DHAS_CORGL
ID DHAS_CORGL Reviewed; 344 AA.
AC P0C1D8; P26511; Q46062;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121};
DE Short=ASA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121};
DE Short=ASADH {ECO:0000255|HAMAP-Rule:MF_02121};
DE EC=1.2.1.11 {ECO:0000255|HAMAP-Rule:MF_02121};
DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121};
GN Name=asd {ECO:0000255|HAMAP-Rule:MF_02121};
GN OrderedLocusNames=Cgl0252, cg0307;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=1980002; DOI=10.1007/bf00262424;
RA Kalinowski J., Bachmann B., Thierbach G., Puehler A.;
RT "Aspartokinase genes lysC alpha and lysC beta overlap and are adjacent to
RT the aspartate beta-semialdehyde dehydrogenase gene asd in Corynebacterium
RT glutamicum.";
RL Mol. Gen. Genet. 224:317-324(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-
CC semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-
CC 4-phosphate. {ECO:0000255|HAMAP-Rule:MF_02121}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-
CC L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02121};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
CC {ECO:0000255|HAMAP-Rule:MF_02121}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 2/3. {ECO:0000255|HAMAP-
CC Rule:MF_02121}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 2/5. {ECO:0000255|HAMAP-Rule:MF_02121}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02121}.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_02121}.
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DR EMBL; X57226; CAA40504.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB97645.1; -; Genomic_DNA.
DR EMBL; BX927148; CAF18823.1; -; Genomic_DNA.
DR PIR; S49978; S49978.
DR RefSeq; NP_599505.1; NC_003450.3.
DR RefSeq; WP_011013506.1; NC_006958.1.
DR AlphaFoldDB; P0C1D8; -.
DR SMR; P0C1D8; -.
DR STRING; 196627.cg0307; -.
DR World-2DPAGE; 0001:P0C1D8; -.
DR KEGG; cgb:cg0307; -.
DR KEGG; cgl:Cgl0252; -.
DR PATRIC; fig|196627.13.peg.256; -.
DR eggNOG; COG0136; Bacteria.
DR HOGENOM; CLU_049966_0_0_11; -.
DR OMA; CEEEMKM; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02121; ASADH; 1.
DR InterPro; IPR000319; Asp-semialdehyde_DH_CS.
DR InterPro; IPR012080; Asp_semialdehyde_DH.
DR InterPro; IPR005986; Asp_semialdehyde_DH_beta.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR Pfam; PF02774; Semialdhyde_dhC; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01296; asd_B; 1.
DR PROSITE; PS01103; ASD; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Diaminopimelate biosynthesis; Lysine biosynthesis;
KW Methionine biosynthesis; NADP; Oxidoreductase; Reference proteome;
KW Threonine biosynthesis.
FT CHAIN 1..344
FT /note="Aspartate-semialdehyde dehydrogenase"
FT /id="PRO_0000141368"
FT ACT_SITE 131
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT ACT_SITE 257
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 10..13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 38..39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 101
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 161..162
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 228
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 326
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
SQ SEQUENCE 344 AA; 36212 MW; 38771D3DACCB41F8 CRC64;
MTTIAVVGAT GQVGQVMRTL LEERNFPADT VRFFASPRSA GRKIEFRGTE IEVEDITQAT
EESLKDIDVA LFSAGGTASK QYAPLFAAAG ATVVDNSSAW RKDDEVPLIV SEVNPSDKDS
LVKGIIANPN CTTMAAMPVL KPLHDAAGLV KLHVSSYQAV SGSGLAGVET LAKQVAAVGD
HNVEFVHDGQ AADAGDVGPY VSPIAYNVLP FAGNLVDDGT FETDEEQKLR NESRKILGLP
DLKVSGTCVR VPVFTGHTLT IHAEFDKAIT VDQAQEILGA ASGVKLVDVP TPLAAAGIDE
SLVGRIRQDS TVDDNRGLVL VVSGDNLRKG AALNTIQIAE LLVK
