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DNA ligase (EC 6.5.1.2) (Polydeoxyribonucleotide synthase [NAD( )])

 DNLJ_ECOLI              Reviewed;         671 AA.
P15042; P78197; P78198;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
25-OCT-2017, entry version 169.
RecName: Full=DNA ligase;
EC=6.5.1.2;
AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)];
Name=ligA; Synonyms=dnaL, lig, lop, pdeC;
OrderedLocusNames=b2411, JW2403;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-13 AND
666-671.
STRAIN=K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
PubMed=3018436; DOI=10.1007/BF00330179;
Ishino Y., Shinagawa H., Makino K., Tsunasawa S., Sakiyama F.,
Nakata A.;
"Nucleotide sequence of the lig gene and primary structure of DNA
ligase of Escherichia coli.";
Mol. Gen. Genet. 204:1-7(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
O'Connor M.J., Ally A., Ally D., Zhang X., Robichaud M., Backman K.;
Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
STRAIN=PB103;
PubMed=9008158; DOI=10.1016/S0092-8674(00)81838-3;
Hale C.A., de Boer P.A.J.;
"Direct binding of FtsZ to ZipA, an essential component of the septal
ring structure that mediates cell division in E. coli.";
Cell 88:175-185(1997).
[7]
CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF GLU-10; TYR-22; HIS-23;
ASP-32; TYR-35 AND ASP-36, AND ACTIVE SITE.
PubMed=11781321; DOI=10.1074/jbc.M111164200;
Sriskanda V., Shuman S.;
"Conserved residues in domain Ia are required for the reaction of
Escherichia coli DNA ligase with NAD+.";
J. Biol. Chem. 277:9695-9700(2002).
[8]
MUTAGENESIS OF LYS-115; ASP-117; GLY-118; ASP-138; GLU-143; GLY-172;
GLU-173; ASN-198; ARG-200; ARG-208; ARG-277; ASP-285; GLY-286;
VAL-288; LYS-290 AND LYS-314.
PubMed=15671015; DOI=10.1074/jbc.M413685200;
Zhu H., Shuman S.;
"Structure-guided mutational analysis of the nucleotidyltransferase
domain of Escherichia coli NAD+-dependent DNA ligase (LigA).";
J. Biol. Chem. 280:12137-12144(2005).
[9]
MUTAGENESIS OF ARG-333; THR-334; ARG-342; ARG-379; 383-VAL-ILE-384;
446-ARG-ARG-447; GLY-455; ARG-487; GLY-489; GLY-521; GLY-553 AND
ARG-614.
PubMed=18515356; DOI=10.1074/jbc.M802945200;
Wang L.K., Nair P.A., Shuman S.;
"Structure-guided mutational analysis of the OB, HhH, and BRCT domains
of Escherichia coli DNA ligase.";
J. Biol. Chem. 283:23343-23352(2008).
[10]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ZINC IONS; AMP
AND DNA.
PubMed=17466627; DOI=10.1016/j.molcel.2007.02.026;
Nandakumar J., Nair P.A., Shuman S.;
"Last stop on the road to repair: structure of E. coli DNA ligase
bound to nicked DNA-adenylate.";
Mol. Cell 26:257-271(2007).
-!- FUNCTION: DNA ligase that catalyzes the formation of
phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl
groups in double-stranded DNA using NAD as a coenzyme and as the
energy source for the reaction. It is essential for DNA
replication and repair of damaged DNA.
-!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl
+ 5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m)
+ AMP + beta-nicotinamide D-nucleotide.
{ECO:0000269|PubMed:11781321}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11781321};
-!- INTERACTION:
P07813:leuS; NbExp=3; IntAct=EBI-553496, EBI-553345;
-!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
subfamily. {ECO:0000305}.
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EMBL; M30255; AAA24071.1; -; Genomic_DNA.
EMBL; M24278; AAA24070.1; -; Genomic_DNA.
EMBL; U00096; AAC75464.1; -; Genomic_DNA.
EMBL; AP009048; BAA16282.2; -; Genomic_DNA.
EMBL; U74650; AAB42062.1; -; Genomic_DNA.
PIR; B65015; LQECC6.
RefSeq; NP_416906.1; NC_000913.3.
RefSeq; WP_000443661.1; NZ_LN832404.1.
PDB; 2OWO; X-ray; 2.30 A; A=1-671.
PDB; 4GLX; X-ray; 1.90 A; A=1-586.
PDB; 5TT5; X-ray; 1.55 A; A=1-671.
