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Database: UniProt
Entry: Q1LG97_CUPMC
LinkDB: Q1LG97_CUPMC
Original site: Q1LG97_CUPMC 
ID   Q1LG97_CUPMC            Unreviewed;       475 AA.
AC   Q1LG97;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Succinate-semialdehyde dehydrogenase {ECO:0000313|EMBL:ABF10829.1};
DE            EC=1.2.1.16 {ECO:0000313|EMBL:ABF10829.1};
GN   Name=gabD {ECO:0000313|EMBL:ABF10829.1};
GN   OrderedLocusNames=Rmet_3961 {ECO:0000313|EMBL:ABF10829.1};
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OG   Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429}.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF10829.1, ECO:0000313|Proteomes:UP000002429};
RN   [1] {ECO:0000313|Proteomes:UP000002429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC   {ECO:0000313|Proteomes:UP000002429};
RC   PLASMID=Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429};
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986}.
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DR   EMBL; CP000353; ABF10829.1; -; Genomic_DNA.
DR   RefSeq; WP_011518468.1; NC_007974.2.
DR   AlphaFoldDB; Q1LG97; -.
DR   KEGG; rme:Rmet_3961; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_0_4; -.
DR   Proteomes; UP000002429; Plasmid megaplasmid CH34.
DR   GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR   CDD; cd07103; ALDH_F5_SSADH_GabD; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABF10829.1}; Plasmid {ECO:0000313|EMBL:ABF10829.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002429}.
FT   DOMAIN          16..471
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   475 AA;  51543 MW;  8F7278FA3B226F8B CRC64;
     MYQDLALYID GEFIKGGDRR EQDVINPATQ ELLGKLPHAT TADLDRALSA AQRAFETWKK
     TSPLERSQIL RRVAELTRTR AKEIGRDITL DQGKPLAEAV GEVMICAEHA EWHAEECRRI
     YGRVIPPRNP AVRQIVVREP IGVCAAFTPW NFPFNQAIRK IVAALGAGCT LILKGPEDSP
     SAVVALARLF HDAGLPPGVL NIVWGVPSEV STYLIESPIV RKISFTGSVP VGKQLAAMAG
     AHMKRVTMEL GGHSPVLVFG DADIEPAAEM LARFKLRNAG QVCVSPTRFY VQEKAYDKFL
     ARFTEVIGSI KVGNGLDDGT QMGPLAHERR IASMEQFLDD ASHRGGKIVA GGSRIGDKGF
     FFAPTVVTDL PDDAKLMVDE PFGPVAPVTR FKDAEEVLRR ANSLPFGLAS YVFTNSLKTA
     NLVSNGLEAG MVNINHFGMA LAETPFGGIK DSGIGSEGGQ ETFDGYLVTK FITQV
//
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