DHAS_PSEAE
ID DHAS_PSEAE Reviewed; 370 AA.
AC Q51344;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE Short=ASA dehydrogenase;
DE Short=ASADH;
DE EC=1.2.1.11;
DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase;
GN Name=asd; OrderedLocusNames=PA3117;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9084174; DOI=10.1099/00221287-143-3-899;
RA Hoang T.T., Williams S., Schweizer H.P., Lam J.S.;
RT "Molecular genetic analysis of the region containing the essential
RT Pseudomonas aeruginosa asd gene encoding aspartate-beta-semialdehyde
RT dehydrogenase.";
RL Microbiology 143:899-907(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND KINETIC PARAMETERS.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=12071715; DOI=10.1006/prep.2002.1626;
RA Moore R.A., Bocik W.E., Viola R.E.;
RT "Expression and purification of aspartate beta-semialdehyde dehydrogenase
RT from infectious microorganisms.";
RL Protein Expr. Purif. 25:189-194(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:0000269|PubMed:12071715}.
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:0000269|PubMed:12071715};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.12 mM for L-aspartate 4-semialdehyde
CC {ECO:0000269|PubMed:12071715};
CC KM=0.13 mM for NADP(+) {ECO:0000269|PubMed:12071715};
CC KM=1.5 mM for phosphate {ECO:0000269|PubMed:12071715};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 2/3.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 2/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U11055; AAB51626.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06505.1; -; Genomic_DNA.
DR PIR; C83255; C83255.
DR RefSeq; NP_251807.1; NC_002516.2.
DR RefSeq; WP_003111187.1; NZ_QZGE01000023.1.
DR PDB; 5BNT; X-ray; 2.10 A; A/B/C/D=1-370.
DR PDBsum; 5BNT; -.
DR AlphaFoldDB; Q51344; -.
DR SMR; Q51344; -.
DR STRING; 287.DR97_4816; -.
DR PaxDb; Q51344; -.
DR PRIDE; Q51344; -.
DR EnsemblBacteria; AAG06505; AAG06505; PA3117.
DR GeneID; 882803; -.
DR KEGG; pae:PA3117; -.
DR PATRIC; fig|208964.12.peg.3269; -.
DR PseudoCAP; PA3117; -.
DR HOGENOM; CLU_066397_0_0_6; -.
DR InParanoid; Q51344; -.
DR OMA; MFDVPDE; -.
DR PhylomeDB; Q51344; -.
DR BioCyc; PAER208964:G1FZ6-3173-MON; -.
DR BRENDA; 1.2.1.11; 5087.
DR SABIO-RK; Q51344; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR Proteomes; UP000002438; 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; IPR011534; Asp_ADH_gamma-type.
DR InterPro; IPR012080; Asp_semialdehyde_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR PANTHER; PTHR46278:SF4; PTHR46278:SF4; 1.
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; TIGR01745; asd_gamma; 1.
DR PROSITE; PS01103; ASD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Diaminopimelate biosynthesis;
KW Lysine biosynthesis; Methionine biosynthesis; NADP; Oxidoreductase;
KW Reference proteome; Threonine biosynthesis.
FT CHAIN 1..370
FT /note="Aspartate-semialdehyde dehydrogenase"
FT /id="PRO_0000141387"
FT ACT_SITE 135
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 10..13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 37..38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 165..166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT CONFLICT 18
FT /note="M -> I (in Ref. 1; AAB51626)"
FT /evidence="ECO:0000305"
FT CONFLICT 42..44
FT /note="GQG -> AQA (in Ref. 1; AAB51626)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="G -> D (in Ref. 1; AAB51626)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="E -> D (in Ref. 1; AAB51626)"
FT /evidence="ECO:0000305"
FT CONFLICT 235..237
FT /note="PNG -> SQRR (in Ref. 1; AAB51626)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="S -> R (in Ref. 1; AAB51626)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="G -> V (in Ref. 1; AAB51626)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:5BNT"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:5BNT"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:5BNT"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:5BNT"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:5BNT"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 112..125
FT /evidence="ECO:0007829|PDB:5BNT"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 135..149
FT /evidence="ECO:0007829|PDB:5BNT"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 169..184
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:5BNT"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:5BNT"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:5BNT"
FT STRAND 270..285
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:5BNT"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 310..316
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:5BNT"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:5BNT"
FT STRAND 342..350
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 353..357
FT /evidence="ECO:0007829|PDB:5BNT"
FT HELIX 358..368
FT /evidence="ECO:0007829|PDB:5BNT"
SQ SEQUENCE 370 AA; 40495 MW; 03E66CF12FA9A378 CRC64;
MKRVGLIGWR GMVGSVLMQR MLEERDFDLI EPVFFTTSNV GGQGPEVGKD IAPLKDAYSI
DELKTLDVIL TCQGGDYTSE VFPKLREAGW QGYWIDAASS LRMEDDAVIV LDPVNRKVID
QALDAGTRNY IGGNCTVSLM LMALGGLFDA GLVEWMSAMT YQAASGAGAQ NMRELLKQMG
AAHASVADDL ANPASAILDI DRKVAETLRS EAFPTEHFGA PLGGSLIPWI DKELPNGQSR
EEWKAQAETN KILARFKNPI PVDGICVRVG AMRCHSQALT IKLNKDVPLT DIEGLISQHN
PWVKLVPNHR EVSVRELTPA AVTGTLSVPV GRLRKLNMGS QYLGAFTVGD QLLWGAAEPL
RRMLRILLER
