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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//