:2BLN}.
STRAND 265 268 {ECO:0000244|PDB:2BLN}.
STRAND 270 281 {ECO:0000244|PDB:2BLN}.
HELIX 289 296 {ECO:0000244|PDB:2BLN}.
STRAND 299 301 {ECO:0000244|PDB:1Z7E}.
STRAND 317 322 {ECO:0000244|PDB:2BLL}.
HELIX 326 337 {ECO:0000244|PDB:2BLL}.
STRAND 342 348 {ECO:0000244|PDB:2BLL}.
HELIX 351 356 {ECO:0000244|PDB:2BLL}.
STRAND 362 366 {ECO:0000244|PDB:2BLL}.
TURN 369 371 {ECO:0000244|PDB:2BLL}.
HELIX 374 382 {ECO:0000244|PDB:2BLL}.
STRAND 384 388 {ECO:0000244|PDB:2BLL}.
HELIX 395 400 {ECO:0000244|PDB:2BLL}.
HELIX 402 409 {ECO:0000244|PDB:2BLL}.
HELIX 411 422 {ECO:0000244|PDB:2BLL}.
STRAND 426 430 {ECO:0000244|PDB:2BLL}.
HELIX 433 436 {ECO:0000244|PDB:2BLL}.
STRAND 442 444 {ECO:0000244|PDB:2BLL}.
TURN 446 448 {ECO:0000244|PDB:2BLL}.
STRAND 451 453 {ECO:0000244|PDB:4WKG}.
HELIX 459 461 {ECO:0000244|PDB:2BLL}.
HELIX 462 481 {ECO:0000244|PDB:2BLL}.
STRAND 485 490 {ECO:0000244|PDB:2BLL}.
STRAND 492 494 {ECO:0000244|PDB:2BLL}.
STRAND 504 506 {ECO:0000244|PDB:2BLL}.
HELIX 510 521 {ECO:0000244|PDB:2BLL}.
STRAND 525 527 {ECO:0000244|PDB:2BLL}.
HELIX 528 530 {ECO:0000244|PDB:2BLL}.
STRAND 534 536 {ECO:0000244|PDB:2BLL}.
HELIX 540 552 {ECO:0000244|PDB:2BLL}.
HELIX 554 556 {ECO:0000244|PDB:2BLL}.
TURN 557 560 {ECO:0000244|PDB:2BLL}.
STRAND 561 565 {ECO:0000244|PDB:2BLL}.
STRAND 570 573 {ECO:0000244|PDB:2BLL}.
HELIX 574 586 {ECO:0000244|PDB:2BLL}.
HELIX 591 593 {ECO:0000244|PDB:2BLL}.
STRAND 600 602 {ECO:0000244|PDB:2BLL}.
HELIX 606 609 {ECO:0000244|PDB:1Z7E}.
HELIX 624 630 {ECO:0000244|PDB:2BLL}.
HELIX 638 652 {ECO:0000244|PDB:2BLL}.
SEQUENCE 660 AA; 74289 MW; A430928AB4041FA3 CRC64;
MKTVVFAYHD MGCLGIEALL AAGYEISAIF THTDNPGEKA FYGSVARLAA ERGIPVYAPD
NVNHPLWVER IAQLSPDVIF SFYYRHLIYD EILQLAPAGA FNLHGSLLPK YRGRAPLNWV
LVNGETETGV TLHRMVKRAD AGAIVAQLRI AIAPDDIAIT LHHKLCHAAR QLLEQTLPAI
KHGNILEIAQ RENEATCFGR RTPDDSFLEW HKPASVLHNM VRAVADPWPG AFSYVGNQKF
TVWSSRVHPH ASKAQPGSVI SVAPLLIACG DGALEIVTGQ AGDGITMQGS QLAQTLGLVQ
GSRLNSQPAC TARRRTRVLI LGVNGFIGNH LTERLLREDH YEVYGLDIGS DAISRFLNHP
HFHFVEGDIS IHSEWIEYHV KKCDVVLPLV AIATPIEYTR NPLRVFELDF EENLRIIRYC
VKYRKRIIFP STSEVYGMCS DKYFDEDHSN LIVGPVNKPR WIYSVSKQLL DRVIWAYGEK
EGLQFTLFRP FNWMGPRLDN LNAARIGSSR AITQLILNLV EGSPIKLIDG GKQKRCFTDI
RDGIEALYRI IENAGNRCDG EIINIGNPEN EASIEELGEM LLASFEKHPL RHHFPPFAGF
RVVESSSYYG KGYQDVEHRK PSIRNAHRCL DWEPKIDMQE TIDETLDFFL RTVDLTDKPS


Related products :

Catalog number Product name Quantity
30-461 CSGlcA-T belongs to the chondroitin N-acetylgalactosaminyltransferase family. It transfers glucuronic acid (GlcUA) from UDP-GlcUA to N-acetylgalactosamine residues on the non-reducing end of the elong 0.05 mg
