ID   DHAS_MYCTU              Reviewed;         345 AA.
AC   P0A542; P47730; P97049;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Aspartate-semialdehyde dehydrogenase;
DE            Short=ASA dehydrogenase;
DE            Short=ASADH;
DE            EC=1.2.1.11;
GN   Name=asd; OrderedLocusNames=Rv3708c, MT3811; ORFNames=MTV025.056c;
OS   Mycobacterium tuberculosis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=1773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Gilker J.M., Jucker M.T.;
RT   "Mycobacterium tuberculosis ask-alpha, ask-beta and asd genes.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   MEDLINE=22206494; PubMed=12218036;
RX   DOI=10.1128/JB.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
RA   Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA   Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA   Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA   Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + phosphate +
CC       NADP(+) = L-4-aspartyl phosphate + NADPH.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; tetrahydrodipicolinate from L-aspartate: step 2/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 2/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 2/5.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase
CC       family.
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DR   EMBL; U90239; AAB49996.1; -; Genomic_DNA.
DR   EMBL; BX842583; CAA18030.1; -; Genomic_DNA.
DR   EMBL; AE000516; AAK48179.1; -; Genomic_DNA.
DR   PIR; E70794; E70794.
DR   RefSeq; NP_218225.1; -.
DR   RefSeq; NP_338365.1; -.
DR   PDB; 2GUL; Model; -; A=1-345.
DR   PDBsum; 2GUL; -.
DR   GeneID; 885118; -.
DR   GeneID; 926449; -.
DR   GenomeReviews; AE000516_GR; MT3811.
DR   GenomeReviews; AL123456_GR; Rv3708c.
DR   KEGG; mtc:MT3811; -.
DR   KEGG; mtu:Rv3708c; -.
DR   TIGR; MT3811; -.
DR   TubercuList; Rv3708c; -.
DR   HOGENOM; P0A542; -.
DR   OMA; P0A542; LELWLCG.
DR   BRENDA; 1.2.1.11; 809.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:EC.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:InterPro.
DR   InterPro; IPR000319; Asp-semialdehyde_DH_CS.
DR   InterPro; IPR012080; Asp_semialdehyde_DH.
DR   InterPro; IPR005986; Asp_semialdehyde_DH_bac.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_C.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   PIRSF; PIRSF000148; ASA_dh; 1.
DR   TIGRFAMs; TIGR01296; asd_B; 1.
DR   PROSITE; PS01103; ASD; 1.
PE   3: Inferred from homology;
KW   3D-structure; Amino-acid biosynthesis; Complete proteome;
KW   Diaminopimelate biosynthesis; Lysine biosynthesis; NADP;
KW   Oxidoreductase.
FT   CHAIN         1    345       Aspartate-semialdehyde dehydrogenase.
FT                                /FTId=PRO_0000141383.
FT   ACT_SITE    130    130       Acyl-thioester intermediate (By
FT                                similarity).
SQ   SEQUENCE   345 AA;  36230 MW;  C886DDB63D03E25D CRC64;
     MGLSIGIVGA TGQVGQVMRT LLDERDFPAS AVRFFASARS QGRKLAFRGQ EIEVEDAETA
     DPSGLDIALF SAGSAMSKVQ APRFAAAGVT VIDNSSAWRK DPDVPLVVSE VNFERDAHRR
     PKGIIANPNC TTMAAMPVLK VLHDEARLVR LVVSSYQAVS GSGLAGVAEL AEQARAVIGG
     AEQLVYDGGA LEFPPPNTYV APIAFNVVPL AGSLVDDGSG ETDEDQKLRF ESRKILGIPD
     LLVSGTCVRV PVFTGHSLSI NAEFAQPLSP ERARELLDGA TGVQLVDVPT PLAAAGVDES
     LVGRIRRDPG VPDGRGLALF VSGDNLRKGA ALNTIQIAEL LTADL
//