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

Respiratory nitrate reductase 1 alpha chain (EC 1.7.99.4) (Nitrate reductase A subunit alpha) (Quinol-nitrate oxidoreductase subunit alpha)

 NARG_ECOLI              Reviewed;        1247 AA.
P09152; P78294;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
22-NOV-2017, entry version 185.
RecName: Full=Respiratory nitrate reductase 1 alpha chain;
EC=1.7.99.4;
AltName: Full=Nitrate reductase A subunit alpha;
AltName: Full=Quinol-nitrate oxidoreductase subunit alpha;
Name=narG; Synonyms=bisD, narC; OrderedLocusNames=b1224, JW1215;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / TG1;
PubMed=2674654; DOI=10.1007/BF00331275;
Blasco F., Iobbi C., Giordano G., Chippaux M., Bonnefoy V.;
"Nitrate reductase of Escherichia coli: completion of the nucleotide
sequence of the nar operon and reassessment of the role of the alpha
and beta subunits in iron binding and electron transfer.";
Mol. Gen. Genet. 218:249-256(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / TG1;
PubMed=2233673;
Blasco F., Iobbi C., Ratouchniak J., Bonnefoy V., Chippaux M.;
"Nitrate reductases of Escherichia coli: sequence of the second
nitrate reductase and comparison with that encoded by the narGHJI
operon.";
Mol. Gen. Genet. 222:104-111(1990).
[3]
SEQUENCE REVISION.
STRAIN=K12 / TG1;
Blasco F.;
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[5]
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).
[6]
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-48.
STRAIN=K12;
PubMed=6094247; DOI=10.1016/0014-5793(84)81295-8;
McPherson M.J., Baron A.J., Pappin D.J.C., Wootton J.C.;
"Respiratory nitrate reductase of Escherichia coli. Sequence
identification of the large subunit gene.";
FEBS Lett. 177:260-264(1984).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
STRAIN=PK27;
PubMed=2995309;
Li S.F., Rabi T., Demoss J.A.;
"Delineation of two distinct regulatory domains in the 5' region of
the nar operon of Escherichia coli.";
J. Bacteriol. 164:25-32(1985).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
STRAIN=K12;
PubMed=2668029; DOI=10.1016/0014-5793(89)80906-8;
Noji S., Nohno T., Saito T., Taniguchi S.;
"The narK gene product participates in nitrate transport induced in
Escherichia coli nitrate-respiring cells.";
FEBS Lett. 252:139-143(1989).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
PubMed=3308846; DOI=10.1128/jb.169.10.4614-4620.1987;
Li S.F., Demoss J.A.;
"Promoter region of the nar operon of Escherichia coli: nucleotide
sequence and transcription initiation signals.";
J. Bacteriol. 169:4614-4620(1987).
[11]
PROTEIN SEQUENCE OF 2-11.
PubMed=3053688;
Sodergren E.J., Hsu P.Y., Demoss J.A.;
"Roles of the narJ and narI gene products in the expression of nitrate
reductase in Escherichia coli.";
J. Biol. Chem. 263:16156-16162(1988).
[12]
MUTAGENESIS OF HIS-50, AND EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
PubMed=9585550; DOI=10.1021/bi972858f;
Magalon A., Asso M., Guigliarelli B., Rothery R.A., Bertrand P.,
Giordano G., Blasco F.;
"Molybdenum cofactor properties and [Fe-S] cluster coordination in
Escherichia coli nitrate reductase A: investigation by site-directed
mutagenesis of the conserved his-50 residue in the NarG subunit.";
Biochemistry 37:7363-7370(1998).
[13]
INTERACTION WITH NARJ.
PubMed=9632249; DOI=10.1046/j.1365-2958.1998.00795.x;
Blasco F., Dos Santos J.P., Magalon A., Frixon C., Guigliarelli B.,
Santini C.L., Giordano G.;
"NarJ is a specific chaperone required for molybdenum cofactor
assembly in nitrate reductase A of Escherichia coli.";
Mol. Microbiol. 28:435-447(1998).
