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Database: UniProt
Entry: J9S9I2_9ACTN
LinkDB: J9S9I2_9ACTN
Original site: J9S9I2_9ACTN 
ID   J9S9I2_9ACTN            Unreviewed;       505 AA.
AC   J9S9I2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Succinate-semialdehyde dehydrogenase {ECO:0000313|EMBL:AFR50616.1};
GN   ORFNames=KTR9_4007 {ECO:0000313|EMBL:AFR50616.1};
OS   Gordonia sp. KTR9.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR50616.1, ECO:0000313|Proteomes:UP000003281};
RN   [1] {ECO:0000313|EMBL:AFR50616.1, ECO:0000313|Proteomes:UP000003281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KTR9 {ECO:0000313|EMBL:AFR50616.1,
RC   ECO:0000313|Proteomes:UP000003281};
RX   PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA   Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA   Indest K.J., Eltis L.D.;
RT   "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT   trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL   Appl. Environ. Microbiol. 78:7798-7800(2012).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP002907; AFR50616.1; -; Genomic_DNA.
DR   RefSeq; WP_014928067.1; NC_018581.1.
DR   AlphaFoldDB; J9S9I2; -.
DR   STRING; 337191.KTR9_4007; -.
DR   KEGG; gor:KTR9_4007; -.
DR   PATRIC; fig|337191.3.peg.4395; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_5_1_11; -.
DR   Proteomes; UP000003281; Chromosome.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd07103; ALDH_F5_SSADH_GabD; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
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.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345}.
FT   DOMAIN          29..497
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   505 AA;  52668 MW;  23000DA88AB45D78 CRC64;
     MTAPAPVTPH NAPEAVSRVN TDLFIGGTWT PAASGERFDV VNPATGDVLA RVADADAVDA
     RHALETAAAH QAGWAATSPR SRSEILYRAH RLIMDRVDGI AAVMTAEMGK PLAEAKGEVA
     YGAEFFRWFA EEAVRIGGDS TTTGDGSHRI VVTRQPVGPC ILITPWNFPL AMGTRKIGPA
     IAAGCTMVLK PAELTPLTTL LLADILVEAG LPPGVLNVVT TSDPSTVVTE WMESGLARKI
     SFTGSTEVGK LLLRQAAGTV MRTSMELGGN APFIVCADAD IPRAVDGLMF AKMRNIGQAC
     TAANRVFVHR SVIDEFTAAF AAKMAGLRVG DGAADNVQVG PLVERAAVEK VSTLVSDAVA
     KGATVVCGGE NPEGPGFFYP PTVLTGVGLD ADLMRTEIFG PVAAIVPFGN AYEPDDPAAD
     DEVIALANDT PWGLVGYLFS QDVDRCARLS AALETGMVGV NTGAVSNPAA PFGGVKESGL
     GREGGRVGLE EFLDMKYTAT PIPLR
//
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