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

Putative acyl-[acyl-carrier-protein] desaturase DesA2 (Putative acyl-ACP desaturase DesA2) (EC 1.14.19.-)

 DESA2_MYCTU             Reviewed;         275 AA.
P9WNZ5; L0T8L4; O53442; Q7D8V3;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
28-FEB-2018, entry version 24.
RecName: Full=Putative acyl-[acyl-carrier-protein] desaturase DesA2 {ECO:0000303|PubMed:14559907, ECO:0000303|PubMed:15929999};
Short=Putative acyl-ACP desaturase DesA2 {ECO:0000303|PubMed:14559907};
EC=1.14.19.- {ECO:0000305|PubMed:14559907};
Name=desA2 {ECO:0000303|PubMed:14559907}; OrderedLocusNames=Rv1094;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
PUTATIVE FUNCTION.
STRAIN=ATCC 25618 / H37Rv;
PubMed=14559907; DOI=10.1074/jbc.M311209200;
Phetsuksiri B., Jackson M., Scherman H., McNeil M., Besra G.S.,
Baulard A.R., Slayden R.A., DeBarber A.E., Barry C.E. III, Baird M.S.,
Crick D.C., Brennan P.J.;
"Unique mechanism of action of the thiourea drug isoxyl on
Mycobacterium tuberculosis.";
J. Biol. Chem. 278:53123-53130(2003).
[3]
IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
PubMed=19099550; DOI=10.1186/1752-0509-2-109;
Raman K., Yeturu K., Chandra N.;
"targetTB: a target identification pipeline for Mycobacterium
tuberculosis through an interactome, reactome and genome-scale
structural analysis.";
BMC Syst. Biol. 2:109-109(2008).
[4]
PUPYLATION AT LYS-145, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=ATCC 25618 / H37Rv;
PubMed=20066036; DOI=10.1371/journal.pone.0008589;
Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
Gygi S.P., Darwin K.H.;
"Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium
tuberculosis.";
PLoS ONE 5:E8589-E8589(2010).
[5]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[6]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MANGANESE, AND
SUBUNIT.
STRAIN=H37Rv;
PubMed=15929999; DOI=10.1110/ps.041288005;
Dyer D.H., Lyle K.S., Rayment I., Fox B.G.;
"X-ray structure of putative acyl-ACP desaturase DesA2 from
Mycobacterium tuberculosis H37Rv.";
Protein Sci. 14:1508-1517(2005).
-!- FUNCTION: May be a desaturase involved in mycobacterial fatty acid
biosynthesis. {ECO:0000305|PubMed:14559907}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000250|UniProtKB:P22337};
Note=Binds 2 Fe(2+) ions per subunit.
{ECO:0000250|UniProtKB:P22337};
-!- PATHWAY: Lipid metabolism; fatty acid metabolism.
{ECO:0000305|PubMed:14559907}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15929999}.
-!- MISCELLANEOUS: Was identified as a high-confidence drug target.
{ECO:0000305|PubMed:19099550}.
-!- SIMILARITY: Belongs to the fatty acid desaturase type 2 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; AL123456; CCP43847.1; -; Genomic_DNA.
PIR; D70896; D70896.
RefSeq; NP_215610.1; NC_000962.3.
RefSeq; WP_003405801.1; NZ_KK339370.1.
PDB; 1ZA0; X-ray; 2.00 A; A=1-275.
PDBsum; 1ZA0; -.
ProteinModelPortal; P9WNZ5; -.
SMR; P9WNZ5; -.
STRING; 83332.Rv1094; -.
iPTMnet; P9WNZ5; -.
PaxDb; P9WNZ5; -.
EnsemblBacteria; CCP43847; CCP43847; Rv1094.
GeneID; 885339; -.
KEGG; mtu:Rv1094; -.
TubercuList; Rv1094; -.
eggNOG; ENOG4106SUI; Bacteria.
eggNOG; ENOG410YM8X; LUCA.
KO; K03922; -.
OMA; GYRADTY; -.
PhylomeDB; P9WNZ5; -.
UniPathway; UPA00199; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0005829; C:cytosol; IDA:MTBBASE.
GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IDA:MTBBASE.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0040007; P:growth; IMP:MTBBASE.
Gene3D; 1.10.620.20; -; 1.
InterPro; IPR005067; Fatty_acid_desaturase-2.
InterPro; IPR009078; Ferritin-like_SF.
InterPro; IPR012348; RNR-like.
PANTHER; PTHR31155; PTHR31155; 1.
Pfam; PF03405; FA_desaturase_2; 1.
PIRSF; PIRSF000346; Dlt9_acylACP_des; 1.
SUPFAM; SSF47240; SSF47240; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Fatty acid biosynthesis;
Fatty acid metabolism; Iron; Isopeptide bond; Lipid biosynthesis;
Lipid metabolism; Metal-binding; Oxidoreductase; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:21969609}.
CHAIN 2 275 Putative acyl-[acyl-carrier-protein]
desaturase DesA2.
/FTId=PRO_0000392676.
METAL 107 107 Iron 1. {ECO:0000250|UniProtKB:P22337,
ECO:0000305|PubMed:15929999}.
METAL 107 107 Iron 2. {ECO:0000250|UniProtKB:P22337,
ECO:0000305|PubMed:15929999}.
METAL 110 110 Iron 1; via pros nitrogen.
{ECO:0000250|UniProtKB:P22337}.
METAL 159 159 Iron 2. {ECO:0000250|UniProtKB:P22337,
ECO:0000305|PubMed:15929999}.
METAL 189 189 Iron 1. {ECO:0000250|UniProtKB:P22337,
ECO:0000305|PubMed:15929999}.
METAL 189 189 Iron 2. {ECO:0000250|UniProtKB:P22337,
ECO:0000305|PubMed:15929999}.
METAL 192 192 Iron 2; via pros nitrogen.
{ECO:0000250|UniProtKB:P22337,
ECO:0000305|PubMed:15929999}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:21969609}.
CROSSLNK 145 145 Isoglutamyl lysine isopeptide (Lys-Gln)
(interchain with Q-Cter in protein Pup).
{ECO:0000269|PubMed:20066036}.
HELIX 9 27 {ECO:0000244|PDB:1ZA0}.
HELIX 34 37 {ECO:0000244|PDB:1ZA0}.
HELIX 40 42 {ECO:0000244|PDB:1ZA0}.
HELIX 47 49 {ECO:0000244|PDB:1ZA0}.
HELIX 56 58 {ECO:0000244|PDB:1ZA0}.
HELIX 63 77 {ECO:0000244|PDB:1ZA0}.
HELIX 95 120 {ECO:0000244|PDB:1ZA0}.
TURN 126 130 {ECO:0000244|PDB:1ZA0}.
HELIX 148 172 {ECO:0000244|PDB:1ZA0}.
HELIX 176 206 {ECO:0000244|PDB:1ZA0}.
HELIX 208 221 {ECO:0000244|PDB:1ZA0}.
TURN 225 228 {ECO:0000244|PDB:1ZA0}.
HELIX 233 241 {ECO:0000244|PDB:1ZA0}.
STRAND 244 246 {ECO:0000244|PDB:1ZA0}.
HELIX 247 260 {ECO:0000244|PDB:1ZA0}.
HELIX 267 272 {ECO:0000244|PDB:1ZA0}.
