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Database: UniProt
Entry: A0A132SLE3_9MYCO
LinkDB: A0A132SLE3_9MYCO
Original site: A0A132SLE3_9MYCO 
ID   A0A132SLE3_9MYCO        Unreviewed;       487 AA.
AC   A0A132SLE3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=NAD-dependent succinate-semialdehyde dehydrogenase {ECO:0000313|EMBL:KWX59899.1};
GN   ORFNames=ASJ79_09375 {ECO:0000313|EMBL:KWX59899.1};
OS   Mycobacterium sp. NAZ190054.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1747766 {ECO:0000313|EMBL:KWX59899.1, ECO:0000313|Proteomes:UP000070146};
RN   [1] {ECO:0000313|EMBL:KWX59899.1, ECO:0000313|Proteomes:UP000070146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAZ190054 {ECO:0000313|EMBL:KWX59899.1,
RC   ECO:0000313|Proteomes:UP000070146};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KWX59899.1}.
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DR   EMBL; LMVQ01000457; KWX59899.1; -; Genomic_DNA.
DR   RefSeq; WP_067960956.1; NZ_LMVQ01000457.1.
DR   AlphaFoldDB; A0A132SLE3; -.
DR   OrthoDB; 6882680at2; -.
DR   Proteomes; UP000070146; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070146}.
FT   DOMAIN          30..481
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        261
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   487 AA;  50348 MW;  9452488D3E1C5146 CRC64;
     MHTADVTADL IAGVDPRHGI LVGGLARTSA STFDVHDPAT GLVIAEVADG APSDATAAAD
     AADRALPVWS ATPPRARADI LRRAFDLMVA QTDRLVALIC AENGKPQADA RAEVAYAADF
     FRWFSEEAVR TDGSYGDSPA GDAVKIVTHR PVGPAALITP WNFPAAMATR KIAPALAAGC
     TVVLKPAAET PLTALAIARL LADAGVPDGV VNVVPTTDAA GVVETLLTDP RVRKVSFTGS
     TAVGRLLLAQ SAERVLNASM ELGGNAPFIV AADADLDAAV AGAMIAKFRG GGQACTAANR
     FYVHADVAEE FTARFGAAIA ALRVGPAVDP ASQIGPLVSA RAAAGVRALL DQAVQEGATI
     AQQADAPEGG WYVAPTLLTD VRPDASILQQ EIFGPLAPVV VWNDEDVLRR WVNDTEYGLA
     AYVYSGRLQT ALRIAASIDA GMVGINRGVV SDPSAPFGGT KQSGLGREGA RDGLREFQET
     QYLSVGM
//
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