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

 Q2GI82_EHRCR            Unreviewed;       336 AA.
Q2GI82;
21-MAR-2006, integrated into UniProtKB/TrEMBL.
21-MAR-2006, sequence version 1.
25-OCT-2017, entry version 93.
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:ABD44616.1};
OrderedLocusNames=ECH_0016 {ECO:0000313|EMBL:ABD44616.1};
Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
Anaplasmataceae; Ehrlichia.
NCBI_TaxID=205920 {ECO:0000313|EMBL:ABD44616.1, ECO:0000313|Proteomes:UP000008320};
[1] {ECO:0000313|EMBL:ABD44616.1, ECO:0000313|Proteomes:UP000008320}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC CRL-10679 / Arkansas {ECO:0000313|Proteomes:UP000008320};
PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S.,
Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N.,
Nelson W., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.,
Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M., Haft D.H.,
Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F.,
Forberger H., Halpin R., Mulligan S., Robinson J., White O.,
Rikihisa Y., Tettelin H.;
"Comparative genomics of emerging human ehrlichiosis agents.";
PLoS Genet. 2:208-222(2006).
-!- 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}.
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EMBL; CP000236; ABD44616.1; -; Genomic_DNA.
RefSeq; WP_006010406.1; NC_007799.1.
ProteinModelPortal; Q2GI82; -.
STRING; 205920.ECH_0016; -.
EnsemblBacteria; ABD44616; ABD44616; ECH_0016.
KEGG; ech:ECH_0016; -.
eggNOG; ENOG4105CM3; Bacteria.
eggNOG; COG0136; LUCA.
HOGENOM; HOG000013357; -.
KO; K00133; -.
OMA; CEEEMKM; -.
OrthoDB; POG091H00EF; -.
UniPathway; UPA00034; UER00016.
UniPathway; UPA00050; UER00463.
UniPathway; UPA00051; UER00464.
Proteomes; UP000008320; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
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: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; IPR012080; Asp_semialdehyde_DH.
InterPro; IPR005986; Asp_semialdehyde_DH_beta.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; TIGR01296; asd_B; 1.
PROSITE; PS01103; ASD; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121};
Complete proteome {ECO:0000313|Proteomes:UP000008320};
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,
ECO:0000313|EMBL:ABD44616.1};
Reference proteome {ECO:0000313|Proteomes:UP000008320};
Threonine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02121}.
DOMAIN 4 119 Semialdhyde_dh.
{ECO:0000259|SMART:SM00859}.
NP_BIND 11 14 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
NP_BIND 39 40 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
NP_BIND 160 161 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
ACT_SITE 130 130 Acyl-thioester intermediate.
{ECO:0000256|HAMAP-Rule:MF_02121}.
ACT_SITE 242 242 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 99 99 Phosphate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 157 157 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 235 235 Substrate. {ECO:0000256|HAMAP-
Rule:MF_02121}.
BINDING 315 315 NADP. {ECO:0000256|HAMAP-Rule:MF_02121}.
SEQUENCE 336 AA; 37203 MW; 5BB8EE1113FBC6EB CRC64;
MSYKIAVVGA TGNVGRVILN ILASRSFPAK EVVALASKKS IGKKLSYGDE VLESQDLDSY
NFTNTDIAIF SAGSSISQQY ARTAANKGCI IIDNTSLFRM EDEIPLVVPE INPEDIAQYY
KHNIIANPNC STIQMLLALN PLHKISKIKR VVVSTYQSVS GAGKSAMDEL YSQTKGTFMN
QNIAPKQFTK RIAFNCIPHI DVFMEDGSTK EEWKMAVETK KILDNNIEVS ATCVRVPVFV
SHSESLNVEF LSEISEEEAY EALENAPGVI ILDRREDGGY ATPLDSVHED EVYVSRLRKD
NTVKHGLNMW LVSDNLRKGA ALNAVQIAEI LVNDYL


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