(data stored in ACNUC1104 zone)

SWISSPROT: B1K373_BURCC

ID   B1K373_BURCC            Unreviewed;       373 AA.
AC   B1K373;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 75.
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=Bcenmc03_3575 {ECO:0000313|EMBL:ACA92727.1};
OS   Burkholderia cenocepacia (strain MC0-3).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA92727.1, ECO:0000313|Proteomes:UP000002169};
RN   [1] {ECO:0000313|Proteomes:UP000002169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-
RT   3.";
RL   Submitted (FEB-2008) 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; CP000959; ACA92727.1; -; Genomic_DNA.
DR   RefSeq; WP_012338485.1; NC_010515.1.
DR   EnsemblBacteria; ACA92727; ACA92727; Bcenmc03_3575.
DR   KEGG; bcm:Bcenmc03_3575; -.
DR   HOGENOM; HOG000161376; -.
DR   KO; K00133; -.
DR   OMA; VGTDPTW; -.
DR   BioCyc; BCEN406425:G1GBC-3796-MONOMER; -.
DR   UniPathway; UPA00034; UER00016.
DR   UniPathway; UPA00050; UER00463.
DR   UniPathway; UPA00051; UER00464.
DR   Proteomes; UP000002169; Chromosome 2.
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   3: Inferred from homology;
DR   PRODOM; B1K373.
DR   SWISS-2DPAGE; B1K373.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002169};
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:ACA92727.1};
KW   Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   DOMAIN        2    121       Semialdhyde_dh. {ECO:0000259|SMART:
FT                                SM00859}.
FT   NP_BIND       9     12       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   NP_BIND     164    165       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   ACT_SITE    134    134       Acyl-thioester intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   ACT_SITE    278    278       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING      72     72       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   BINDING     101    101       Phosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     161    161       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     240    240       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     243    243       Phosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     271    271       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     354    354       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
SQ   SEQUENCE   373 AA;  40200 MW;  D42457BF34ABBBCC CRC64;
     MNVGLVGWRG MVGSVLMQRM QEEGDFDLIE PVFFSTSNTG GKAPSFAKNE TTLKDATNVD
     ELKKCDVIIT CQGGDYTNDV FPKLRAAGWN GYWIDAASSL RMQDDAVIIL DPVNLDVIKD
     ALVKGTKNFI GGNCTVSLML MALGGLFREN LVDWITAMTY QAASGAGAQN MRELLSQMGT
     LNGAVQEQLA DPASAILDID RRVLAAMNSD AMPTSHFGVP LAGSLIPWID KDLGNGMSKE
     EWKGGAETNK ILGKPAMGEP GSIPVDGLCV RIGAMRCHSQ ALTIKLKKDV PLDEINGILA
     SANDWVKVVP NEREASMRDL SPAKITGTLS VPVGRLRKLA MGGEYLSAFT VGDQLLWGAA
     EPLRRMLRIL LDK
//

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