PDBsum; 2OWO; -.
PDBsum; 4GLX; -.
PDBsum; 5TT5; -.
ProteinModelPortal; P15042; -.
SMR; P15042; -.
BioGrid; 4259672; 128.
DIP; DIP-10098N; -.
IntAct; P15042; 20.
MINT; MINT-204717; -.
STRING; 316385.ECDH10B_2576; -.
PaxDb; P15042; -.
PRIDE; P15042; -.
EnsemblBacteria; AAC75464; AAC75464; b2411.
EnsemblBacteria; BAA16282; BAA16282; BAA16282.
GeneID; 946885; -.
KEGG; ecj:JW2403; -.
KEGG; eco:b2411; -.
PATRIC; fig|1411691.4.peg.4320; -.
EchoBASE; EB0529; -.
EcoGene; EG10534; ligA.
eggNOG; ENOG4105C77; Bacteria.
eggNOG; COG0272; LUCA.
HOGENOM; HOG000218459; -.
InParanoid; P15042; -.
KO; K01972; -.
PhylomeDB; P15042; -.
BioCyc; EcoCyc:EG10534-MONOMER; -.
BioCyc; MetaCyc:EG10534-MONOMER; -.
BRENDA; 6.5.1.2; 2026.
EvolutionaryTrace; P15042; -.
PRO; PR:P15042; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
GO; GO:0003911; F:DNA ligase (NAD+) activity; IDA:EcoliWiki.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070403; F:NAD+ binding; IMP:EcoCyc.
GO; GO:0006288; P:base-excision repair, DNA ligation; IDA:EcoCyc.
GO; GO:0006266; P:DNA ligation; IDA:EcoCyc.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
CDD; cd00027; BRCT; 1.
CDD; cd00114; LIGANc; 1.
Gene3D; 3.40.50.10190; -; 1.
HAMAP; MF_01588; DNA_ligase_A; 1.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR018239; DNA_ligase_AS.
InterPro; IPR033136; DNA_ligase_CS.
InterPro; IPR001679; DNAligase.
InterPro; IPR013839; DNAligase_adenylation.
InterPro; IPR013840; DNAligase_N.
InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR004150; NAD_DNA_ligase_OB.
InterPro; IPR010994; RuvA_2-like.
InterPro; IPR004149; Znf_DNAligase_C4.
Pfam; PF00533; BRCT; 1.
Pfam; PF01653; DNA_ligase_aden; 1.
Pfam; PF03120; DNA_ligase_OB; 1.
Pfam; PF03119; DNA_ligase_ZBD; 1.
PIRSF; PIRSF001604; LigA; 1.
SMART; SM00292; BRCT; 1.
SMART; SM00278; HhH1; 4.
SMART; SM00532; LIGANc; 1.
SUPFAM; SSF47781; SSF47781; 1.
SUPFAM; SSF50249; SSF50249; 1.
SUPFAM; SSF52113; SSF52113; 1.
TIGRFAMs; TIGR00575; dnlj; 1.
PROSITE; PS50172; BRCT; 1.
PROSITE; PS01055; DNA_LIGASE_N1; 1.
PROSITE; PS01056; DNA_LIGASE_N2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
DNA damage; DNA repair; DNA replication; Ligase; Magnesium;
Metal-binding; NAD; Reference proteome; Zinc.
CHAIN 1 671 DNA ligase.
/FTId=PRO_0000161745.
DOMAIN 593 671 BRCT.
NP_BIND 32 36 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
NP_BIND 81 82 NAD. {ECO:0000255|HAMAP-Rule:MF_01588,
ECO:0000305|PubMed:17466627}.
REGION 330 334 Interaction with target DNA.
{ECO:0000305|PubMed:17466627}.
REGION 453 458 Interaction with target DNA.
{ECO:0000305|PubMed:17466627}.
REGION 519 524 Interaction with target DNA.
{ECO:0000305|PubMed:17466627}.
REGION 551 556 Interaction with target DNA.
{ECO:0000305|PubMed:17466627}.
ACT_SITE 115 115 N6-AMP-lysine intermediate.
{ECO:0000255|HAMAP-Rule:MF_01588,
ECO:0000269|PubMed:11781321}.
METAL 408 408 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588,
ECO:0000269|PubMed:17466627}.
METAL 411 411 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588,
ECO:0000269|PubMed:17466627}.
METAL 426 426 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588,
ECO:0000269|PubMed:17466627}.
