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

 J8B7G1_BACCE            Unreviewed;       348 AA.
J8B7G1;
31-OCT-2012, integrated into UniProtKB/TrEMBL.
31-OCT-2012, sequence version 1.
13-FEB-2019, entry version 33.
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=IEE_01642 {ECO:0000313|EMBL:EJQ47019.1};
Bacillus cereus BAG5X1-1.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
Bacillus cereus group.
NCBI_TaxID=1053189 {ECO:0000313|EMBL:EJQ47019.1, ECO:0000313|Proteomes:UP000006600};
[1] {ECO:0000313|EMBL:EJQ47019.1, ECO:0000313|Proteomes:UP000006600}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BAG5X1-1 {ECO:0000313|EMBL:EJQ47019.1,
ECO:0000313|Proteomes:UP000006600};
The Broad Institute Genome Sequencing Platform;
The Broad Institute Genome Sequencing Center for Infectious Disease;
Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V.,
Timmery S., Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X.,
Shank E.B., Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q.,
Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A.,
Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C.,
Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
Nusbaum C., Birren B.;
"The Genome Sequence of Bacillus cereus BAG5X1-1.";
Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
-!- 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:
Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-
phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284,
ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535,
ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519;
EC=1.2.1.11; Evidence={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:EJQ47019.1}.
-----------------------------------------------------------------------
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EMBL; AHDJ01000019; EJQ47019.1; -; Genomic_DNA.
RefSeq; WP_002014577.1; NZ_JH791996.1.
ProteinModelPortal; J8B7G1; -.
EnsemblBacteria; EJQ47019; EJQ47019; IEE_01642.
GeneID; 29401809; -.
PATRIC; fig|1053189.3.peg.1664; -.
UniPathway; UPA00034; UER00016.
UniPathway; UPA00050; UER00463.
UniPathway; UPA00051; UER00464.
Proteomes; UP000006600; Unassembled WGS sequence.
GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
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; IPR012080; Asp_semialdehyde_DH.
InterPro; IPR005986; Asp_semialdehyde_DH_beta.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
Pfam; PF01118; Semialdhyde_dh; 1.
Pfam; PF02774; Semialdhyde_dhC; 1.
SMART; SM00859; Semialdhyde_dh; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01296; asd_B; 1.
PROSITE; PS01103; ASD; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
Complete proteome {ECO:0000313|Proteomes:UP000006600};
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 8 123 Semialdhyde_dh.
{ECO:0000259|SMART:SM00859}.
NP_BIND 15 18 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
NP_BIND 43 44 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 252 252 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 103 103 Phosphate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 159 159 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 245 245 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 326 326 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
SEQUENCE 348 AA; 38037 MW; 0E6C3EB53FFF9F2A CRC64;
MEKQKTFHVA VVGATGAVGE QMLNTLEKRE FPIGKLTLLS SKRSAGKKLV FKGEEFTVQE
ATPESFEGVD IALFSAGGSV SKQLAPEAAK RGAIVVDNTS AFRMTENVPL VVPEVNENDL
KEHNGIIANP NCSTIQMVVA LEPVRQQYGL KRVIVSTYQA VSGAGAAAIE ELHEQSQAIL
NGEEVKANVL PVSGDEKHFQ IAFNAIPQID KFQDNGFTFE EMKMINETKK IMHMPELEVA
ATCVRLPVVS GHSESVYIEV DKEGVTVEEM KNLLANAEGI VLQDNPAEQL YPMPATAVGK
NEVFVGRIRK DLNNDKGFHL WVVSDNLLKG AAWNSVQIAE RLVKLQLV


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Kits Elisa; taq POLYMERASE

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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 HI_0646] 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)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); 3C-like serine proteinase (3CLSP) (EC 3.4.21.-) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); 3C-like serine proteinase (3CLSP) (EC 3.4.21.-) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[asd OR1_03294] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd OR1_03295] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd OR37_00671] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd OR221_2329] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd OR37_03116] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd HPHPP11_0720] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd HPHPH11_1467] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd HPHPP1_1481] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[iolA mmsA yxdA BSU39760 E83A] Malonate-semialdehyde dehydrogenase (MSA dehydrogenase) (EC 1.2.1.-) (Methylmalonate-semialdehyde dehydrogenase) (MMSA dehydrogenase) (MMSDH) (MSDH) (EC 1.2.1.27)
[asd HPHPP2_1347] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd ATE51_01574] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd OUS_1519] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd OUM_1300] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd OUE_1320] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd OUK_1468] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd OUG_1407] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd OUO_1112] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd Loa_00899] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[ALDH18A1 GSAS P5CS PYCS] Delta-1-pyrroline-5-carboxylate synthase (P5CS) (Aldehyde dehydrogenase family 18 member A1) [Includes: Glutamate 5-kinase (GK) (EC 2.7.2.11) (Gamma-glutamyl kinase); Gamma-glutamyl phosphate reductase (GPR) (EC 1.2.1.41) (Glutamate-5-semialdehyde dehydrogenase) (Glutamyl-gamma-semialdehyde dehydrogenase)]
[asd HPHPP62_1235] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd HPHPA8_1040] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd HPHPA26_1293] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd HPNQ4099_1389] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd HPCPY6311_1209] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd HPHPH16_1360] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)
[asd HPNQ4200_1104] Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)

Bibliography :
[22683789] Structures of ternary complexes of aspartate-semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis H37Rv.
[18323627] The structure of a redundant enzyme: a second isoform of aspartate beta-semialdehyde dehydrogenase in Vibrio cholerae.
[18236087] Molecular modelling and comparative structural account of aspartyl beta-semialdehyde dehydrogenase of Mycobacterium tuberculosis (H37Rv).
[15583380] Structural basis for discrimination between oxyanion substrates or inhibitors in aspartate-beta-semialdehyde dehydrogenase.
[15272161] The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase.
[14726201] L-cystine inhibits aspartate-beta-semialdehyde dehydrogenase by covalently binding to the essential 135Cys of the enzyme.