(data stored in SCRATCH zone)

SWISSPROT: C6WF57_ACTMD

ID   C6WF57_ACTMD            Unreviewed;       355 AA.
AC   C6WF57;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 59.
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=Amir_0218 {ECO:0000313|EMBL:ACU34189.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34189.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34189.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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: L-aspartate 4-semialdehyde + phosphate +
CC       NADP(+) = L-4-aspartyl phosphate + NADPH. {ECO:0000256|HAMAP-
CC       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; CP001630; ACU34189.1; -; Genomic_DNA.
DR   RefSeq; WP_012782852.1; NC_013093.1.
DR   STRING; 446462.Amir_0218; -.
DR   EnsemblBacteria; ACU34189; ACU34189; Amir_0218.
DR   KEGG; ami:Amir_0218; -.
DR   eggNOG; ENOG4105CM3; Bacteria.
DR   eggNOG; COG0136; LUCA.
DR   HOGENOM; HOG000013357; -.
DR   KO; K00133; -.
DR   OMA; VGTDPTW; -.
DR   OrthoDB; POG091H00EF; -.
DR   UniPathway; UPA00034; UER00016.
DR   UniPathway; UPA00050; UER00463.
DR   UniPathway; UPA00051; UER00464.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_02121; ASADH; 1.
DR   InterPro; IPR012080; Asp_semialdehyde_DH.
DR   InterPro; IPR005986; Asp_semialdehyde_DH_beta.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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.
PE   3: Inferred from homology;
DR   PRODOM; C6WF57.
DR   SWISS-2DPAGE; C6WF57.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
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:ACU34189.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   DOMAIN        6    122       Semialdhyde_dh. {ECO:0000259|SMART:
FT                                SM00859}.
FT   NP_BIND      13     16       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   NP_BIND      42     43       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   NP_BIND     162    163       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   ACT_SITE    132    132       Acyl-thioester intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_02121}.
FT   ACT_SITE    262    262       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     102    102       Phosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     159    159       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     255    255       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02121}.
FT   BINDING     335    335       NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
SQ   SEQUENCE   355 AA;  37522 MW;  89D76BEF7E6C841C CRC64;
     MSGGPVLALV GATGAVGTVM ISIINNRETV PWGEIRLIAS ARSAGKKIHV RGEDLTVVEL
     TPEAFDGVDV AMFDVPDEVS ARWAPIAAAR GAVAVDNSGA FRMDDEVPLV VPEVNADRIG
     DRPKGIIANP NCTTLSMMAA IGALHREFGL RELVVASYQA ASGGGQAAID RLRAEVEAVS
     GKQVGERAGD VREALDAAGL PVSDSPFPAP LALNVVPWAG SLKDDGWTSE ELKVRNESRK
     ILGIPDLKVS ATCVRVPVVT THSLAVHAVF ERPVTVGQAH KIFEEQPSVV LVDEPEAQRF
     PTPADVVGGD PTYVGRVRQA LDFPNALDFF VCGDNLRKGA ALNTYEIAEE LAGRL
//

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