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

Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)

 A0A1D2QNN9_9GAMM        Unreviewed;       377 AA.
A0A1D2QNN9;
30-NOV-2016, integrated into UniProtKB/TrEMBL.
30-NOV-2016, sequence version 1.
25-OCT-2017, entry version 8.
RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121};
Short=ASA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121};
Short=ASADH {ECO:0000256|HAMAP-Rule:MF_02121};
EC=1.2.1.11 {ECO:0000256|HAMAP-Rule:MF_02121};
AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121};
Name=asd {ECO:0000256|HAMAP-Rule:MF_02121};
ORFNames=AB835_10190 {ECO:0000313|EMBL:ODS23201.1};
Candidatus Endobugula sertula (Bugula neritina bacterial symbiont).
Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
Cellvibrionaceae; Candidatus Endobugula.
NCBI_TaxID=62101 {ECO:0000313|EMBL:ODS23201.1};
[1] {ECO:0000313|EMBL:ODS23201.1}
NUCLEOTIDE SEQUENCE.
STRAIN=AB1-4 {ECO:0000313|EMBL:ODS23201.1};
PubMed=27590822;
Miller I.J., Vanee N., Fong S.S., Lim-Fong G.E., Kwan J.C.;
"Lack of overt genome reduction in the bryostatin-producing bryozoan
symbiont, 'Candidatus Endobugula sertula'.";
Appl. Environ. Microbiol. 0:0-0(2016).
-!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-
semialdehyde (L-ASA) by the reductive dephosphorylation of L-
aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.
-!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + phosphate +
NADP(+) = L-4-aspartyl phosphate + NADPH. {ECO:0000256|HAMAP-
Rule:MF_02121}.
-!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
{ECO:0000256|HAMAP-Rule:MF_02121}.
-!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
novo pathway; L-homoserine from L-aspartate: step 2/3.
{ECO:0000256|HAMAP-Rule:MF_02121}.
-!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
threonine from L-aspartate: step 2/5. {ECO:0000256|HAMAP-
Rule:MF_02121}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02121}.
-!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase
family. {ECO:0000256|HAMAP-Rule:MF_02121,
ECO:0000256|SAAS:SAAS00827794}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02121}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:ODS23201.1}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; MDLC01000036; ODS23201.1; -; Genomic_DNA.
UniPathway; UPA00034; UER00016.
UniPathway; UPA00050; UER00463.
UniPathway; UPA00051; UER00464.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
HAMAP; MF_02121; ASADH; 1.
InterPro; IPR000319; Asp-semialdehyde_DH_CS.
InterPro; IPR011534; Asp_ADH_gamma-type.
InterPro; IPR012080; Asp_semialdehyde_DH.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
PANTHER; PTHR10174:SF116; PTHR10174:SF116; 1.
Pfam; PF01118; Semialdhyde_dh; 1.
Pfam; PF02774; Semialdhyde_dhC; 1.
SMART; SM00859; Semialdhyde_dh; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01745; asd_gamma; 1.
PROSITE; PS01103; ASD; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
NADP {ECO:0000256|HAMAP-Rule:MF_02121};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02121};
Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}.
DOMAIN 2 121 Semialdhyde_dh.
{ECO:0000259|SMART:SM00859}.
NP_BIND 9 12 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
NP_BIND 37 38 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
NP_BIND 164 165 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
ACT_SITE 134 134 Acyl-thioester intermediate.
{ECO:0000256|HAMAP-Rule:MF_02121}.
ACT_SITE 282 282 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 72 72 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
BINDING 101 101 Phosphate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 161 161 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 240 240 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 243 243 Phosphate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 275 275 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 358 358 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
SEQUENCE 377 AA; 40913 MW; 0A2D02E19BDD51FF CRC64;
MKVGFVGWRG MVGSVLMGRM IEENDFSNIE PVFFTTSSVG GEGPTIGKNS KPLKDAKDIT
ELAKMDAIVS CQGGDYTKEV FSPLRESGWN GYWIDAASTL RMEDTAVIVL DPVNAHVIER
ALDNGVKDFI GGNCTVSLML MAIGGLINAG HVEWISAMTY QAASGGGARH MRELISQMGE
LRDTVADELV DPTSAILDID KKIAEKMRDG SLLQDNFGVP LAGSVLPYID SELDSGQSRE
EWKGDAETNK IIGTSCQSNT TGLIPHIPVD GVCVRVGAMR CHSQALTIKL KQYLPIEEIE
SLINNANDWV TVVPNHKEAS LSDLTPTAVT GTLTIPVGRL RKMHMGPQYL SAFTVGDQLL
WGAAEPLRRM LQILLKH