METAL 432 432 Zinc. {ECO:0000255|HAMAP-Rule:MF_01588,
ECO:0000269|PubMed:17466627}.
BINDING 113 113 NAD. {ECO:0000255|HAMAP-Rule:MF_01588,
ECO:0000305|PubMed:17466627}.
BINDING 136 136 NAD. {ECO:0000255|HAMAP-Rule:MF_01588,
ECO:0000305|PubMed:17466627}.
BINDING 173 173 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
BINDING 290 290 NAD. {ECO:0000255|HAMAP-Rule:MF_01588,
ECO:0000305|PubMed:17466627}.
BINDING 314 314 NAD. {ECO:0000255|HAMAP-Rule:MF_01588}.
SITE 487 487 Interaction with target DNA.
{ECO:0000305|PubMed:17466627}.
SITE 492 492 Interaction with target DNA.
{ECO:0000305|PubMed:17466627}.
MUTAGEN 10 10 E->A: No effect.
{ECO:0000269|PubMed:11781321}.
MUTAGEN 22 22 Y->A,S: Reduces nick joining activity by
99.9%. {ECO:0000269|PubMed:11781321}.
MUTAGEN 22 22 Y->F: Reduces nick joining activity by
91%. {ECO:0000269|PubMed:11781321}.
MUTAGEN 23 23 H->A,Y: Reduces nick joining activity by
90%. {ECO:0000269|PubMed:11781321}.
MUTAGEN 32 32 D->A,E: Reduces nick joining activity by
99%. {ECO:0000269|PubMed:11781321}.
MUTAGEN 32 32 D->N: Reduces nick joining activity by
91%. {ECO:0000269|PubMed:11781321}.
MUTAGEN 35 35 Y->A: Reduces nick joining activity by
98%. {ECO:0000269|PubMed:11781321}.
MUTAGEN 35 35 Y->F: Reduces nick joining activity by
77%. {ECO:0000269|PubMed:11781321}.
MUTAGEN 35 35 Y->S: Reduces nick joining activity by
99.9%. {ECO:0000269|PubMed:11781321}.
MUTAGEN 36 36 D->A: Reduces nick joining activity by
99.8%. {ECO:0000269|PubMed:11781321}.
MUTAGEN 36 36 D->E: Reduces nick joining activity by
96%. {ECO:0000269|PubMed:11781321}.
MUTAGEN 36 36 D->N: Reduces nick joining activity by
88%. {ECO:0000269|PubMed:11781321}.
MUTAGEN 115 115 K->Q,R: Reduces nick joining activity by
99.9%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 117 117 D->E: Reduces nick joining activity by
97%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 117 117 D->N: Reduces nick joining activity by
99.9%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 118 118 G->A: Reduces nick joining activity by
99.9%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 138 138 D->A: Reduces nick joining activity by
63%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 143 143 E->A: Reduces nick joining activity by
48%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 172 172 G->A: Reduces nick joining activity by
64%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 173 173 E->A,D,Q: Reduces nick joining activity
by 99.9%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 198 198 N->A: Reduces nick joining activity by
74%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 200 200 R->A,K,Q: Reduces nick joining activity
by 99.9%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 208 208 R->A,K,Q: Reduces nick joining activity
by 99%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 277 277 R->A: Reduces nick joining activity by
99%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 285 285 D->E: Reduces nick joining activity by
96%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 285 285 D->N: Reduces nick joining activity by
99%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 286 286 G->A: Reduces nick joining activity by
86%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 288 288 V->A: Reduces nick joining activity by
25%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 290 290 K->A: Reduces nick joining activity by
87%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 314 314 K->Q: Reduces nick joining activity by
99%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 314 314 K->R: Reduces nick joining activity by
95%. {ECO:0000269|PubMed:15671015}.
MUTAGEN 333 333 R->A,Q: Reduces nick joining activity by
over 95%. Abolishes nick joining
activity; when associated with A-334.
{ECO:0000269|PubMed:18515356}.
MUTAGEN 334 334 T->A: Abolishes nick joining activity;
when associated with A-333.
{ECO:0000269|PubMed:18515356}.
MUTAGEN 342 342 R->A: Reduces nick joining activity by
80%. {ECO:0000269|PubMed:18515356}.
MUTAGEN 379 379 R->A,Q: Reduces nick joining activity by
over 95%. {ECO:0000269|PubMed:18515356}.
MUTAGEN 383 384 VI->AA: Reduces nick joining activity by
95%. {ECO:0000269|PubMed:18515356}.