26-230 ChGn transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of glucuronic acid (GlcUA). This protein is required for addition of the first GalNAc to the core tetrasacchar 0.05 mg
CSB-EL002299CH Chicken Bifunctional purine biosynthesis protein PURH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase(ATIC) ELISA kit 96T
CSB-EL002299HU Human Bifunctional purine biosynthesis protein PURH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase(ATIC) ELISA kit 96T
CSB-EL002299BO Bovine Bifunctional purine biosynthesis protein PURH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase(ATIC) ELISA kit 96T
CSB-EL002299MO Mouse Bifunctional purine biosynthesis protein PURH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase(ATIC) ELISA kit 96T
CSB-EL002299HU Human Bifunctional purine biosynthesis protein PURH [Includes Phosphoribosylaminoimidazolecarboxamide formyltransferase(ATIC) ELISA kit SpeciesHuman 96T
CSB-EL002299CH Chicken Bifunctional purine biosynthesis protein PURH [Includes Phosphoribosylaminoimidazolecarboxamide formyltransferase(ATIC) ELISA kit SpeciesChicken 96T
CSB-EL002299MO Mouse Bifunctional purine biosynthesis protein PURH [Includes Phosphoribosylaminoimidazolecarboxamide formyltransferase(ATIC) ELISA kit SpeciesMouse 96T
CSB-EL002299BO Bovine Bifunctional purine biosynthesis protein PURH [Includes Phosphoribosylaminoimidazolecarboxamide formyltransferase(ATIC) ELISA kit SpeciesBovine 96T
EIAAB45517 Mouse,Mus musculus,UDP-glucuronate decarboxylase 1,UDP-glucuronic acid decarboxylase 1,UGD,Uxs1,UXS-1
EIAAB45515 Rat,Rattus norvegicus,UDP-glucuronate decarboxylase 1,UDP-glucuronic acid decarboxylase 1,UGD,Uxs1,UXS-1
E1749h Rat ELISA Kit FOR UDP-glucuronic acid decarboxylase 1 96T
EIAAB45516 Homo sapiens,Human,UDP-glucuronate decarboxylase 1,UDP-glucuronic acid decarboxylase 1,UGD,UNQ2538_PRO6079,UXS1,UXS-1
I0551 UDP-glucuronic acid decarboxylase 1 (UXS1), Rat, ELISA Kit 96T
CSB-EL025777RA Rat UDP-glucuronic acid decarboxylase 1(UXS1) ELISA kit 96T
E1895m Human ELISA Kit FOR UDP-glucuronic acid decarboxylase 1 96T
I0549 UDP-glucuronic acid decarboxylase 1 (UXS1), Human, ELISA Kit 96T
I0550 UDP-glucuronic acid decarboxylase 1 (UXS1), Mouse, ELISA Kit 96T
CSB-EL025777RA Rat UDP-glucuronic acid decarboxylase 1(UXS1) ELISA kit SpeciesRat 96T
CSB-EL025777HU Human UDP-glucuronic acid decarboxylase 1(UXS1) ELISA kit 96T
CSB-EL025777MO Mouse UDP-glucuronic acid decarboxylase 1(UXS1) ELISA kit 96T
CSB-EL025777MO Mouse UDP-glucuronic acid decarboxylase 1(UXS1) ELISA kit SpeciesMouse 96T
UXS1_RAT ELISA Kit FOR UDP-glucuronic acid decarboxylase 1; organism: Rat; gene name: Uxs1 96T
CSB-EL025777HU Human UDP-glucuronic acid decarboxylase 1(UXS1) ELISA kit SpeciesHuman 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