[14]
INTERACTION WITH NARJ, AND DOMAIN.
PubMed=16540088; DOI=10.1016/j.bbrc.2006.02.133;
Chan C.S., Howell J.M., Workentine M.L., Turner R.J.;
"Twin-arginine translocase may have a role in the chaperone function
of NarJ from Escherichia coli.";
Biochem. Biophys. Res. Commun. 343:244-251(2006).
[15]
INTERACTION WITH NARJ, AND DOMAIN.
STRAIN=K12 / MC4100 / JA176;
PubMed=16286471; DOI=10.1074/jbc.M505902200;
Vergnes A., Pommier J., Toci R., Blasco F., Giordano G., Magalon A.;
"NarJ chaperone binds on two distinct sites of the aponitrate
reductase of Escherichia coli to coordinate molybdenum cofactor
insertion and assembly.";
J. Biol. Chem. 281:2170-2176(2006).
[16]
INTERACTION WITH NARJ.
PubMed=20236317; DOI=10.1111/j.1742-4658.2010.07611.x;
Zakian S., Lafitte D., Vergnes A., Pimentel C., Sebban-Kreuzer C.,
Toci R., Claude J.B., Guerlesquin F., Magalon A.;
"Basis of recognition between the NarJ chaperone and the N-terminus of
the NarG subunit from Escherichia coli nitrate reductase.";
FEBS J. 277:1886-1895(2010).
[17]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=12910261; DOI=10.1038/nsb969;
Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F.,
Weiner J.H., Strynadka N.C.J.;
"Insights into the respiratory electron transfer pathway from the
structure of nitrate reductase A.";
Nat. Struct. Biol. 10:681-687(2003).
[18]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-1247.
PubMed=14725769; DOI=10.1016/j.str.2003.11.020;
Jormakka M., Richardson D., Byrne B., Iwata S.;
"Architecture of NarGH reveals a structural classification of Mo-
bisMGD enzymes.";
Structure 12:95-104(2004).
-!- FUNCTION: The nitrate reductase enzyme complex allows E.coli to
use nitrate as an electron acceptor during anaerobic growth. The
alpha chain is the actual site of nitrate reduction.
-!- CATALYTIC ACTIVITY: Nitrite + acceptor = nitrate + reduced
acceptor.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Note=Binds 1 [4Fe-4S] cluster per subunit.;
-!- COFACTOR:
Name=Mo-bis(molybdopterin guanine dinucleotide);
Xref=ChEBI:CHEBI:60539;
Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide)
(Mo-bis-MGD) cofactor per subunit.;
-!- SUBUNIT: Dimer of heterotrimers each composed of an alpha, a beta
and a gamma chain. Alpha and beta are catalytic chains; gamma
chains are involved in binding the enzyme complex to the
cytoplasmic membrane. Interacts with the NarJ chaperone.
{ECO:0000269|PubMed:16286471, ECO:0000269|PubMed:16540088,
ECO:0000269|PubMed:20236317, ECO:0000269|PubMed:9632249}.
-!- INTERACTION:
P11349:narH; NbExp=13; IntAct=EBI-547248, EBI-555067;
P0AF26:narJ; NbExp=18; IntAct=EBI-547248, EBI-555043;
P19317:narW; NbExp=9; IntAct=EBI-547248, EBI-555088;
P19318:narY; NbExp=5; IntAct=EBI-547248, EBI-555059;
-!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
-!- INDUCTION: By nitrate.
-!- DOMAIN: Apoenzyme contains at least 2 NarJ-binding sites, one
interfering with membrane anchoring and another being involved in
molybdenum insertion. The first binding-site is a short peptide
sequence near the N-terminus that contains a twin-arginine
homologous motif. {ECO:0000269|PubMed:16286471,
ECO:0000269|PubMed:16540088}.
-!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
oxidoreductase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/NAR/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X16181; CAA34303.1; -; Genomic_DNA.