MUTAGEN 446 447 RR->AA: Reduces nick joining activity by
95%. {ECO:0000269|PubMed:18515356}.
MUTAGEN 455 455 G->A: Reduces nick joining activity by
50%. {ECO:0000269|PubMed:18515356}.
MUTAGEN 455 455 G->D,V: Reduces nick joining activity by
95%. {ECO:0000269|PubMed:18515356}.
MUTAGEN 487 487 R->A: Reduces nick joining activity by
over 90%. {ECO:0000269|PubMed:18515356}.
MUTAGEN 489 489 G->D,V: Reduces nick joining activity by
95%. {ECO:0000269|PubMed:18515356}.
MUTAGEN 521 521 G->A: Reduces nick joining activity by
95%. {ECO:0000269|PubMed:18515356}.
MUTAGEN 521 521 G->D,V: Loss of nick joining activity.
{ECO:0000269|PubMed:18515356}.
MUTAGEN 553 553 G->D,V: Reduces nick joining activity by
95%. {ECO:0000269|PubMed:18515356}.
MUTAGEN 614 614 R->A: Reduces nick joining activity by
85%. {ECO:0000269|PubMed:18515356}.
CONFLICT 69 69 A -> R (in Ref. 1; AAA24071).
{ECO:0000305}.
HELIX 4 24 {ECO:0000244|PDB:4GLX}.
STRAND 28 30 {ECO:0000244|PDB:4GLX}.
HELIX 34 48 {ECO:0000244|PDB:4GLX}.
HELIX 50 52 {ECO:0000244|PDB:4GLX}.
HELIX 58 60 {ECO:0000244|PDB:4GLX}.
STRAND 72 74 {ECO:0000244|PDB:4GLX}.
STRAND 83 85 {ECO:0000244|PDB:2OWO}.
HELIX 88 100 {ECO:0000244|PDB:4GLX}.
STRAND 102 104 {ECO:0000244|PDB:2OWO}.
STRAND 110 126 {ECO:0000244|PDB:4GLX}.
STRAND 129 135 {ECO:0000244|PDB:4GLX}.
STRAND 139 144 {ECO:0000244|PDB:4GLX}.
HELIX 146 149 {ECO:0000244|PDB:4GLX}.
STRAND 161 163 {ECO:0000244|PDB:4GLX}.
STRAND 166 175 {ECO:0000244|PDB:4GLX}.
HELIX 178 190 {ECO:0000244|PDB:4GLX}.
HELIX 199 207 {ECO:0000244|PDB:4GLX}.
HELIX 212 216 {ECO:0000244|PDB:4GLX}.
STRAND 221 233 {ECO:0000244|PDB:4GLX}.
HELIX 239 248 {ECO:0000244|PDB:4GLX}.
STRAND 258 262 {ECO:0000244|PDB:4GLX}.
HELIX 263 276 {ECO:0000244|PDB:4GLX}.
HELIX 277 279 {ECO:0000244|PDB:4GLX}.
STRAND 280 282 {ECO:0000244|PDB:4GLX}.
STRAND 284 293 {ECO:0000244|PDB:4GLX}.
HELIX 294 300 {ECO:0000244|PDB:4GLX}.
STRAND 304 313 {ECO:0000244|PDB:4GLX}.
STRAND 319 331 {ECO:0000244|PDB:4GLX}.
STRAND 335 348 {ECO:0000244|PDB:4GLX}.
STRAND 351 357 {ECO:0000244|PDB:4GLX}.
HELIX 361 367 {ECO:0000244|PDB:4GLX}.
STRAND 374 380 {ECO:0000244|PDB:4GLX}.
TURN 381 383 {ECO:0000244|PDB:4GLX}.
STRAND 384 390 {ECO:0000244|PDB:4GLX}.
HELIX 392 394 {ECO:0000244|PDB:4GLX}.
TURN 409 411 {ECO:0000244|PDB:4GLX}.
STRAND 414 416 {ECO:0000244|PDB:4GLX}.
STRAND 425 427 {ECO:0000244|PDB:4GLX}.
HELIX 429 431 {ECO:0000244|PDB:4GLX}.
HELIX 433 444 {ECO:0000244|PDB:4GLX}.
TURN 446 449 {ECO:0000244|PDB:4GLX}.
HELIX 456 464 {ECO:0000244|PDB:4GLX}.
HELIX 471 475 {ECO:0000244|PDB:4GLX}.