Related products :

Catalog number Product name Quantity
EIAAB40021 Aldehyde dehydrogenase family 5 member A1,Aldh5a1,Mouse,Mus musculus,NAD(+)-dependent succinic semialdehyde dehydrogenase,Succinate-semialdehyde dehydrogenase, mitochondrial
EIAAB40019 Aldehyde dehydrogenase family 5 member A1,Aldh5a1,NAD(+)-dependent succinic semialdehyde dehydrogenase,Rat,Rattus norvegicus,Ssadh,Succinate-semialdehyde dehydrogenase, mitochondrial
EIAAB40020 Aldehyde dehydrogenase family 5 member A1,ALDH5A1,Homo sapiens,Human,NAD(+)-dependent succinic semialdehyde dehydrogenase,SSADH,Succinate-semialdehyde dehydrogenase, mitochondrial
EIAAB25036 Aldehyde dehydrogenase family 6 member A1,Aldh6a1,Malonate-semialdehyde dehydrogenase [acylating],Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial,MMSDH,Mouse,Mus musculus
EIAAB25037 Aldehyde dehydrogenase family 6 member A1,ALDH6A1,Homo sapiens,Human,Malonate-semialdehyde dehydrogenase [acylating],Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial,MMSDH,MMSDH
EIAAB25038 Aldehyde dehydrogenase family 6 member A1,Aldh6a1,Malonate-semialdehyde dehydrogenase [acylating],Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial,MMSDH,Mmsdh,Rat,Rattus norvegicus
EIAAB25035 Aldehyde dehydrogenase family 6 member A1,ALDH6A1,Bos taurus,Bovine,Malonate-semialdehyde dehydrogenase [acylating],Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial,MMSDH,MMSDH
EH1288 Succinate-semialdehyde dehydrogenase, mitochondrial Elisa Kit 96T
AASS AASDH Gene aminoadipate-semialdehyde dehydrogenase
E1043m Rat ELISA Kit FOR Alpha-aminoadipic semialdehyde dehydrogenase 96T
H3514 Succinate-semialdehyde dehydrogenase, mitochondrial (ALDH5A1), Rat, ELISA Kit 96T
enz-008 Recombinant Human Aminoadipate-Semialdehyde Dehydrogenase-Phosphopantetheinyl Transferase 1mg
enz-008 Recombinant Human Aminoadipate-Semialdehyde Dehydrogenase-Phosphopantetheinyl Transferase 20
CSB-EL001577RA Rat Succinate-semialdehyde dehydrogenase, mitochondrial(ALDH5A1) ELISA kit 96T
ADPPT_RAT Rat ELISA Kit FOR L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase 96T
enz-008 Recombinant Human Aminoadipate-Semialdehyde Dehydrogenase-Phosphopantetheinyl Transferase 5
CSB-EL001579RA Rat Alpha-aminoadipic semialdehyde dehydrogenase(ALDH7A1) ELISA kit 96T
AL7A1_MOUSE Mouse ELISA Kit FOR Alpha-aminoadipic semialdehyde dehydrogenase 96T
REN-008 Recombinant Human Aminoadipate-Semialdehyde Dehydrogenase-Phosphopantetheinyl Transferase 5
E14086h Human ELISA Kit FOR Alpha-aminoadipic semialdehyde dehydrogenase 96T
7-02360 Recombinant Human Aminoadipate-Semialdehyde Dehydrogenase-Phosphopantetheinyl Transferase 20
E0147m Mouse ELISA Kit FOR Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial 96T
CSB-EL001577RA Rat Succinate-semialdehyde dehydrogenase, mitochondrial(ALDH5A1) ELISA kit SpeciesRat 96T
enz-008 Recombinant Human Aminoadipate-Semialdehyde Dehydrogenase-Phosphopantetheinyl Transferase ENZYMES 5
E0633d Bovine ELISA Kit FOR Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial 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