(data stored in SCRATCH zone)

SWISSPROT: Q13DV8_RHOPS

ID   Q13DV8_RHOPS            Unreviewed;       344 AA.
AC   Q13DV8;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 92.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121};
DE            Short=ASA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121};
DE            Short=ASADH {ECO:0000256|HAMAP-Rule:MF_02121};
DE            EC=1.2.1.11 {ECO:0000256|HAMAP-Rule:MF_02121};
DE   AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121};
GN   Name=asd {ECO:0000256|HAMAP-Rule:MF_02121};
GN   OrderedLocusNames=RPD_0493 {ECO:0000313|EMBL:ABE37731.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37731.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37731.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37731.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-
CC       semialdehyde (L-ASA) by the reductive dephosphorylation of L-
CC       aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-
CC         phospho-L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57535,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519;
CC         EC=1.2.1.11; Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_02121}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 2/3.
CC       {ECO:0000256|HAMAP-Rule:MF_02121}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 2/5. {ECO:0000256|HAMAP-
CC       Rule:MF_02121}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02121}.
CC   -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase
CC       family. {ECO:0000256|HAMAP-Rule:MF_02121,
CC       ECO:0000256|SAAS:SAAS00827794}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02121}.
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DR   EMBL; CP000283; ABE37731.1; -; Genomic_DNA.
DR   RefSeq; WP_011500919.1; NC_007958.1.
DR   STRING; 316057.RPD_0493; -.
DR   EnsemblBacteria; ABE37731; ABE37731; RPD_0493.
DR   KEGG; rpd:RPD_0493; -.
DR   eggNOG; ENOG4105CM3; Bacteria.
DR   eggNOG; COG0136; LUCA.
DR   HOGENOM; HOG000013357; -.
DR   KO; K00133; -.
DR   OMA; CEEEMKM; -.
DR   OrthoDB; 1799040at2; -.
DR   BioCyc; RPAL316057:RPD_RS02535-MONOMER; -.
DR   UniPathway; UPA00034; UER00016.
DR   UniPathway; UPA00050; UER00463.
DR   UniPathway; UPA00051; UER00464.
DR   Proteomes; UP000001818; 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;
DR   PRODOM; Q13DV8.
DR   SWISS-2DPAGE; Q13DV8.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
KW   Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_02121};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02121,
KW   ECO:0000313|EMBL:ABE37731.1};
KW   Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   DOMAIN        4    119       Semialdhyde_dh. {ECO:0000259|SMART:
FT                                SM00859}.
FT   NP_BIND      11     14       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   NP_BIND      39     40       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   NP_BIND     160    161       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   ACT_SITE    130    130       Acyl-thioester intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   ACT_SITE    242    242       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING      99     99       Phosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     157    157       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     235    235       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     315    315       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
SQ   SEQUENCE   344 AA;  37367 MW;  5DD4CC8AC1F4EBAD CRC64;
     MGYKVAVVGA TGNVGREMLA ILDERKFPAD EVVALASRRS IGVEVSYGDK TLKCKALEHY
     DFSDVDICLM SAGGAVSKEW SPQIGAQGAV VIDNSSAWRM DPDVPLIVPE VNAAAAAGFT
     KKNIIANPNC STAQLVVALK PLHDHAKITR VVVSTYQSVS GAGKEGMDEL FSQTKAVYTN
     SELVNKKFPK RIAFNVIPEI DVFMEDGYTK EEWKMMVETK KILDPAIKLS ATCVRVPVFV
     GHSEAVNIEF ENPITADEAR DILRRSPGCL VIDKHEPGGY VTPYEAAGED ATYISRIRTD
     PTVDNGLVLW CVSDNLRKGA ALNAIQIAEV LINRKLITAK KKAA
//

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