GENTAUR Molecular Products.
Monoclonal Antibody, ELISA Kit, Polyclonal Antibody, Recombinant/Purified Protein.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)
A0A0A8WW39_9DELT Unreviewed; 367 AA.
A0A0A8WW39;
04-MAR-2015, integrated into UniProtKB/TrEMBL.
04-MAR-2015, sequence version 1.
25-OCT-2017, entry version 19.
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,
ECO:0000313|EMBL:GAM10987.1};
ORFNames=OR1_03295 {ECO:0000313|EMBL:GAM10987.1};
Geobacter sp. OR-1.
Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
Geobacteraceae; Geobacter.
NCBI_TaxID=1266765 {ECO:0000313|EMBL:GAM10987.1, ECO:0000313|Proteomes:UP000030972};
[1] {ECO:0000313|EMBL:GAM10987.1, ECO:0000313|Proteomes:UP000030972}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR-1 {ECO:0000313|EMBL:GAM10987.1,
ECO:0000313|Proteomes:UP000030972};
PubMed=23668621; DOI=10.1021/es400231x;
Ohtsuka T., Yamaguchi N., Makino T., Sakurai K., Kimura K., Kudo K.,
Homma E., Dong DT., Amachi S.;
"Arsenic dissolution from Japanese paddy soil by a dissimilatory
arsenate-reducing bacterium Geobacter sp. OR-1.";
Environ. Sci. Technol. 47:6263-6271(2013).
[2] {ECO:0000313|EMBL:GAM10987.1, ECO:0000313|Proteomes:UP000030972}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR-1 {ECO:0000313|EMBL:GAM10987.1,
ECO:0000313|Proteomes:UP000030972};
Ehara A., Suzuki H., Amachi S.;
"Draft Genome Sequence of Geobacter sp. Strain OR-1, an Arsenate-
Respiring Bacterium Isolated from Japanese Paddy Soil.";
Genome Announc. 3:e01478-14(2015).
-!- 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:GAM10987.1}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; BAZF01000018; GAM10987.1; -; Genomic_DNA.
RefSeq; WP_041972970.1; NZ_BAZF01000018.1.
EnsemblBacteria; GAM10987; GAM10987; OR1_03295.
UniPathway; UPA00034; UER00016.
UniPathway; UPA00050; UER00463.
UniPathway; UPA00051; UER00464.
Proteomes; UP000030972; Unassembled WGS sequence.
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};
Complete proteome {ECO:0000313|Proteomes:UP000030972};
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};
Reference proteome {ECO:0000313|Proteomes:UP000030972};
Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}.
DOMAIN 2 119 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 162 163 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
ACT_SITE 132 132 Acyl-thioester intermediate.
{ECO:0000256|HAMAP-Rule:MF_02121}.
ACT_SITE 272 272 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 70 70 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
BINDING 99 99 Phosphate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 159 159 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 239 239 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 242 242 Phosphate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 265 265 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 348 348 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
SEQUENCE 367 AA; 39900 MW; 44B852B3084562EE CRC64;
MKVGMVGWRG MVGSVLMQRM QEENDFSLGF EPVFFTTSQA GQPAPMGGGT LKKADDIEEL
KKLDIIITCQ GGDYTKAVHP ELRKQGWNGY WIDAASTLRM EDNAVIILDP VNRNVIDAAL
AKGQKDFIGG NCTVSLMLMG LGGLFRAGLV EWLSSMTYQA ASGAGAPNMR ELLSQMGVLQ
GVVAEELKNP GSAILEIDKK VTATLRDGSM PMKEFGGFPL AGNVLPWIDR EVEDGQSREE
WKGFSETNKI LGTTSPIPVD GICVRVGAMR CHSQGITMKL TKDLPLADIE QIIANDNQWV
KLIPNTKADT LAGLTPAAVS GLLTVPVGRV RKMKMGPQYV QAFTCGDQLL WGAAEPLRRM
LRILMEK
Related products :
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
Pathways :
WP1493: Carbon assimilation C4 pathway
WP1566: Citrate cycle (TCA cycle)
WP1614: 1- and 2-Methylnaphthalene degradation
WP1628: beta-Alanine metabolism
WP1655: Geraniol degradation
WP1567: Glycolysis and Gluconeogenesis
WP1581: Histidine metabolism
WP1612: 1,2-Dichloroethane degradation
WP1615: 3-Chloroacrylic acid degradation
WP1621: Arginine and proline metabolism
WP1622: Ascorbate and aldarate metabolism
WP1626: Benzoate degradation via CoA ligation
WP1627: Benzoate degradation via hydroxylation
WP1633: Bisphenol A degradation
WP1634: Butanoate metabolism
WP1647: Fatty acid biosynthesis
WP1652: Fructose and mannose metabolism
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1665: Limonene and pinene degradation
WP1666: Linoleic acid metabolism
WP167: Eicosanoid Synthesis
WP1671: Methane metabolism
WP1673: Naphthalene and anthracene degradation
WP1680: Oxidative phosphorylation
Related Genes :
[asd hom b3433 JW3396] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd HI_0646] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd Rv3708c MTV025.056c] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd1 VC_2036] Aspartate-semialdehyde dehydrogenase 1 (ASA dehydrogenase 1) (ASADH 1) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase 1)
[asd2 asd VC_2107] Aspartate-semialdehyde dehydrogenase 2 (ASA dehydrogenase 2) (ASADH 2) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase 2)
[asd MJ0205] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[HOM2 YDR158W YD8358.12] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[leuB asd CMQ79_05370] Multifunctional fusion protein [Includes: 3-isopropylmalate dehydrogenase (EC 1.1.1.85) (3-IPM-DH) (Beta-IPM dehydrogenase) (IMDH); Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)]
[asd STM3539] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[SPCC1827.06c] Probable aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd PA3117] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd BSU16750] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd UAO_02023] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd NMB2079] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd NMA0351] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd c4220] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[patA asd S100892_02063] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd Z4797 ECs4278] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd STY4271 t3981] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd SF3456 S4307] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd slr0549] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd A6R73_07155] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd asd_1 asd_2 asd_3 asd_4 AZJ05_03090 AZJ06_02235 AZJ08_04460 AZJ10_03115 AZJ11_07185 AZJ13_08415 AZJ14_03675 AZJ15_05715 AZJ16_01260 AZJ18_06410 AZJ19_04860 AZJ20_07885 AZJ80_07775 AZK24_07745 CWI64_00715 ERS019416_01301 ERS019595_01888 ERS020138_00850 ERS020158_01027 ERS020491_00573 ERS020525_01180 ERS020528_01307 ERS020532_01397 ERS020541_00357 ERS020726_01370 ERS020726_01376 ERS020726_01384 ERS020726_01388 ERS021218_01947 ERS021733_03500 ERS022363_00892 ERS068943_01020 ERS232524_01825 ERS409064_01891 NTPn46_10260 SpnNT_01253] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd BQ2027_MB3735C] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd HP_1189] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd Cgl0252 cg0307] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd aq_1866] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd Cj1023c] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd_1 asd CLOBL_46240] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
Bibliography :
No related Items
Enter catalog number :
Favorites Pages:
No Favorits