HELIX 479 483 {ECO:0000244|PDB:4GLX}.
HELIX 490 503 {ECO:0000244|PDB:4GLX}.
HELIX 508 514 {ECO:0000244|PDB:4GLX}.
HELIX 522 532 {ECO:0000244|PDB:4GLX}.
HELIX 535 540 {ECO:0000244|PDB:4GLX}.
HELIX 543 546 {ECO:0000244|PDB:4GLX}.
HELIX 554 565 {ECO:0000244|PDB:4GLX}.
HELIX 567 578 {ECO:0000244|PDB:4GLX}.
SEQUENCE 671 AA; 73606 MW; DD2BDC64D8E65256 CRC64;
MESIEQQLTE LRTTLRHHEY LYHVMDAPEI PDAEYDRLMR ELRELETKHP ELITPDSPTQ
RVGAAPLAAF SQIRHEVPML SLDNVFDEES FLAFNKRVQD RLKNNEKVTW CCELKLDGLA
VSILYENGVL VSAATRGDGT TGEDITSNVR TIRAIPLKLH GENIPARLEV RGEVFLPQAG
FEKINEDARR TGGKVFANPR NAAAGSLRQL DPRITAKRPL TFFCYGVGVL EGGELPDTHL
GRLLQFKKWG LPVSDRVTLC ESAEEVLAFY HKVEEDRPTL GFDIDGVVIK VNSLAQQEQL
GFVARAPRWA VAFKFPAQEQ MTFVRDVEFQ VGRTGAITPV ARLEPVHVAG VLVSNATLHN
ADEIERLGLR IGDKVVIRRA GDVIPQVVNV VLSERPEDTR EVVFPTHCPV CGSDVERVEG
EAVARCTGGL ICGAQRKESL KHFVSRRAMD VDGMGDKIID QLVEKEYVHT PADLFKLTAG
KLTGLERMGP KSAQNVVNAL EKAKETTFAR FLYALGIREV GEATAAGLAA YFGTLEALEA
ASIEELQKVP DVGIVVASHV HNFFAEESNR NVISELLAEG VHWPAPIVIN AEEIDSPFAG
KTVVLTGSLS QMSRDDAKAR LVELGAKVAG SVSKKTDLVI AGEAAGSKLA KAQELGIEVI
DEAEMLRLLG S


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EIAAB11595 Chicken,DNA ligase 4,DNA ligase IV,Gallus gallus,LIG4,Polydeoxyribonucleotide synthase [ATP] 4,RCJMB04_10b2
18-272-195933 Lig1 - Rabbit polyclonal to Lig1; EC 6.5.1.1; DNA ligase I; Polydeoxyribonucleotide synthase [ATP] 1 Polyclonal 0.2 ml
EIAAB33280 CTP synthase 2,CTP synthetase 2,Ctps2,Rat,Rattus norvegicus,UTP--ammonia ligase 2
EIAAB33278 CTP synthase 1,CTP synthetase 1,Ctps,Mouse,Mus musculus,UTP--ammonia ligase 1
EIAAB33282 Bos taurus,Bovine,CTP synthase 2,CTP synthetase 2,CTPS2,UTP--ammonia ligase 2
EIAAB33281 CTP synthase 2,CTP synthetase 2,Ctps2,CTPsH,Mouse,Mus musculus,UTP--ammonia ligase 2
EIAAB33279 CTP synthase 1,CTP synthetase 1,CTPS,Homo sapiens,Human,UTP--ammonia ligase 1
EIAAB33284 CTP synthase 2,CTP synthetase 2,CTPS2,Homo sapiens,Human,UTP--ammonia ligase 2
EIAAB25831 C1orf166,E3 ubiquitin-protein ligase MUL1,GIDE,Growth inhibition and death E3 ligase,Homo sapiens,Human,MAPL,Mitochondrial ubiquitin ligase activator of NFKB 1,Mitochondrial-anchored protein ligase,MU
EIAAB36858 ACSB,ACSVL6,BA-CoA ligase,BACS,BAL,Bile acid-CoA ligase,Bile acyl-CoA synthetase,Cholate--CoA ligase,FACVL3,FATP5,FATP-5,Fatty acid transport protein 5,Fatty-acid-coenzyme A ligase, very long-chain 3,
EIAAB33283 Chicken,CTP synthase 2,CTP synthetase 2,CTPS2,Gallus gallus,RCJMB04_4c5,UTP--ammonia ligase 2
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
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
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
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
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,


 

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