EMBL; X01164; CAA25611.1; -; Genomic_DNA.
EMBL; M11586; AAA24201.1; -; Genomic_DNA.
EMBL; U00096; AAC74308.1; -; Genomic_DNA.
EMBL; AP009048; BAA36094.1; -; Genomic_DNA.
EMBL; X15996; CAA34127.1; -; Genomic_DNA.
EMBL; L36649; AAA64296.1; -; Genomic_DNA.
PIR; E64869; RDECNA.
RefSeq; NP_415742.1; NC_000913.3.
RefSeq; WP_000032939.1; NZ_LN832404.1.
PDB; 1Q16; X-ray; 1.90 A; A=1-1247.
PDB; 1R27; X-ray; 2.00 A; A/C=2-1247.
PDB; 1SIW; X-ray; 2.20 A; A=2-1247.
PDB; 1Y4Z; X-ray; 2.00 A; A=2-1247.
PDB; 1Y5I; X-ray; 1.90 A; A=2-1247.
PDB; 1Y5L; X-ray; 2.50 A; A=2-1247.
PDB; 1Y5N; X-ray; 2.50 A; A=2-1247.
PDB; 3EGW; X-ray; 1.90 A; A=2-1245.
PDB; 3IR5; X-ray; 2.30 A; A=1-1247.
PDB; 3IR6; X-ray; 2.80 A; A=1-1247.
PDB; 3IR7; X-ray; 2.50 A; A=1-1247.
PDBsum; 1Q16; -.
PDBsum; 1R27; -.
PDBsum; 1SIW; -.
PDBsum; 1Y4Z; -.
PDBsum; 1Y5I; -.
PDBsum; 1Y5L; -.
PDBsum; 1Y5N; -.
PDBsum; 3EGW; -.
PDBsum; 3IR5; -.
PDBsum; 3IR6; -.
PDBsum; 3IR7; -.
ProteinModelPortal; P09152; -.
SMR; P09152; -.
BioGrid; 4263271; 48.
DIP; DIP-10311N; -.
IntAct; P09152; 23.
MINT; MINT-1233973; -.
STRING; 316385.ECDH10B_1283; -.
DrugBank; DB04464; N-Formylmethionine.
TCDB; 5.A.3.1.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
PaxDb; P09152; -.
PRIDE; P09152; -.
EnsemblBacteria; AAC74308; AAC74308; b1224.
EnsemblBacteria; BAA36094; BAA36094; BAA36094.
GeneID; 945782; -.
KEGG; ecj:JW1215; -.
KEGG; eco:b1224; -.
PATRIC; fig|1411691.4.peg.1057; -.
EchoBASE; EB0632; -.
EcoGene; EG10638; narG.
eggNOG; ENOG4105CRU; Bacteria.
eggNOG; COG5013; LUCA.
HOGENOM; HOG000237341; -.
InParanoid; P09152; -.
KO; K00370; -.
PhylomeDB; P09152; -.
BioCyc; EcoCyc:NARG-MONOMER; -.
BioCyc; MetaCyc:NARG-MONOMER; -.
BRENDA; 1.7.5.1; 2026.
BRENDA; 1.7.99.4; 2026.
EvolutionaryTrace; P09152; -.
PRO; PR:P09152; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0031224; C:intrinsic component of membrane; IDA:EcoCyc.
GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IDA:EcoCyc.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0044799; C:NarGHI complex; IDA:EcoCyc.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
GO; GO:0009055; F:electron carrier activity; IDA:EcoCyc.
GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
GO; GO:0043546; F:molybdopterin cofactor binding; IDA:EcoCyc.
GO; GO:0008940; F:nitrate reductase activity; IDA:EcoCyc.
GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
GO; GO:0042126; P:nitrate metabolic process; IMP:EcoCyc.
InterPro; IPR009010; Asp_de-COase-like_dom_sf.
InterPro; IPR006657; MoPterin_dinucl-bd_dom.
InterPro; IPR006656; Mopterin_OxRdtase.
InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
InterPro; IPR006468; NarG.
