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

Ornithine decarboxylase 1 (ODC) (EC 4.1.1.17)

 DCOR1_DROME             Reviewed;         394 AA.
P40807; Q9V352;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
12-APR-2005, sequence version 3.
18-JUL-2018, entry version 140.
RecName: Full=Ornithine decarboxylase 1;
Short=ODC;
EC=4.1.1.17;
Name=Odc1; ORFNames=CG8721;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND DEVELOPMENTAL STAGE.
STRAIN=Canton-S;
PubMed=8329117; DOI=10.1089/dna.1993.12.499;
Rom E., Kahana C.;
"Isolation and characterization of the Drosophila ornithine
decarboxylase locus: evidence for the presence of two transcribed ODC
genes in the Drosophila genome.";
DNA Cell Biol. 12:499-508(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Testis;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
-!- FUNCTION: Catalyzes the first and rate-limiting step of polyamine
biosynthesis that converts ornithine into putrescine, which is the
precursor for the polyamines, spermidine and spermine. Polyamines
are essential for cell proliferation and are implicated in
cellular processes, ranging from DNA replication to apoptosis.
{ECO:0000250|UniProtKB:P11926}.
-!- CATALYTIC ACTIVITY: L-ornithine = putrescine + CO(2).
{ECO:0000250|UniProtKB:P11926}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250|UniProtKB:P11926};
-!- ENZYME REGULATION: Inhibited by antizyme (AZ) in response to
polyamine levels. AZ inhibits the assembly of the functional
homodimer by binding to ODC monomers and targeting them for
ubiquitin-independent proteolytic destruction by the 26S
proteasome. {ECO:0000250|UniProtKB:P11926}.
-!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis
via L-ornithine pathway; putrescine from L-ornithine: step 1/1.
-!- SUBUNIT: Homodimer. Only the dimer is catalytically active, as the
active sites are constructed of residues from both monomers.
{ECO:0000250|UniProtKB:P11926}.
-!- DEVELOPMENTAL STAGE: Expressed in adults.
{ECO:0000269|PubMed:8329117}.
-!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X66601; CAA47167.1; -; Genomic_DNA.
EMBL; X66599; CAA47165.1; -; mRNA.
EMBL; AE013599; AAF59150.1; -; Genomic_DNA.
EMBL; AY094710; AAM11063.1; -; mRNA.
RefSeq; NP_477052.2; NM_057704.5.
UniGene; Dm.3665; -.
ProteinModelPortal; P40807; -.
SMR; P40807; -.
BioGrid; 61627; 1.
IntAct; P40807; 1.
STRING; 7227.FBpp0087939; -.
PaxDb; P40807; -.
PRIDE; P40807; -.
EnsemblMetazoa; FBtr0088863; FBpp0087939; FBgn0013307.
GeneID; 35766; -.
KEGG; dme:Dmel_CG8721; -.
CTD; 4953; -.
FlyBase; FBgn0013307; Odc1.
eggNOG; KOG0622; Eukaryota.
eggNOG; COG0019; LUCA.
GeneTree; ENSGT00390000011560; -.
InParanoid; P40807; -.
KO; K01581; -.
OMA; VVGYICE; -.
OrthoDB; EOG091G0AJV; -.
PhylomeDB; P40807; -.
Reactome; R-DME-351143; Agmatine biosynthesis.
Reactome; R-DME-351202; Metabolism of polyamines.
UniPathway; UPA00535; UER00288.
GenomeRNAi; 35766; -.
PRO; PR:P40807; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0013307; -.
Genevisible; P40807; DM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0004586; F:ornithine decarboxylase activity; ISS:FlyBase.
GO; GO:0033387; P:putrescine biosynthetic process from ornithine; IBA:GO_Central.
Gene3D; 2.40.37.10; -; 2.
Gene3D; 3.20.20.10; -; 1.
InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
InterPro; IPR022643; De-COase2_C.
InterPro; IPR022657; De-COase2_CS.
InterPro; IPR022644; De-COase2_N.
InterPro; IPR022653; De-COase2_pyr-phos_BS.
InterPro; IPR000183; Orn/DAP/Arg_de-COase.
InterPro; IPR002433; Orn_de-COase.
InterPro; IPR029066; PLP-binding_barrel.
PANTHER; PTHR11482; PTHR11482; 1.
Pfam; PF02784; Orn_Arg_deC_N; 1.
Pfam; PF00278; Orn_DAP_Arg_deC; 1.
PRINTS; PR01179; ODADCRBXLASE.
PRINTS; PR01182; ORNDCRBXLASE.
SUPFAM; SSF50621; SSF50621; 1.
SUPFAM; SSF51419; SSF51419; 1.
PROSITE; PS00878; ODR_DC_2_1; 1.
PROSITE; PS00879; ODR_DC_2_2; 1.
2: Evidence at transcript level;
Complete proteome; Decarboxylase; Lyase; Polyamine biosynthesis;
Pyridoxal phosphate; Reference proteome.
CHAIN 1 394 Ornithine decarboxylase 1.
/FTId=PRO_0000149899.
REGION 265 268 Pyridoxal phosphate binding.
{ECO:0000250|UniProtKB:P11926}.
REGION 314 315 Substrate binding.
{ECO:0000250|UniProtKB:P07805}.
ACT_SITE 343 343 Proton donor; shared with dimeric
partner. {ECO:0000250|UniProtKB:P11926}.
BINDING 194 194 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:P11926}.
BINDING 231 231 Pyridoxal phosphate; via amino nitrogen.
{ECO:0000250|UniProtKB:P11926}.
BINDING 344 344 Substrate; shared with dimeric partner.
{ECO:0000250|UniProtKB:P07805}.
BINDING 372 372 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:P11926}.
SITE 191 191 Stacks against the aromatic ring of
pyridoxal phosphate and stabilizes
reaction intermediates.
{ECO:0000250|UniProtKB:P00860}.
MOD_RES 62 62 N6-(pyridoxal phosphate)lysine.
{ECO:0000250|UniProtKB:P11926}.
CONFLICT 44 45 KL -> NV (in Ref. 1; CAA47167/CAA47165).
{ECO:0000305}.
CONFLICT 242 242 K -> Q (in Ref. 1; CAA47165).
{ECO:0000305}.
CONFLICT 325 325 L -> Q (in Ref. 1; CAA47165).
{ECO:0000305}.
CONFLICT 348 348 K -> Q (in Ref. 1; CAA47165).
{ECO:0000305}.
SEQUENCE 394 AA; 44195 MW; 5D2F348D1467E39B CRC64;
MAAATPEIQF YERELNIRRV IEECDLQRLD QALNICDLSS VERKLRLWQK LLPRIKPFYA
VKCNDDPMVV RLLAQLGAGF DCASKNEVKL VLGFDVSPER IIFANPCRPV SHLEYAKEHQ
VSNGTVDNEF EVYKLHTHYP NSNLIVRFKS EAKEAQCPLG DKFGCDADVD AAALMLLAKS
LELKVTGTSF HVGSGCSELQ AYDRAIKKAK NLFKFGALLG YDMDFLDIGG GFPGSDDVKF
EKIAESVNTS VQRHFPDERV HIIAEPGRFF VAAACTLVCK IHAKREIRNE AGKLDTVMYY
LNDGVYGSFN CILYDHQVVI AEHYLDNAES LPHLKSLIWG PSCDALDKIS EDLHLPNLNR
GDLLGFRNMG AYTMPIASAF NGFEVPKTLY FQAI


