DHAS_CAMJE
ID DHAS_CAMJE Reviewed; 343 AA.
AC Q59291; Q0P9M9; Q9PNR7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 128.
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=Cj1023c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DZ72/92;
RX PubMed=9127485;
RA Pawelec D., Jagusztyn-Krynicka E.K.;
RT "Complete nucleotide sequence of the Campylobacter jejuni 72Dz asd gene.";
RL Acta Microbiol. Pol. 45:299-304(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; X97964; CAA66607.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL35141.1; -; Genomic_DNA.
DR PIR; D81304; D81304.
DR RefSeq; WP_002852931.1; NC_002163.1.
DR RefSeq; YP_002344418.1; NC_002163.1.
DR AlphaFoldDB; Q59291; -.
DR SMR; Q59291; -.
DR IntAct; Q59291; 61.
DR STRING; 192222.Cj1023c; -.
DR PaxDb; Q59291; -.
DR PRIDE; Q59291; -.
DR EnsemblBacteria; CAL35141; CAL35141; Cj1023c.
DR GeneID; 905315; -.
DR KEGG; cje:Cj1023c; -.
DR PATRIC; fig|192222.6.peg.1005; -.
DR eggNOG; COG0136; Bacteria.
DR HOGENOM; CLU_049966_0_1_7; -.
DR OMA; CEEEMKM; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR Proteomes; UP000000799; 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..343
FT /note="Aspartate-semialdehyde dehydrogenase"
FT /id="PRO_0000141366"
FT ACT_SITE 134
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 13..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 41..42
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 103
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 164..165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 220
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT BINDING 321
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02121"
FT CONFLICT 43..56
FT /note="VGSEVEFKGKAYKV -> AGNQIEFRGKSYTI (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 62..65
FT /note="NVFK -> DAFR (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="I -> V (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="S -> A (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="K -> E (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="D -> E (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 141..142
FT /note="QV -> HI (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="N -> D (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="Q -> E (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="E -> R (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="P -> A (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="Y -> H (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="D -> G (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="V -> I (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="V -> I (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="E -> A (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="I -> V (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="K -> N (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 266..267
FT /note="KE -> RD (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 270..271
FT /note="KK -> QN (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="I -> V (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="D -> E (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="N -> D (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="A -> L (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 308..311
FT /note="YDKK -> THKN (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="K -> E (in Ref. 1; CAA66607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 38375 MW; D122507423187E26 CRC64;
MSKKQKIAIV GATGAVGEEL LNVLDELDFP VESILPLASA KSVGSEVEFK GKAYKVKELT
ENVFKENPID IAFFSAGGSV SEKYAKFAVE SGAVVIDNTS HFRMEKDVPL VVPECNPEDI
KDWKKTGIIA NPNCSTIQMV QVLKPLNDAF NLKRVDVSTY QAASGAGKEG MQELVEAMQS
FFAFKLDEFE PQTFPYTLAL NLIPQIDVFM DNDYTKEELK MVNETQKILH KNLEVSATCV
RVPVLRSHSE AITMHFEKEI DVKKAKEILK KAPSVIVIDD PKNKKYPMPL MTSDTNETYV
GRIRADVYDK KILHLWCVAD QIRVGAATNA VRIAQKWLEL KNK
