(data stored in ACNUC1104 zone)

SWISSPROT: C0ZN71_RHOE4

ID   C0ZN71_RHOE4            Unreviewed;       344 AA.
AC   C0ZN71;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   13-FEB-2019, entry version 68.
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   ECO:0000313|EMBL:BAH31123.1};
GN   OrderedLocusNames=RER_04150 {ECO:0000313|EMBL:BAH31123.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH31123.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH31123.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus
RT   erythropolis strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
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; AP008957; BAH31123.1; -; Genomic_DNA.
DR   RefSeq; WP_019746568.1; NC_012490.1.
DR   STRING; 234621.RER_04150; -.
DR   EnsemblBacteria; BAH31123; BAH31123; RER_04150.
DR   GeneID; 31540273; -.
DR   KEGG; rer:RER_04150; -.
DR   PATRIC; fig|234621.6.peg.856; -.
DR   eggNOG; ENOG4105CM3; Bacteria.
DR   eggNOG; COG0136; LUCA.
DR   HOGENOM; HOG000013357; -.
DR   KO; K00133; -.
DR   OMA; CEEEMKM; -.
DR   UniPathway; UPA00034; UER00016.
DR   UniPathway; UPA00050; UER00463.
DR   UniPathway; UPA00051; UER00464.
DR   Proteomes; UP000002204; 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; C0ZN71.
DR   SWISS-2DPAGE; C0ZN71.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002204};
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:BAH31123.1};
KW   Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   DOMAIN        3    121       Semialdhyde_dh. {ECO:0000259|SMART:
FT                                SM00859}.
FT   NP_BIND      10     13       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   NP_BIND      38     39       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   NP_BIND     161    162       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   ACT_SITE    131    131       Acyl-thioester intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   ACT_SITE    257    257       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     101    101       Phosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     158    158       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     250    250       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     326    326       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
SQ   SEQUENCE   344 AA;  35753 MW;  B8071ED7B4A6DEDD CRC64;
     MTTIAVVGAT GQVGIVMRTL LEERNFPADK VRFFASARSA GKKLTFRGEE IVVEDAEATS
     DEDLKGIDIA LFSAGATLSR AQAPRFAAAG ATVVDNSSAW RKDPEVPLVV SEVNPQDTKN
     LVKGIIANPN CTTMAAMPVL KVLHDEAGLQ RLIVSSYQAV SGSGIAGVEE LLGQVRAVVG
     DAEKLVHDGS AVDFPAPNNY VAPIAFNVLP LAGSLVDDGS GETDEDQKLR NESRKILGLP
     DLLVSGTCVR VPVVTGHSLA INAEFANPLS VARAKEILAD APGVELVEVP TPLAAAGGNA
     SLVGRIRQDP GVPEGRGLAL FVSGDNLRKG AALNTIQIAE LLVG
//

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