(data stored in SCRATCH zone)

SWISSPROT: Q13S29_PARXL

ID   Q13S29_PARXL            Unreviewed;       373 AA.
AC   Q13S29;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 100.
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   ORFNames=Bxe_B2885 {ECO:0000313|EMBL:ABE33110.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33110.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33110.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33110.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(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; CP000271; ABE33110.1; -; Genomic_DNA.
DR   RefSeq; WP_011490493.1; NZ_CP008762.1.
DR   STRING; 266265.Bxe_B2885; -.
DR   EnsemblBacteria; ABE33110; ABE33110; Bxe_B2885.
DR   GeneID; 4006750; -.
DR   KEGG; bxb:DR64_5215; -.
DR   KEGG; bxe:Bxe_B2885; -.
DR   PATRIC; fig|266265.5.peg.4804; -.
DR   eggNOG; ENOG4107QJH; Bacteria.
DR   eggNOG; COG0136; LUCA.
DR   HOGENOM; HOG000161376; -.
DR   KO; K00133; -.
DR   OMA; VGTDPTW; -.
DR   OrthoDB; 1799040at2; -.
DR   BioCyc; BXEN266265:BXE_RS22770-MONOMER; -.
DR   UniPathway; UPA00034; UER00016.
DR   UniPathway; UPA00050; UER00463.
DR   UniPathway; UPA00051; UER00464.
DR   Proteomes; UP000001817; 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; Q13S29.
DR   SWISS-2DPAGE; Q13S29.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
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:ABE33110.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
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;  40215 MW;  95A6ED67EA88FAB2 CRC64;
     MNVGLVGWRG MVGSVLMQRM QQEGDFDLIE PVFFSTSNAG GNAPSFAKNE TKLKDATSIE
     DLKKCEAIIS CQGGDYTNEV FPKLRAAGWN GYWIDAASSL RMKDDAVIIL DPVNLDVIKN
     ALVKGQKNFI GGNCTVSLML MALGGLFREN LVDWMTAMTY QAASGAGAQN MRELLQQMGT
     LYGAAKEDLA DPSSAILDID RRVLSAMNSD RMPTGNFGVP LAGSLIPWID KDLGNGMSKE
     EWKGGAETNK ILGKPAMGTP GSIPVDGLCV RIGAMRCHSQ ALTIKLNKDV PLDEVNSILA
     SGNDWVKVVP NEREASMRDL SPAVVTGTLT VPVGRVRKLA MGGEYLSAFT VGDQLLWGAA
     EPLRRMLRIV LDK
//

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