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

Serine O-succinyltransferase (SST) (EC 2.3.1.-)

 A0A0J9WX68_XANOP        Unreviewed;       399 AA.
A0A0J9WX68;
14-OCT-2015, integrated into UniProtKB/TrEMBL.
14-OCT-2015, sequence version 1.
22-NOV-2017, entry version 23.
RecName: Full=Serine O-succinyltransferase {ECO:0000256|HAMAP-Rule:MF_00296};
Short=SST {ECO:0000256|HAMAP-Rule:MF_00296};
EC=2.3.1.- {ECO:0000256|HAMAP-Rule:MF_00296};
Name=metX {ECO:0000313|EMBL:ACD59247.1};
OrderedLocusNames=PXO_01100 {ECO:0000313|EMBL:ACD59247.1},
PXO_06257 {ECO:0000313|EMBL:ACD59439.1};
Xanthomonas oryzae pv. oryzae (strain PXO99A).
Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
Xanthomonadaceae; Xanthomonas.
NCBI_TaxID=360094 {ECO:0000313|EMBL:ACD59247.1, ECO:0000313|Proteomes:UP000001740};
[1] {ECO:0000313|EMBL:ACD59247.1, ECO:0000313|Proteomes:UP000001740}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PXO99A {ECO:0000313|EMBL:ACD59247.1,
ECO:0000313|Proteomes:UP000001740};
PubMed=18452608; DOI=10.1186/1471-2164-9-204;
Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M.,
Rabinowicz P.D., Tsuge S., Furutani A., Ochiai H., Delcher A.L.,
Kelley D., Madupu R., Puiu D., Radune D., Shumway M., Trapnell C.,
Aparna G., Jha G., Pandey A., Patil P.B., Ishihara H., Meyer D.F.,
Szurek B., Verdier V., Koebnik R., Dow J.M., Ryan R.P., Hirata H.,
Tsuyumu S., Won Lee S., Seo Y.S., Sriariyanum M., Ronald P.C.,
Sonti R.V., Van Sluys M.A., Leach J.E., White F.F., Bogdanove A.J.;
"Genome sequence and rapid evolution of the rice pathogen Xanthomonas
oryzae pv. oryzae PXO99A.";
BMC Genomics 9:204-204(2008).
[2] {ECO:0000313|EMBL:ACD59247.1}
NUCLEOTIDE SEQUENCE.
STRAIN=PXO99A {ECO:0000313|EMBL:ACD59247.1};
Salzberg S.;
Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:ACD59247.1}
NUCLEOTIDE SEQUENCE.
STRAIN=PXO99A {ECO:0000313|EMBL:ACD59247.1};
Booher N.J., Carpenter S.C.D., Sebra R.P., Wang L., Salzberg S.L.,
Leach J.E., Bogdanove A.J.;
Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-
serine, forming succinyl-L-serine. {ECO:0000256|HAMAP-
Rule:MF_00296}.
-!- CATALYTIC ACTIVITY: Succinyl-CoA + L-serine = CoA + O-succinyl-L-
serine. {ECO:0000256|HAMAP-Rule:MF_00296}.
-!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-
cysteine from L-serine: step 1/2. {ECO:0000256|HAMAP-
Rule:MF_00296}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00296}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00296}.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
{ECO:0000256|HAMAP-Rule:MF_00296, ECO:0000256|SAAS:SAAS00851697}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00296}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; CP000967; ACD59247.1; -; Genomic_DNA.
EMBL; CP000967; ACD59439.1; -; Genomic_DNA.
RefSeq; WP_011258800.1; NC_010717.2.
ProteinModelPortal; A0A0J9WX68; -.
SMR; A0A0J9WX68; -.
EnsemblBacteria; ACD59247; ACD59247; PXO_01100.
EnsemblBacteria; ACD59439; ACD59439; PXO_06257.
GeneID; 34177023; -.
KEGG; xop:PXO_01100; -.
KEGG; xop:PXO_06257; -.
PATRIC; fig|291331.8.peg.2308; -.
KO; K00641; -.
OMA; CQGTTGP; -.
UniPathway; UPA00136; UER00199.
Proteomes; UP000001740; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016750; F:O-succinyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
Gene3D; 3.40.50.1820; -; 1.
HAMAP; MF_00296; Homoser_O_acetyltr; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR000073; AB_hydrolase_1.
InterPro; IPR008220; HAT_MetX-like.
Pfam; PF00561; Abhydrolase_1; 1.
PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
SUPFAM; SSF53474; SSF53474; 2.
TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
3: Inferred from homology;
Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00296,
ECO:0000256|SAAS:SAAS00851686};
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00296};
Complete proteome {ECO:0000313|Proteomes:UP000001740};
Cysteine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00296};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00296};
Transferase {ECO:0000256|HAMAP-Rule:MF_00296,
ECO:0000256|SAAS:SAAS00851686}.
DOMAIN 45 384 AB hydrolase-1.
{ECO:0000259|Pfam:PF00561}.
REGION 52 55 Important for substrate specificity.
{ECO:0000256|HAMAP-Rule:MF_00296}.
ACT_SITE 149 149 Nucleophile. {ECO:0000256|HAMAP-
Rule:MF_00296,
ECO:0000256|PIRSR:PIRSR000443-1}.
ACT_SITE 345 345 {ECO:0000256|HAMAP-Rule:MF_00296,
ECO:0000256|PIRSR:PIRSR000443-1}.
ACT_SITE 378 378 {ECO:0000256|HAMAP-Rule:MF_00296,
ECO:0000256|PIRSR:PIRSR000443-1}.
BINDING 218 218 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00296}.
BINDING 379 379 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00296}.
SITE 186 186 Important for acyl-CoA specificity.
{ECO:0000256|HAMAP-Rule:MF_00296}.
SEQUENCE 399 AA; 43044 MW; 350B49A02511681F CRC64;
MTEFIPLGTL YHALPSPFQM KRGGVLHQAH VAYETWGALA ADRSNAVLIV TGLSPNAHAA
ANQANPEPGW WEAMVGPGKP IDTARWFVVC VNSLGSCKGS TGPASVNPAT GALYRLTFPD
LSIEDVADAA ADVVRALGIA QLACLIGNSM GGMTALALLL RHPGIARSHI NISGSAQALP
FSIAIRSLQR EAIRLDPHWN GGHYDDTRYP ESGMRMARKL GVITYRSALE WDGRFGRVRL
DSEQSEDDPF GLEFQVESYL EGHARRFVRF FDPNCYLYLS RSMDWFDLAE YVDDKPAADM
GIDSPGADAL PAAKSETGVS TASTVLAGLA RIRIARALAI GANTDILFPV QQQEQIADGL
RAGDADARFI GLDSPQGHDA FLVDFARFGP AVRDFLQGC