SEQUENCE 275 AA; 31359 MW; 448D136940150E99 CRC64;
MAQKPVADAL TLELEPVVEA NMTRHLDTED IWFAHDYVPF DQGENFAFLG GRDWDPSQST
LPRTITDACE ILLILKDNLA GHHRELVEHF ILEDWWGRWL GRWTAEEHLH AIALREYLVV
TREVDPVANE DVRVQHVMKG YRAEKYTQVE TLVYMAFYER CGAVFCRNLA AQIEEPILAG
LIDRIARDEV RHEEFFANLV THCLDYTRDE TIAAIAARAA DLDVLGADIE AYRDKLQNVA
DAGIFGKPQL RQLISDRITA WGLAGEPSLK QFVTG


Related products :

Catalog number Product name Quantity
18-003-42290 Acyl-CoA desaturase - EC 1.14.19.1; Stearoyl-CoA desaturase; Fatty acid desaturase; Delta(9)-desaturase Polyclonal 0.1 mg Protein A
EIAAB37528 ACOD4,Acyl-CoA-desaturase 4,Homo sapiens,HSCD5,Human,SCD4,SCD5,Stearoyl-CoA 9-desaturase,Stearoyl-CoA desaturase 5
EIAAB37529 Acyl-CoA-desaturase 4,Bos taurus,Bovine,SCD5,Stearoyl-CoA 9-desaturase,Stearoyl-CoA desaturase 5
25-764 FADS1 is a member of the fatty acid desaturase (FADS) family. Desaturase enzymes regulate unsaturation of fatty acids through the introduction of double bonds between defined carbons of the fatty acyl 0.05 mg
29-745 FADS1 is a member of the fatty acid desaturase (FADS) family. Desaturase enzymes regulate unsaturation of fatty acids through the introduction of double bonds between defined carbons of the fatty acyl 0.1 mg
CSB-EL020802PI Pig Acyl-CoA desaturase(SCD) ELISA kit SpeciesPig 96T
CSB-EL020802BO Bovine Acyl-CoA desaturase(SCD) ELISA kit 96T
CSB-EL020802HU Human Acyl-CoA desaturase(SCD) ELISA kit 96T
CSB-EL020802GO Goat Acyl-CoA desaturase(SCD) ELISA kit 96T
CSB-EL020802BO Bovine Acyl-CoA desaturase(SCD) ELISA kit SpeciesBovine 96T
ARP32797_T200 Anti-Acyl-CoA Desaturase (SCD) Species_Reactivity: Human
CSB-EL020802GO Goat Acyl-CoA desaturase(SCD) ELISA kit SpeciesGoat 96T
CSB-EL020802HU Human Acyl-CoA desaturase(SCD) ELISA kit SpeciesHuman 96T
CSB-EL020802SH Sheep Acyl-CoA desaturase(SCD) ELISA kit SpeciesSheep 96T
AS13 2668 rabbit polyclonal Plastid acyl-ACP desaturase 50
ACOD_BOVIN ELISA Kit FOR Acyl-CoA desaturase; organism: Bovine; gene name: SCD 96T
CSB-E17579r Rat Acyl-CoA desaturase 1 (Scd1_Scd) ELISA kit, Species Rat, Sample Type serum, plasma 96T
26-896 Short_branched chain acyl-CoA dehydrogenase (ACADSB) is a member of the acyl-CoA dehydrogenase family of enzymes that catalyze the dehydrogenation of acyl-CoA derivatives in the metabolism of fatty ac 0.05 mg
EIAAB14290 [Acyl-carrier-protein] malonyltransferase,Homo sapiens,Human,Malonyl-CoA-acyl carrier protein transacylase, mitochondrial,MCAT,MCT,Mitochondrial malonyltransferase,MT
EIAAB14289 [Acyl-carrier-protein] malonyltransferase,Malonyl-CoA-acyl carrier protein transacylase, mitochondrial,Mcat,MCT,Mitochondrial malonyltransferase,Mouse,Mt,Mus musculus
25-757 Acyl-CoA thioesterases, such as ACOT2, are a group of enzymes that hydrolyze CoA esters, such as acyl-CoAs, bile CoAs, and CoA esters of prostaglandins, to the corresponding free acid and CoA.Acyl-CoA 0.05 mg
orb70386 Acyl Carrier Protein (65-74) peptide This is Acyl Carrier Protein (65-74) peptide. For research use only. 1 mg
orb70387 Acyl Carrier Protein (65-74) peptide This is Acyl Carrier Protein (65-74) peptide. For research use only. 1 mg
26-455 ACBD4 is a member of the acyl-coenzyme A binding domain containing protein family. All family members contain the conserved acyl-Coenzyme A binding domain, which binds acyl-CoA thiol esters. They are 0.05 mg
E1426h Human ELISA Kit FOR Putative acyl-coenzyme A thioesterase 6 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