ID   ASTD_BURXL              Reviewed;         487 AA.
AC   Q141D3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=N-succinylglutamate 5-semialdehyde dehydrogenase;
DE            EC=1.2.1.71;
DE   AltName: Full=Succinylglutamic semialdehyde dehydrogenase;
DE            Short=SGSD;
GN   Name=astD; OrderedLocusNames=Bxeno_A1518; ORFNames=Bxe_A2920;
OS   Burkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the NAD-dependent reduction of
CC       succinylglutamate semialdehyde into succinylglutamate (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: N-succinyl-L-glutamate 5-semialdehyde + NAD(+)
CC       + H(2)O = N-succinyl-L-glutamate + NADH.
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC       pathway; L-glutamate and succinate from L-arginine: step 4/5.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD
CC       subfamily.
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DR   EMBL; CP000270; ABE30056.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_558108.1; -.
DR   GeneID; 4004449; -.
DR   GenomeReviews; CP000270_GR; Bxeno_A1518.
DR   KEGG; bxe:Bxe_A2920; -.
DR   HOGENOM; Q141D3; -.
DR   OMA; Q141D3; HESETAF.
DR   GO; GO:0043824; F:succinylglutamate-semialdehyde dehydrogenas...; IEA:EC.
DR   GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01174; -; 1.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   InterPro; IPR017649; SuccinylGlu_semiald_DH_AstD.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   TIGRFAMs; TIGR03240; arg_catab_astD; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Arginine metabolism; Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    487       N-succinylglutamate 5-semialdehyde
FT                                dehydrogenase.
FT                                /FTId=PRO_0000262393.
FT   NP_BIND     221    226       NAD (By similarity).
FT   ACT_SITE    244    244       By similarity.
FT   ACT_SITE    278    278       By similarity.
SQ   SEQUENCE   487 AA;  51705 MW;  B6578808C1255D64 CRC64;
     MSELFIGGEW AAGTGPAFAS RNPGTGAAVW EGNSASADDV DRAVRSARRA FAAWSASSVD
     ERCAVVRRFA ALVTERKEAL AEAIGRETGK PLWEARTEAA SMAAKVEISI QAYNERTGEK
     RSAMADGTAV LRHRPHGVVA VFGPYNFPGH LPNGHIVPAL IAGNAVVFKP SELAPGVAAL
     TVQIWRDAGL PAGVLNLVQG EKDTGIALAN HRQIDGLFFT GSSDTGTLLH KQFGGRPEIV
     LALEMGGNNP LVIGPVADVD AAVHHTIQSA FLSAGQRCTC ARRIFVPNDA AGDRFLERFT
     EVTSRITVGE YNADPQPFMG AVISVRAASR LVAAQERLLA DGAKALLKME QRDPKLGFVT
     PAILDVTNVA NRPDEEHFGP LAQIIRYGSF NEALEQANDT EFGLSAGLLA DDEALWAHFQ
     RTIRAGIVNW NRPTNGASSG APFGGPGRSG NHRPSAYYAA DYCAFPMASV ESAQLQMPAS
     VSPGLQF
//