InterPro; IPR028189; Nitr_red_alph_N.
Pfam; PF00384; Molybdopterin; 1.
Pfam; PF01568; Molydop_binding; 1.
Pfam; PF14710; Nitr_red_alph_N; 1.
SMART; SM00926; Molybdop_Fe4S4; 1.
SUPFAM; SSF50692; SSF50692; 1.
TIGRFAMs; TIGR01580; narG; 1.
PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
1: Evidence at protein level;
3D-structure; 4Fe-4S; Cell membrane; Complete proteome;
Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
Membrane; Metal-binding; Molybdenum; Nitrate assimilation;
Oxidoreductase; Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3053688}.
CHAIN 2 1247 Respiratory nitrate reductase 1 alpha
chain.
/FTId=PRO_0000063233.
DOMAIN 43 107 4Fe-4S Mo/W bis-MGD-type.
{ECO:0000255|PROSITE-ProRule:PRU01004}.
METAL 50 50 Iron-sulfur (4Fe-4S); via pros nitrogen.
METAL 54 54 Iron-sulfur (4Fe-4S).
METAL 58 58 Iron-sulfur (4Fe-4S).
METAL 93 93 Iron-sulfur (4Fe-4S).
METAL 223 223 Molybdenum.
MUTAGEN 50 50 H->S: Loss of activity.
{ECO:0000269|PubMed:9585550}.
CONFLICT 10 10 Y -> K (in Ref. 11; AA sequence).
{ECO:0000305}.
HELIX 3 6 {ECO:0000244|PDB:1Q16}.
HELIX 7 9 {ECO:0000244|PDB:1Q16}.
HELIX 11 13 {ECO:0000244|PDB:1Q16}.
STRAND 14 18 {ECO:0000244|PDB:1Q16}.
TURN 19 22 {ECO:0000244|PDB:1Q16}.
STRAND 23 26 {ECO:0000244|PDB:1Q16}.
HELIX 31 33 {ECO:0000244|PDB:1Q16}.
HELIX 34 40 {ECO:0000244|PDB:1Q16}.
STRAND 43 48 {ECO:0000244|PDB:1Q16}.
STRAND 52 55 {ECO:0000244|PDB:1Q16}.
STRAND 60 65 {ECO:0000244|PDB:1Q16}.
STRAND 68 74 {ECO:0000244|PDB:1Q16}.
HELIX 94 97 {ECO:0000244|PDB:1Q16}.
HELIX 98 102 {ECO:0000244|PDB:1Q16}.
STRAND 113 115 {ECO:0000244|PDB:1Q16}.
HELIX 116 126 {ECO:0000244|PDB:1Q16}.
HELIX 132 140 {ECO:0000244|PDB:1Q16}.
HELIX 143 150 {ECO:0000244|PDB:1Q16}.
TURN 151 154 {ECO:0000244|PDB:1Q16}.
STRAND 158 160 {ECO:0000244|PDB:1Q16}.
HELIX 163 180 {ECO:0000244|PDB:1Q16}.
HELIX 183 185 {ECO:0000244|PDB:1Q16}.
STRAND 186 189 {ECO:0000244|PDB:1Q16}.
HELIX 193 195 {ECO:0000244|PDB:1Q16}.
HELIX 197 210 {ECO:0000244|PDB:1Q16}.
STRAND 213 215 {ECO:0000244|PDB:1Q16}.
TURN 218 222 {ECO:0000244|PDB:1Q16}.
HELIX 227 232 {ECO:0000244|PDB:1Q16}.
HELIX 241 246 {ECO:0000244|PDB:1Q16}.
STRAND 248 254 {ECO:0000244|PDB:1Q16}.
HELIX 257 260 {ECO:0000244|PDB:1Q16}.
HELIX 262 264 {ECO:0000244|PDB:1Q16}.
HELIX 265 271 {ECO:0000244|PDB:1Q16}.
HELIX 272 274 {ECO:0000244|PDB:1Q16}.
