DHAS_STRMU
ID DHAS_STRMU Reviewed; 358 AA.
AC P10539;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 150.
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}; OrderedLocusNames=SMU_989;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2434499; DOI=10.1016/s0021-9258(18)61509-1;
RA Cardineau G.A., Curtiss R. III;
RT "Nucleotide sequence of the asd gene of Streptococcus mutans.
RT Identification of the promoter region and evidence for attenuator-like
RT sequences preceding the structural gene.";
RL J. Biol. Chem. 262:3344-3353(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; J02667; AAA26850.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58690.1; -; Genomic_DNA.
DR PIR; A29137; A29137.
DR RefSeq; NP_721384.1; NC_004350.2.
DR RefSeq; WP_002263802.1; NC_004350.2.
DR AlphaFoldDB; P10539; -.
DR SMR; P10539; -.
DR STRING; 210007.SMU_989; -.
DR PRIDE; P10539; -.
DR EnsemblBacteria; AAN58690; AAN58690; SMU_989.
DR GeneID; 66817594; -.
DR KEGG; smu:SMU_989; -.
DR PATRIC; fig|210007.7.peg.882; -.
DR eggNOG; COG0136; Bacteria.
DR HOGENOM; CLU_049966_0_1_9; -.
DR OMA; CEEEMKM; -.
DR PhylomeDB; P10539; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR Proteomes; UP000002512; 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..358
FT /note="Aspartate-semialdehyde dehydrogenase"
FT /id="PRO_0000141392"
FT ACT_SITE 128
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 11..14
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 39..40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 99
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 158..159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 223
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 325
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT CONFLICT 64
FT /note="G -> A (in Ref. 1; AAA26850)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="L -> F (in Ref. 1; AAA26850)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="T -> H (in Ref. 1; AAA26850)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="Missing (in Ref. 1; AAA26850)"
FT /evidence="ECO:0000305"
FT CONFLICT 335..340
FT /note="VQIAES -> IITANR (in Ref. 1; AAA26850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 38903 MW; 11F5E4AD52C1A40B CRC64;
MGYTVAIVGA TGAVGTRMIQ QLEQSTLPVD KVRLLSSSRS AGKVLQYKDQ DVTVELTTKD
SFEGVDIALF SAGGSVSAKF APYAVKAGAV VVDNTSHFRQ NPDVPLVVPE VNAYAMDAHN
GIIACPNCST IQMMVALEPI RQKWGLSRVI VSTYQAVSGA GQSAINETVR EIKEVVNDGV
DPKAVHADIL PSGGDKKHYP IAFNALAQID VFTDNDYTYE EMKMTNETKK IMEEPELPVS
ATCVRVPILF SHSEAVYIET KDVAPIEEVK AAIAAFPGAV LEDDIKHQIY PQAANAVGSR
ETFVGRIRKD LDIENGIHMW VVSDNLLKGA AWNSVQIAES LHERGLVRST SELKFELK
