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Database: UniProt
Entry: A0A150LCL7_9BACI
LinkDB: A0A150LCL7_9BACI
Original site: A0A150LCL7_9BACI 
ID   A0A150LCL7_9BACI        Unreviewed;       483 AA.
AC   A0A150LCL7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   ORFNames=B4102_2362 {ECO:0000313|EMBL:KYD10078.1};
OS   Heyndrickxia sporothermodurans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX   NCBI_TaxID=46224 {ECO:0000313|EMBL:KYD10078.1, ECO:0000313|Proteomes:UP000075666};
RN   [1] {ECO:0000313|EMBL:KYD10078.1, ECO:0000313|Proteomes:UP000075666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4102 {ECO:0000313|EMBL:KYD10078.1,
RC   ECO:0000313|Proteomes:UP000075666};
RA   Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA   Eijlander R.T., Kuipers O.P.;
RT   "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated from
RT   Foods.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492}.
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:KYD10078.1}.
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DR   EMBL; LQYN01000018; KYD10078.1; -; Genomic_DNA.
DR   RefSeq; WP_066228014.1; NZ_LQYN01000018.1.
DR   AlphaFoldDB; A0A150LCL7; -.
DR   STRING; 46224.B4102_2362; -.
DR   PATRIC; fig|46224.3.peg.1372; -.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000075666; 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   GO; GO:0006081; P:cellular aldehyde metabolic process; 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; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075666}.
FT   DOMAIN          16..477
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        252
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   483 AA;  52648 MW;  09EF6DF39EFA0D96 CRC64;
     MLIGQKEKGI FINGEWREAY SGTYRSITNP ATLEKLTEIS YGGKEDALEA IEEAKAAFSA
     WSKRTARERS RFLYKAYEKM LENKEQLAQI LTSEQGKPLT EARTEIESAA SYLLWYAEEA
     NRVYGEIIPP SNANKRSLVI PQAIGVIAAI TPWNFPASMV TRKLGPSLAA GCTVVLKPAS
     QTPLTAMAIV KIFEEVGLPK GVLNLVAGDA RAIGDALTQS PDVRLITFTG STEVGRDLMK
     NSAQHIKKLS LELGGHAPIL VLEDANLETA VDLTIASKFR NCGQTCICAN RVYVHQNIAE
     EFIEKLSAKV RNLKIGNGNE DSTVIGPMID RNAVEKVTEH VEDALKHGAS IVAGGKEWNG
     GLGGHFYEPT VLVDVNDQMK VMNEETFGPV LPIETFDLLE EVIEKANQLP YGLAAYVMTE
     STNRLFQLTE ALEYGIIGVN DVFPATAEAP FGGIKESGFG KEGGKEGILE FVEMKYVSIG
     ITK
//
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