STRAND 277 281 {ECO:0000244|PDB:1Q16}.
HELIX 287 291 {ECO:0000244|PDB:1Q16}.
STRAND 292 296 {ECO:0000244|PDB:1Q16}.
TURN 300 302 {ECO:0000244|PDB:1Y5N}.
HELIX 303 318 {ECO:0000244|PDB:1Q16}.
TURN 319 321 {ECO:0000244|PDB:1Q16}.
HELIX 325 334 {ECO:0000244|PDB:1Q16}.
STRAND 339 345 {ECO:0000244|PDB:1Q16}.
STRAND 347 355 {ECO:0000244|PDB:1Q16}.
HELIX 358 360 {ECO:0000244|PDB:1Q16}.
STRAND 361 363 {ECO:0000244|PDB:1Y5N}.
HELIX 364 366 {ECO:0000244|PDB:1Q16}.
HELIX 371 373 {ECO:0000244|PDB:1Q16}.
STRAND 377 379 {ECO:0000244|PDB:1Q16}.
HELIX 391 393 {ECO:0000244|PDB:1Q16}.
STRAND 395 397 {ECO:0000244|PDB:1Q16}.
STRAND 405 407 {ECO:0000244|PDB:1Q16}.
TURN 408 410 {ECO:0000244|PDB:1Q16}.
TURN 421 423 {ECO:0000244|PDB:1SIW}.
STRAND 425 433 {ECO:0000244|PDB:1Q16}.
STRAND 450 462 {ECO:0000244|PDB:1Q16}.
STRAND 468 473 {ECO:0000244|PDB:1Q16}.
HELIX 474 481 {ECO:0000244|PDB:1Q16}.
STRAND 493 496 {ECO:0000244|PDB:1Q16}.
HELIX 505 512 {ECO:0000244|PDB:1Q16}.
HELIX 516 533 {ECO:0000244|PDB:1Q16}.
STRAND 537 541 {ECO:0000244|PDB:1Q16}.
HELIX 543 546 {ECO:0000244|PDB:1Q16}.
HELIX 551 564 {ECO:0000244|PDB:1Q16}.
STRAND 574 577 {ECO:0000244|PDB:1Q16}.
HELIX 587 594 {ECO:0000244|PDB:1Q16}.
TURN 595 599 {ECO:0000244|PDB:1Q16}.
STRAND 604 606 {ECO:0000244|PDB:1Q16}.
HELIX 608 615 {ECO:0000244|PDB:1Q16}.
HELIX 618 621 {ECO:0000244|PDB:1Q16}.
HELIX 627 629 {ECO:0000244|PDB:1Q16}.
HELIX 636 638 {ECO:0000244|PDB:1Q16}.
HELIX 643 652 {ECO:0000244|PDB:1Q16}.
STRAND 662 664 {ECO:0000244|PDB:1Q16}.
TURN 666 668 {ECO:0000244|PDB:3EGW}.
HELIX 669 675 {ECO:0000244|PDB:1Q16}.
HELIX 680 690 {ECO:0000244|PDB:1Q16}.
STRAND 691 693 {ECO:0000244|PDB:1Q16}.
HELIX 696 698 {ECO:0000244|PDB:1Q16}.
STRAND 702 706 {ECO:0000244|PDB:1Q16}.
STRAND 709 714 {ECO:0000244|PDB:1Q16}.
TURN 717 721 {ECO:0000244|PDB:1Q16}.
STRAND 722 724 {ECO:0000244|PDB:1R27}.
HELIX 725 731 {ECO:0000244|PDB:1Q16}.
TURN 744 748 {ECO:0000244|PDB:1Q16}.
STRAND 753 755 {ECO:0000244|PDB:1Q16}.
STRAND 767 775 {ECO:0000244|PDB:1Q16}.
HELIX 778 781 {ECO:0000244|PDB:1Q16}.
STRAND 784 789 {ECO:0000244|PDB:1Q16}.
STRAND 797 799 {ECO:0000244|PDB:1Q16}.
