(data stored in ACNUC7421 zone)

SWISSPROT: ASTD1_PSEHT

ID   ASTD1_PSEHT             Reviewed;         489 AA.
AC   Q3IFT7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 86.
DE   RecName: Full=N-succinylglutamate 5-semialdehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01174};
DE            EC=1.2.1.71 {ECO:0000255|HAMAP-Rule:MF_01174};
DE   AltName: Full=Succinylglutamic semialdehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01174};
DE            Short=SGSD 1 {ECO:0000255|HAMAP-Rule:MF_01174};
GN   Name=astD1 {ECO:0000255|HAMAP-Rule:MF_01174};
GN   OrderedLocusNames=PSHAa0196;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Catalyzes the NAD-dependent reduction of
CC       succinylglutamate semialdehyde into succinylglutamate.
CC       {ECO:0000255|HAMAP-Rule:MF_01174}.
CC   -!- CATALYTIC ACTIVITY: N-succinyl-L-glutamate 5-semialdehyde + NAD(+)
CC       + H(2)O = N-succinyl-L-glutamate + NADH. {ECO:0000255|HAMAP-
CC       Rule:MF_01174}.
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC       pathway; L-glutamate and succinate from L-arginine: step 4/5.
CC       {ECO:0000255|HAMAP-Rule:MF_01174}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01174}.
DR   EMBL; CR954246; CAI85299.1; -; Genomic_DNA.
DR   RefSeq; WP_011326914.1; NC_007481.1.
DR   ProteinModelPortal; Q3IFT7; -.
DR   SMR; Q3IFT7; -.
DR   STRING; 326442.PSHAa0196; -.
DR   EnsemblBacteria; CAI85299; CAI85299; PSHAa0196.
DR   KEGG; pha:PSHAa0196; -.
DR   PATRIC; fig|326442.8.peg.189; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271506; -.
DR   KO; K06447; -.
DR   OMA; NKQLTGA; -.
DR   OrthoDB; POG091H03EI; -.
DR   UniPathway; UPA00185; UER00282.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0043824; F:succinylglutamate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019545; P:arginine catabolic process to succinate; IEA:UniProtKB-UniPathway.
DR   CDD; cd07095; ALDH_SGSD_AstD; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   HAMAP; MF_01174; Aldedh_AstD; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR017649; SuccinylGlu_semiald_DH_AstD.
DR   PANTHER; PTHR11699:SF231; PTHR11699:SF231; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 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;
DR   PRODOM; Q3IFT7.
DR   SWISS-2DPAGE; Q3IFT7.
KW   Arginine metabolism; Complete proteome; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    489       N-succinylglutamate 5-semialdehyde
FT                                dehydrogenase 1.
FT                                /FTId=PRO_0000262412.
FT   NP_BIND     223    228       NAD. {ECO:0000255|HAMAP-Rule:MF_01174}.
FT   ACT_SITE    246    246       {ECO:0000255|HAMAP-Rule:MF_01174}.
FT   ACT_SITE    280    280       {ECO:0000255|HAMAP-Rule:MF_01174}.
SQ   SEQUENCE   489 AA;  52132 MW;  CA361C82827678A9 CRC64;
     MTHPAQFING QWSQGQGTEF SSVNPANNNV IFQANSATAE QVDAAVSAAR EAFYAWADKT
     FAERLEIVKA FAAQLKENSE ELAITIAQET GKPLWETRTE AGAMVGKIAI SEKAFLERTG
     DVENAMPLGR AMIRHKPHGV VAVFGPYNFP GHLPNGHIVP ALLAGNTVIF KPSELTPKVA
     ELTLKLWEKA GLPAGVINLV QGEVATGKAL AAHKGIDGLF FTGSSRTGHI LHEQFAGQPG
     KILALEMGGN NPLIITDVED TKAVVHDIIQ SAFISSGQRC TCARKLFLPT GSKGDVILER
     LITATKAIKV GNYDDADQPF MGSMISSAAA AGMVKAQNEL VELGAQVLVE LEHTVNTGFV
     TPGIIECTNI SDFPDEEHFG PLLKVFRFDD FDQAIDKAND TSFGLSAGLL SDSAADYEHF
     LRRIRAGIVN WNRPITGASS AAPFGGIGAS GNHRASAYYA ADYCAYPVAS VELEKVAMPA
     TLSPGLKID
//

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