ID   ASTD_COLP3              Reviewed;         492 AA.
AC   Q488Y0;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=CPS_0634;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ28301.1; -; Genomic_DNA.
DR   RefSeq; YP_267384.1; -.
DR   GeneID; 3522560; -.
DR   GenomeReviews; CP000083_GR; CPS_0634.
DR   KEGG; cps:CPS_0634; -.
DR   NMPDR; fig|167879.3.peg.377; -.
DR   TIGR; CPS_0634; -.
DR   HOGENOM; Q488Y0; -.
DR   OMA; Q488Y0; TNIAELP.
DR   BioCyc; CPSY167879:CPS_0634-MON; -.
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; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   InterPro; IPR017649; SuccinylGlu_semiald_DH_AstD.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
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    492       N-succinylglutamate 5-semialdehyde
FT                                dehydrogenase.
FT                                /FTId=PRO_0000262398.
FT   NP_BIND     225    230       NAD (By similarity).
FT   ACT_SITE    248    248       By similarity.
FT   ACT_SITE    282    282       By similarity.
SQ   SEQUENCE   492 AA;  52600 MW;  7740FDE2F7F1083F CRC64;
     MSHANPVQFI NGQWQAGLGH DVSSSNPARN EVIWQGKTAS KDQVNDAVLS ARQAFESWAN
     ISLEARVAVV TKFAELLAEN KDALATTIAL ETGKPKWETT GEAGAMVAKV AISLKAYNER
     TGTVENPMPG AKAFIRHKPH GVVAIFGPYN FPGHLPNGHI VPALIAGNTI VFKPSELTPR
     VAQEMLKLWE QAGLPNGVIN LVQGEVETGK ALASHKLIDG LFFTGSSNTG HILHEQFAGQ
     PGKILALEMG GNNPLVVKDV SDIDAVVHDI VQSAFVTTGQ RCTCARRLFI EANEQGDAIL
     ARLIEVTKNL TIGYYDDEAQ PFMGSMISEK AALSLVDAQA KLLALGAKSV LDLKHLEVGT
     GFVSPGIIDV SDIIADIPDE EYFGPLVKLY RYNDFDKAID EANNTGFGLS AGLLSDSEAS
     YNHFFTRIRA GIVNWNKPIT GASSAAPFGG IGASGNHRAS AFYAADYCAY PIASVEAEKV
     SLPETLTPGM KF
//