ID   GABD1_MYCLE             Reviewed;         457 AA.
AC   O69497;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 55.
DE   RecName: Full=Succinate-semialdehyde dehydrogenase [NADP+];
DE            Short=SSADH;
DE            Short=SSDH;
DE            EC=1.2.1.16;
GN   Name=gabD1; OrderedLocusNames=ML2573; ORFNames=MLCB1883.11c;
OS   Mycobacterium leprae.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=1769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   MEDLINE=21128732; PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Catalyzes the NADP(+)-dependent oxidation of succinate
CC       semialdehyde to succinate. It is believed to be the main source of
CC       succinate semialdehyde dehydrogenase activity in Mycobacterium (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Succinate semialdehyde + NAD(P)(+) + H(2)O =
CC       succinate + NAD(P)H.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; AL022486; CAA18560.1; -; Genomic_DNA.
DR   EMBL; AL583926; CAC32105.1; -; Genomic_DNA.
DR   PIR; T44871; T44871.
DR   RefSeq; NP_302648.1; -.
DR   HSSP; P05091; 1O04.
DR   GeneID; 910883; -.
DR   GenomeReviews; AL450380_GR; ML2573.
DR   KEGG; mle:ML2573; -.
DR   NMPDR; fig|272631.1.peg.1520; -.
DR   Leproma; ML2573; -.
DR   HOGENOM; O69497; -.
DR   OMA; O69497; VPQSALY.
DR   BioCyc; MLEP272631:ML2573-MON; -.
DR   BRENDA; 1.2.1.16; 808.
DR   GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P...; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; NADP; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN         1    457       Succinate-semialdehyde dehydrogenase
FT                                [NADP+].
FT                                /FTId=PRO_0000310703.
FT   NP_BIND     209    214       NAD or NADP (By similarity).
FT   ACT_SITE    231    231       By similarity.
FT   ACT_SITE    265    265       By similarity.
SQ   SEQUENCE   457 AA;  48879 MW;  1EEF6444A6DD13BD CRC64;
     MSIATINPAT GETVKTFTPT TQDEVEDAIA RAYARFDNYR HTTFTQRAKW ANATADLLEA
     EANQSAALMT LEMGKTLQSA KDEAMKCAKG FRYYAEKAET LLADEPAEAA AVGASKALAR
     YQPLGVVLAV MPWNFPLWQT VRFAAPALMA GNVGLLKHAS NVPQCALYLA DVIARGGFPE
     DCFQTLLISA NGVEAILRDP RVAAATLTGS EPAGQAVGAI AGNEIKPTVL ELGGSDPFIV
     MPSADLDAAV ATAVTGRVQN NGQSCIAAKR FIAHADIYDE FVEKFVARME TLRVGDPTDP
     DTDVGPLATE SGRAQVEQQV DAAAAAGAVI RCGGKRPDRP GWFYPPTVIT DITKDMALYT
     DEVFGPVASV YCATNIDDAI EIANATPFGL GSNAWTQNES EQRHFIDNIV AGQVFINGMT
     VSYPELPFGG IKRSGYGREL STHGIREFCN IKTVWIA
//