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Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase)

 DHAS_LEPIN              Reviewed;         349 AA.
P41394;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
06-DEC-2002, sequence version 2.
07-JUN-2017, entry version 115.
RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121};
Short=ASA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121};
Short=ASADH {ECO:0000255|HAMAP-Rule:MF_02121};
EC=1.2.1.11 {ECO:0000255|HAMAP-Rule:MF_02121};
AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121};
Name=asd {ECO:0000255|HAMAP-Rule:MF_02121}; OrderedLocusNames=LB_355;
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai
(strain 56601).
Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
NCBI_TaxID=189518;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Serogroup Icterohaemorrhagiae;
PubMed=1348268; DOI=10.1099/00221287-138-1-47;
Baril C., Richaud C., Fourni E., Baranton G., Saint-Girons I.;
"Cloning of dapD, aroD and asd of Leptospira interrogans serovar
icterohaemorrhagiae, and nucleotide sequence of the asd gene.";
J. Gen. Microbiol. 138:47-53(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=56601;
PubMed=12712204; DOI=10.1038/nature01597;
Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H.,
Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F.,
Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F.,
Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W.,
Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A.,
Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z.,
Xu J.-G., Zhao G.-P.;
"Unique physiological and pathogenic features of Leptospira
interrogans revealed by whole-genome sequencing.";
Nature 422:888-893(2003).
-!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-
semialdehyde (L-ASA) by the reductive dephosphorylation of L-
aspartyl-4-phosphate. {ECO:0000255|HAMAP-Rule:MF_02121}.
-!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + phosphate +
NADP(+) = L-4-aspartyl phosphate + NADPH. {ECO:0000255|HAMAP-
Rule:MF_02121}.
-!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
{ECO:0000255|HAMAP-Rule:MF_02121}.
-!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
novo pathway; L-homoserine from L-aspartate: step 2/3.
{ECO:0000255|HAMAP-Rule:MF_02121}.
-!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
threonine from L-aspartate: step 2/5. {ECO:0000255|HAMAP-
Rule:MF_02121}.
-!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02121}.
-!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase
family. {ECO:0000255|HAMAP-Rule:MF_02121}.
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EMBL; S92223; AAB21985.1; -; Genomic_DNA.
EMBL; M77500; AAA25262.1; -; Genomic_DNA.
EMBL; AE010301; AAN51914.1; -; Genomic_DNA.
PIR; A44846; A44846.
RefSeq; NP_714899.1; NC_004343.2.
RefSeq; WP_000092012.1; NC_004343.2.
ProteinModelPortal; P41394; -.
SMR; P41394; -.
STRING; 189518.LB_355; -.
EnsemblBacteria; AAN51914; AAN51914; LB_355.
GeneID; 1153914; -.
KEGG; lil:LB_355; -.
PATRIC; fig|189518.3.peg.4670; -.
eggNOG; ENOG4107QK3; Bacteria.
eggNOG; COG0136; LUCA.
HOGENOM; HOG000013358; -.
InParanoid; P41394; -.
KO; K00133; -.
OMA; CEEEMKM; -.
UniPathway; UPA00034; UER00016.
UniPathway; UPA00050; UER00463.
UniPathway; UPA00051; UER00464.
Proteomes; UP000001408; Chromosome II.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0006531; P:aspartate metabolic process; IEA:InterPro.
GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
HAMAP; MF_02121; ASADH; 1.
InterPro; IPR000319; Asp-semialdehyde_DH_CS.
InterPro; IPR005676; Asp_semi-ald_DH_pep-lack.
InterPro; IPR012080; Asp_semialdehyde_DH.
InterPro; IPR016040; NAD(P)-bd_dom.
InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
Pfam; PF01118; Semialdhyde_dh; 1.
Pfam; PF02774; Semialdhyde_dhC; 1.
SMART; SM00859; Semialdhyde_dh; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR00978; asd_EA; 1.
PROSITE; PS01103; ASD; 1.
3: Inferred from homology;
Amino-acid biosynthesis; Complete proteome;
Diaminopimelate biosynthesis; Lysine biosynthesis;
Methionine biosynthesis; NADP; Oxidoreductase; Reference proteome;
Threonine biosynthesis.
CHAIN 1 349 Aspartate-semialdehyde dehydrogenase.
/FTId=PRO_0000141380.
NP_BIND 12 15 NADP. {ECO:0000255|HAMAP-Rule:MF_02121}.
NP_BIND 39 40 NADP. {ECO:0000255|HAMAP-Rule:MF_02121}.
NP_BIND 178 179 NADP. {ECO:0000255|HAMAP-Rule:MF_02121}.
NP_BIND 326 327 NADP. {ECO:0000255|HAMAP-Rule:MF_02121}.
ACT_SITE 148 148 Acyl-thioester intermediate.
{ECO:0000255|HAMAP-Rule:MF_02121}.
ACT_SITE 241 241 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_02121}.
BINDING 113 113 Phosphate. {ECO:0000255|HAMAP-
Rule:MF_02121}.
BINDING 175 175 Substrate. {ECO:0000255|HAMAP-
Rule:MF_02121}.
BINDING 201 201 Substrate. {ECO:0000255|HAMAP-
Rule:MF_02121}.
BINDING 204 204 Phosphate. {ECO:0000255|HAMAP-
Rule:MF_02121}.
BINDING 234 234 Substrate. {ECO:0000255|HAMAP-
Rule:MF_02121}.
CONFLICT 31 31 V -> I (in Ref. 1; AAB21985/AAA25262).
{ECO:0000305}.
SEQUENCE 349 AA; 38018 MW; 1DB092D05CE66254 CRC64;
MSRVKVAVLG ATGSVGQRFI QLLDHHPFFE VTHLCASENS AGKTYGEVMK TRWKISSDIP
AYAKNLVITT PDPAKTKDVV LAFSGLDSNV AGEVEKNYAN AGIHIISNSK NHRMDPTVPI
LSAEVNSSHL EVLTSQKTKG KIITNSNCTI MGVTISLKPL LDRFGIESVM LFSMQAISGA
GYPGVPTMDI LGNVIPHIGG EEEKAEIEPL KCLGKVENGK ILHADFSISA HCNRVPVFDG
HTVCVSVKFK KKPSREEIIS SWKDFSGEPQ TLGLPLAPNP VILFREEEDR PQPRLDLDTG
KGMTTVIGRL RPDPILDWKY VVLSHNTIRG AAGAALLNAE LLYKKKFLG


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