STRAND 805 810 {ECO:0000244|PDB:1Q16}.
STRAND 813 815 {ECO:0000244|PDB:1Y5L}.
HELIX 823 837 {ECO:0000244|PDB:1Q16}.
TURN 838 841 {ECO:0000244|PDB:1Q16}.
STRAND 844 851 {ECO:0000244|PDB:1Q16}.
HELIX 858 860 {ECO:0000244|PDB:1Q16}.
STRAND 864 866 {ECO:0000244|PDB:1Q16}.
HELIX 870 872 {ECO:0000244|PDB:1Q16}.
TURN 879 881 {ECO:0000244|PDB:1Q16}.
STRAND 885 892 {ECO:0000244|PDB:1Q16}.
HELIX 893 895 {ECO:0000244|PDB:1Q16}.
HELIX 896 900 {ECO:0000244|PDB:1Q16}.
HELIX 906 909 {ECO:0000244|PDB:1Q16}.
STRAND 912 914 {ECO:0000244|PDB:1Q16}.
STRAND 917 919 {ECO:0000244|PDB:1Q16}.
HELIX 922 932 {ECO:0000244|PDB:1Q16}.
STRAND 936 938 {ECO:0000244|PDB:1Y5L}.
TURN 939 942 {ECO:0000244|PDB:1Q16}.
STRAND 943 945 {ECO:0000244|PDB:1Q16}.
HELIX 949 959 {ECO:0000244|PDB:1Q16}.
TURN 961 963 {ECO:0000244|PDB:1Q16}.
HELIX 965 979 {ECO:0000244|PDB:1Q16}.
HELIX 984 986 {ECO:0000244|PDB:1Q16}.
HELIX 988 990 {ECO:0000244|PDB:1Q16}.
HELIX 997 1002 {ECO:0000244|PDB:1Q16}.
STRAND 1013 1015 {ECO:0000244|PDB:1Q16}.
STRAND 1019 1021 {ECO:0000244|PDB:1Q16}.
HELIX 1027 1032 {ECO:0000244|PDB:1Q16}.
STRAND 1041 1043 {ECO:0000244|PDB:1Q16}.
HELIX 1050 1054 {ECO:0000244|PDB:1Q16}.
TURN 1072 1078 {ECO:0000244|PDB:1Q16}.
STRAND 1085 1090 {ECO:0000244|PDB:1Q16}.
STRAND 1095 1098 {ECO:0000244|PDB:1Q16}.
TURN 1102 1104 {ECO:0000244|PDB:1Q16}.
HELIX 1106 1111 {ECO:0000244|PDB:1Q16}.
STRAND 1117 1121 {ECO:0000244|PDB:1Q16}.
HELIX 1122 1128 {ECO:0000244|PDB:1Q16}.
STRAND 1135 1140 {ECO:0000244|PDB:1Q16}.
STRAND 1143 1152 {ECO:0000244|PDB:1Q16}.
STRAND 1159 1161 {ECO:0000244|PDB:1Q16}.
STRAND 1168 1171 {ECO:0000244|PDB:1Q16}.
TURN 1176 1178 {ECO:0000244|PDB:1Q16}.
STRAND 1179 1181 {ECO:0000244|PDB:1Q16}.
HELIX 1185 1187 {ECO:0000244|PDB:1Q16}.
HELIX 1195 1197 {ECO:0000244|PDB:1Q16}.
STRAND 1205 1207 {ECO:0000244|PDB:1Q16}.
TURN 1209 1211 {ECO:0000244|PDB:1Q16}.
STRAND 1222 1227 {ECO:0000244|PDB:1Q16}.
STRAND 1229 1231 {ECO:0000244|PDB:1Q16}.
STRAND 1234 1238 {ECO:0000244|PDB:1Q16}.
