ID A0A1Y0C0H9_9MYCO Unreviewed; 482 AA.
AC A0A1Y0C0H9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Putative succinate-semialdehyde dehydrogenase [NADP(+)] 2 {ECO:0000256|ARBA:ARBA00039663};
DE EC=1.2.1.79 {ECO:0000256|ARBA:ARBA00039122};
GN ORFNames=BTO20_08930 {ECO:0000313|EMBL:ART68689.1};
OS Mycobacterium dioxanotrophicus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=482462 {ECO:0000313|EMBL:ART68689.1, ECO:0000313|Proteomes:UP000195331};
RN [1] {ECO:0000313|EMBL:ART68689.1, ECO:0000313|Proteomes:UP000195331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH-06 {ECO:0000313|EMBL:ART68689.1,
RC ECO:0000313|Proteomes:UP000195331};
RA He Y.;
RT "Whole Genome Sequence of 1,4-Dioxane Degrading Bacterium Mycobacterium
RT dioxanotrophicus PH-06.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH +
CC succinate; Xref=Rhea:RHEA:13213, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57706,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.79;
CC Evidence={ECO:0000256|ARBA:ARBA00036722};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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DR EMBL; CP020809; ART68689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0C0H9; -.
DR KEGG; mdx:BTO20_08930; -.
DR OrthoDB; 6882680at2; -.
DR Proteomes; UP000195331; 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 InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
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 PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000195331}.
FT DOMAIN 14..475
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 247
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 482 AA; 50047 MW; 82DF2F2831551695 CRC64;
MIELLNHIDG AWTGGAAAQL VDNNPAFPEQ TVATGTLADH DQLDRAVRAA REAAARWARE
PMHARAAVLS RAADLVDRSA EAWGAELTRE EGKTLAEGIG EVRRAAQILR YYGGAADREA
GAVYSSPRAG EQILVTRKPI GVVAIVTPFN FPIAIPTWKI APALVYGNTV VFKPASVVPV
LAMRLTEALV EAGLPPGVLN LVIAGGAVAS ALAEHPGVDA ISFTGSTAVG RGIAAAAAAR
GVPVQAEMGG KNAAVVLEDA DLDLAAEQVM LGAFRSSGQK CTATSRLIVA DAVADEFLTE
LAIRVKGLEV GDPMQASVAV GPVVNESACR YIKQRTADAV SDGARVVASA EDHQSGSGDG
YFVTPTVLQL PSVQAPLWSE ELFGPVLSVL RASTTEQAFE LANSGDYGLS AAVFTTDLSR
ALAAVDDLDV GVLHVNSESA GADPHVPFGG AKRSGYGPKE QGEAAREFFT HTTTVYLRGG
RP
//