Related products :

Catalog number Product name Quantity
EIAAB28675 2-oxoglutarate dehydrogenase complex component E2,Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex,Dihydrolipoyllysine-residue succinyltransferase component of 2-
EIAAB28678 2-oxoglutarate dehydrogenase complex component E2,Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex,Dihydrolipoyllysine-residue succinyltransferase component of 2-
EIAAB28677 2-oxoglutarate dehydrogenase complex component E2,Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex,Dihydrolipoyllysine-residue succinyltransferase component of 2-
EIAAB28676 2-oxoglutarate dehydrogenase complex component E2,Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex,Dihydrolipoyllysine-residue succinyltransferase component of 2-
EIAAB39937 D-serine ammonia-lyase,D-serine dehydratase,Homo sapiens,Human,L-serine ammonia-lyase,L-serine dehydratase,Serine racemase,SRR
EIAAB39936 D-serine ammonia-lyase,D-serine dehydratase,L-serine ammonia-lyase,L-serine dehydratase,Mouse,Mus musculus,Serine racemase,Srr
EIAAB39934 D-serine ammonia-lyase,D-serine dehydratase,L-serine ammonia-lyase,L-serine dehydratase,Rat,Rattus norvegicus,Serine racemase,Srr
EIAAB39935 Bos taurus,Bovine,D-serine ammonia-lyase,D-serine dehydratase,L-serine ammonia-lyase,L-serine dehydratase,Serine racemase,SRR
REN-083 Recombinant Human Dihydrolipoamide S-Succinyltransferase 2
enz-083 Recombinant Human Dihydrolipoamide S-Succinyltransferase 2
enz-083 Recombinant Human Dihydrolipoamide S-Succinyltransferase 10
enz-083 Recombinant Human Dihydrolipoamide S-Succinyltransferase 1mg
OETENZ-083 Dihydrolipoamide S-Succinyltransferase Human Recombinant 10
enz-083 Recombinant Human Dihydrolipoamide S-Succinyltransferase ENZYMES 10
enz-083 Recombinant Human Dihydrolipoamide S-Succinyltransferase ENZYMES 2
enz-083 Recombinant Human Dihydrolipoamide S-Succinyltransferase DLST 10
enz-083 Recombinant Human Dihydrolipoamide S-Succinyltransferase DLST 2
enz-083 Recombinant Human Dihydrolipoamide S-Succinyltransferase ENZYMES 1mg
enz-083 Recombinant Human Dihydrolipoamide S-Succinyltransferase DLST 1mg
7-02672 Recombinant Human Dihydrolipoamide S-Succinyltransferase 10
OETENZ-083 Dihydrolipoamide S-Succinyltransferase Human Recombinant 2
7-02671 Recombinant Human Dihydrolipoamide S-Succinyltransferase 2
7-02673 Recombinant Human Dihydrolipoamide S-Succinyltransferase 1mg
E10024h Human Dihydrolipoyl Succinyltransferase ELISA Kit 96T
UB-E03701 Human Dihydrolipoyl Succinyltransferase(DLST)ELISA Kit 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