SEQUENCE 1247 AA; 140489 MW; 640ABAD5FF01DF25 CRC64;
MSKFLDRFRY FKQKGETFAD GHGQLLNTNR DWEDGYRQRW QHDKIVRSTH GVNCTGSCSW
KIYVKNGLVT WETQQTDYPR TRPDLPNHEP RGCPRGASYS WYLYSANRLK YPMMRKRLMK
MWREAKALHS DPVEAWASII EDADKAKSFK QARGRGGFVR SSWQEVNELI AASNVYTIKN
YGPDRVAGFS PIPAMSMVSY ASGARYLSLI GGTCLSFYDW YCDLPPASPQ TWGEQTDVPE
SADWYNSSYI IAWGSNVPQT RTPDAHFFTE VRYKGTKTVA VTPDYAEIAK LCDLWLAPKQ
GTDAAMALAM GHVMLREFHL DNPSQYFTDY VRRYTDMPML VMLEERDGYY AAGRMLRAAD
LVDALGQENN PEWKTVAFNT NGEMVAPNGS IGFRWGEKGK WNLEQRDGKT GEETELQLSL
LGSQDEIAEV GFPYFGGDGT EHFNKVELEN VLLHKLPVKR LQLADGSTAL VTTVYDLTLA
NYGLERGLND VNCATSYDDV KAYTPAWAEQ ITGVSRSQII RIAREFADNA DKTHGRSMII
VGAGLNHWYH LDMNYRGLIN MLIFCGCVGQ SGGGWAHYVG QEKLRPQTGW QPLAFALDWQ
RPARHMNSTS YFYNHSSQWR YETVTAEELL SPMADKSRYT GHLIDFNVRA ERMGWLPSAP
QLGTNPLTIA GEAEKAGMNP VDYTVKSLKE GSIRFAAEQP ENGKNHPRNL FIWRSNLLGS
SGKGHEFMLK YLLGTEHGIQ GKDLGQQGGV KPEEVDWQDN GLEGKLDLVV TLDFRLSSTC
LYSDIILPTA TWYEKDDMNT SDMHPFIHPL SAAVDPAWEA KSDWEIYKAI AKKFSEVCVG
HLGKETDIVT LPIQHDSAAE LAQPLDVKDW KKGECDLIPG KTAPHIMVVE RDYPATYERF
TSIGPLMEKI GNGGKGIAWN TQSEMDLLRK LNYTKAEGPA KGQPMLNTAI DAAEMILTLA
PETNGQVAVK AWAALSEFTG RDHTHLALNK EDEKIRFRDI QAQPRKIISS PTWSGLEDEH
VSYNAGYTNV HELIPWRTLS GRQQLYQDHQ WMRDFGESLL VYRPPIDTRS VKEVIGQKSN
GNQEKALNFL TPHQKWGIHS TYSDNLLMLT LGRGGPVVWL SEADAKDLGI ADNDWIEVFN
SNGALTARAV VSQRVPAGMT MMYHAQERIV NLPGSEITQQ RGGIHNSVTR ITPKPTHMIG
GYAHLAYGFN YYGTVGSNRD EFVVVRKMKN IDWLDGEGND QVQESVK


Related products :

Catalog number Product name Quantity
AS08313 NarG | catalytic alfa subunit of nitrate reductase 1
AS08313 NarG | catalytic alfa subunit of nitrate reductase 1
E0441h ELISA kit Anterior pituitary glycoprotein hormones common subunit alpha,CGA,CG-alpha,Choriogonadotropin alpha chain,Chorionic gonadotrophin subunit alpha,Follicle-stimulating hormone alpha chain,Foll 96T
U0441h CLIA Anterior pituitary glycoprotein hormones common subunit alpha,CGA,CG-alpha,Choriogonadotropin alpha chain,Chorionic gonadotrophin subunit alpha,Follicle-stimulating hormone alpha chain,Follitropi 96T
E0441h ELISA Anterior pituitary glycoprotein hormones common subunit alpha,CGA,CG-alpha,Choriogonadotropin alpha chain,Chorionic gonadotrophin subunit alpha,Follicle-stimulating hormone alpha chain,Follitrop 96T
18-003-43025 GA-binding protein alpha chain - GABP-subunit alpha; Transcription factor E4TF1-60; Nuclear respiratory factor 2 subunit alpha Polyclonal 0.1 mg Protein A
E1345m ELISA Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
U1345m CLIA Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
E1345m ELISA kit Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