Related products :

Catalog number Product name Quantity
MA1073 Monoclonal Anti-Ornithine Decarboxylase (ODC), Clone number: ODC-22, Ig type: mouse IgG2b, Immunogen: Recombinant mouse ornithine decarboxylase., Specificity: Human. No cross reactivity with other pro 100μg/vial
LF-MA50073 anti-Ornithine Decarboxylase (ODC-22), Mouse monoclonal to Ornithine Decarboxylase, Isotype IgG2b, Host Mouse 200 ul
20-272-191151 Ornithine Decarboxylase - Mouse monoclonal [3F293] to Ornithine Decarboxylase Monoclonal 0.05 ml
B513I Ornithine Decarboxylase Broth USE For detection of the ability of microorganisms to decarboxylate ornithine. Qty per Litre of Medium: 9
B513I Ornithine Decarboxylase Broth USE : For detection of the ability of microorganisms to decarboxylate ornithine. 5x500gm
MCA3310Z MOUSE ANTI HUMAN ORNITHINE DECARBOXYLASE Azide Free, Product Type Monoclonal Antibody, Specificity ORNITHINE DECARBOXYLASE 1, Target Species Human, Host Mouse, Format Azide Free, Isotypes IgG2b, 0.1 mg
B233 MIO Medium (Motility Indole Ornithine Medium) USE : For the identification of Enterobacteriaceae on the basis of motility,indole production and ornithine decarboxylase activity. 5x500gm
B233 MIO Medium (Motility Indole Ornithine Medium) USE For the identification of Enterobacteriaceae on the basis of motility,indole production and ornithine decarboxylase activity. Qty per Litre of Medium: 31
Y105298 Ornithine Decarboxylase 50ug
Y103692 Ornithine Decarboxylase (ODC) AB1 100ug
78009 IgG,ORNITHINE DECARBOXYLASE 1 ml
TM 186 MIO MEDIUM (MOTILITY INDOLE ORNITHINE MEDIUM) (for identification of Enterobacteriaceae on the basis of motility, indole production and ornithine decarboxylase activity.) 500 gm
GTX15167 Ornithine Decarboxylase (ODC1) 50 µl
E02O0013 Rat Ornithine Decarboxylase Elisa Kit (ODC) 96 Tests/kit
E-EL-R0694 Rat ODC (Ornithine Decarboxylase) ELISA Kit 96T
EH1503 Ornithine decarboxylase Elisa Kit 96T
CG81 Ornithine decarboxylase ODC1 lmg
GTX23141 Ornithine Decarboxylase (ODC1) 500 µl
EUD2501 Ornithine Decarboxylase (ODC1) 50 µl
REN-181 Recombinant Human Ornithine Decarboxylase 1 2
MB-O1305 Ornithine Decarboxylase Broth 500g
Y103692 Ornithine Decarboxylase (ODC) AB1 Antibody 100ug
CG81 Ornithine decarboxylase ODC1 500
DL-ODC-Hu Human Ornithine Decarboxylase (ODC) ELISA Kit 96T
GWB-A17693 Ornithine Decarboxylase, Antibody


 

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