GENTAUR Molecular Products.

 A0A0A8WW39_9DELT        Unreviewed;       367 AA.
 A0A0A8WW39;
 04-MAR-2015, integrated into UniProtKB/TrEMBL.
 04-MAR-2015, sequence version 1.
 23-MAY-2018, entry version 20.
 RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121};
          Short=ASA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121};
          Short=ASADH {ECO:0000256|HAMAP-Rule:MF_02121};
          EC=1.2.1.11 {ECO:0000256|HAMAP-Rule:MF_02121};
 AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_02121};
 Name=asd {ECO:0000256|HAMAP-Rule:MF_02121,
 ECO:0000313|EMBL:GAM10987.1};
 ORFNames=OR1_03295 {ECO:0000313|EMBL:GAM10987.1};
 Geobacter sp. OR-1.
 Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
 Geobacteraceae; Geobacter.
 NCBI_TaxID=1266765 {ECO:0000313|EMBL:GAM10987.1, ECO:0000313|Proteomes:UP000030972};
 [1] {ECO:0000313|EMBL:GAM10987.1, ECO:0000313|Proteomes:UP000030972}
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=OR-1 {ECO:0000313|EMBL:GAM10987.1,
 ECO:0000313|Proteomes:UP000030972};
 PubMed=23668621; DOI=10.1021/es400231x;
 Ohtsuka T., Yamaguchi N., Makino T., Sakurai K., Kimura K., Kudo K.,
 Homma E., Dong DT., Amachi S.;
 "Arsenic dissolution from Japanese paddy soil by a dissimilatory
 arsenate-reducing bacterium Geobacter sp. OR-1.";
 Environ. Sci. Technol. 47:6263-6271(2013).
 [2] {ECO:0000313|EMBL:GAM10987.1, ECO:0000313|Proteomes:UP000030972}
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=OR-1 {ECO:0000313|EMBL:GAM10987.1,
 ECO:0000313|Proteomes:UP000030972};
 Ehara A., Suzuki H., Amachi S.;
 "Draft Genome Sequence of Geobacter sp. Strain OR-1, an Arsenate-
 Respiring Bacterium Isolated from Japanese Paddy Soil.";
 Genome Announc. 3:e01478-14(2015).
 -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-
     semialdehyde (L-ASA) by the reductive dephosphorylation of L-
     aspartyl-4-phosphate. {ECO:0000256|HAMAP-Rule:MF_02121}.
 -!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + phosphate +
     NADP(+) = L-4-aspartyl phosphate + NADPH. {ECO:0000256|HAMAP-
     Rule:MF_02121}.
 -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
     pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
     {ECO:0000256|HAMAP-Rule:MF_02121}.
 -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
     novo pathway; L-homoserine from L-aspartate: step 2/3.
     {ECO:0000256|HAMAP-Rule:MF_02121}.
 -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
     threonine from L-aspartate: step 2/5. {ECO:0000256|HAMAP-
     Rule:MF_02121}.
 -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02121}.
 -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase
     family. {ECO:0000256|HAMAP-Rule:MF_02121,
     ECO:0000256|SAAS:SAAS00827794}.
 -!- CAUTION: Lacks conserved residue(s) required for the propagation
     of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02121}.
 -!- CAUTION: The sequence shown here is derived from an
     EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
     preliminary data. {ECO:0000313|EMBL:GAM10987.1}.
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 EMBL; BAZF01000018; GAM10987.1; -; Genomic_DNA.
 RefSeq; WP_041972970.1; NZ_BAZF01000018.1.
 EnsemblBacteria; GAM10987; GAM10987; OR1_03295.
 UniPathway; UPA00034; UER00016.
 UniPathway; UPA00050; UER00463.
 UniPathway; UPA00051; UER00464.
 Proteomes; UP000030972; Unassembled WGS sequence.
 GO; GO:0005737; C:cytoplasm; IEA:InterPro.
 GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
 GO; GO:0051287; F:NAD binding; IEA:InterPro.
 GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
 GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
 GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-UniRule.
 GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-UniRule.
 GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
 GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
 GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
 HAMAP; MF_02121; ASADH; 1.
 InterPro; IPR000319; Asp-semialdehyde_DH_CS.
 InterPro; IPR011534; Asp_ADH_gamma-type.
 InterPro; IPR012080; Asp_semialdehyde_DH.
 InterPro; IPR036291; NAD(P)-bd_dom_sf.
 InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
 InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
 PANTHER; PTHR10174:SF116; PTHR10174:SF116; 1.
 Pfam; PF01118; Semialdhyde_dh; 1.
 Pfam; PF02774; Semialdhyde_dhC; 1.
 SMART; SM00859; Semialdhyde_dh; 1.
 SUPFAM; SSF51735; SSF51735; 1.
 TIGRFAMs; TIGR01745; asd_gamma; 1.
 PROSITE; PS01103; ASD; 1.
 3: Inferred from homology;
 Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
 Complete proteome {ECO:0000313|Proteomes:UP000030972};
 Diaminopimelate biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
 Lysine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
 Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
 NADP {ECO:0000256|HAMAP-Rule:MF_02121};
 Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02121};
 Reference proteome {ECO:0000313|Proteomes:UP000030972};
 Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}.
 DOMAIN        2    119       Semialdhyde_dh.
                              {ECO:0000259|SMART:SM00859}.
 NP_BIND       9     12       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
 NP_BIND      37     38       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
 NP_BIND     162    163       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
 ACT_SITE    132    132       Acyl-thioester intermediate.
                              {ECO:0000256|HAMAP-Rule:MF_02121}.
 ACT_SITE    272    272       Proton acceptor. {ECO:0000256|HAMAP-
                              Rule:MF_02121}.
 BINDING      70     70       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
 BINDING      99     99       Phosphate. {ECO:0000256|HAMAP-
                              Rule:MF_02121}.
 BINDING     159    159       Substrate. {ECO:0000256|HAMAP-
                              Rule:MF_02121}.
 BINDING     239    239       Substrate. {ECO:0000256|HAMAP-
                              Rule:MF_02121}.
 BINDING     242    242       Phosphate. {ECO:0000256|HAMAP-
                              Rule:MF_02121}.
 BINDING     265    265       Substrate. {ECO:0000256|HAMAP-
                              Rule:MF_02121}.
 BINDING     348    348       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
 SEQUENCE   367 AA;  39900 MW;  44B852B3084562EE CRC64;
 MKVGMVGWRG MVGSVLMQRM QEENDFSLGF EPVFFTTSQA GQPAPMGGGT LKKADDIEEL
 KKLDIIITCQ GGDYTKAVHP ELRKQGWNGY WIDAASTLRM EDNAVIILDP VNRNVIDAAL
 AKGQKDFIGG NCTVSLMLMG LGGLFRAGLV EWLSSMTYQA ASGAGAPNMR ELLSQMGVLQ
 GVVAEELKNP GSAILEIDKK VTATLRDGSM PMKEFGGFPL AGNVLPWIDR EVEDGQSREE
 WKGFSETNKI LGTTSPIPVD GICVRVGAMR CHSQGITMKL TKDLPLADIE QIIANDNQWV
 KLIPNTKADT LAGLTPAAVS GLLTVPVGRV RKMKMGPQYV QAFTCGDQLL WGAAEPLRRM
 LRILMEK

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