20-272-191784 hCG alpha - Mouse monoclonal [CH5] to hCG alpha; Anterior pituitary glycoprotein hormones common subunit alpha; Follitropin alpha chain; Follicle-stimulating hormone alpha chain; FSH-alpha; Lutropin a 0.5 mg
E2211h ELISA Homo sapiens,Human,LAMA,LAMA1,Laminin A chain,Laminin subunit alpha-1,Laminin-1 subunit alpha,Laminin-3 subunit alpha,S-LAM alpha,S-laminin subunit alpha 96T
U2211h CLIA kit Homo sapiens,Human,LAMA,LAMA1,Laminin A chain,Laminin subunit alpha-1,Laminin-1 subunit alpha,Laminin-3 subunit alpha,S-LAM alpha,S-laminin subunit alpha 96T
E2211h ELISA kit Homo sapiens,Human,LAMA,LAMA1,Laminin A chain,Laminin subunit alpha-1,Laminin-1 subunit alpha,Laminin-3 subunit alpha,S-LAM alpha,S-laminin subunit alpha 96T
U2211h CLIA Homo sapiens,Human,LAMA,LAMA1,Laminin A chain,Laminin subunit alpha-1,Laminin-1 subunit alpha,Laminin-3 subunit alpha,S-LAM alpha,S-laminin subunit alpha 96T
EIAAB31829 3-oxo-5-alpha-steroid 4-dehydrogenase 3,Homo sapiens,Human,Probable polyprenol reductase,S5AR 3,SR type 3,SRD5A2L,SRD5A3,Steroid 5-alpha-reductase 2-like,Steroid 5-alpha-reductase 3
EIAAB31830 3-oxo-5-alpha-steroid 4-dehydrogenase 3,Mouse,Mus musculus,Probable polyprenol reductase,S5AR 3,SR type 3,Srd5a2l,Srd5a3,Steroid 5-alpha-reductase 2-like,Steroid 5-alpha-reductase 3
E2211h Homo sapiens,Human,LAMA,LAMA1,Laminin A chain,Laminin subunit alpha-1,Laminin-1 subunit alpha,Laminin-3 subunit alpha,S-LAM alpha,S-laminin subunit alpha
U1345h CLIA E170,Epiligrin 170 kDa subunit,Epiligrin subunit alpha,Homo sapiens,Human,Kalinin subunit alpha,LAMA3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alp 96T
E1345h ELISA E170,Epiligrin 170 kDa subunit,Epiligrin subunit alpha,Homo sapiens,Human,Kalinin subunit alpha,LAMA3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit al 96T
E1345h ELISA kit E170,Epiligrin 170 kDa subunit,Epiligrin subunit alpha,Homo sapiens,Human,Kalinin subunit alpha,LAMA3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subun 96T
AS8 310 Nitrate Reductase _ NR 0.2 mg
AS8 310 Nitrate Reductase _ NR 0.2 mg
E0441r ELISA Anterior pituitary glycoprotein hormones common subunit alpha,Cga,Cga1,Follicle-stimulating hormone alpha chain,Follitropin alpha chain,FSH-alpha,Glycoprotein hormones alpha chain,LSH-alpha,Lute 96T
U0441r CLIA Anterior pituitary glycoprotein hormones common subunit alpha,Cga,Cga1,Follicle-stimulating hormone alpha chain,Follitropin alpha chain,FSH-alpha,Glycoprotein hormones alpha chain,LSH-alpha,Lutei 96T
15-288-21224 Propionyl-CoA carboxylase alpha chain. mitochondrial - EC 6.4.1.3; PCCase subunit alpha; Propanoyl-CoA carbon dioxide ligase subunit alpha Polyclonal 0.1 mg


 

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