ID A0A150LD74_9BACI Unreviewed; 493 AA.
AC A0A150LD74;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN ORFNames=B4135_3462 {ECO:0000313|EMBL:KYD10287.1};
OS Caldibacillus debilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX NCBI_TaxID=301148 {ECO:0000313|EMBL:KYD10287.1, ECO:0000313|Proteomes:UP000075683};
RN [1] {ECO:0000313|EMBL:KYD10287.1, ECO:0000313|Proteomes:UP000075683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4135 {ECO:0000313|EMBL:KYD10287.1,
RC ECO:0000313|Proteomes:UP000075683};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Draft Genome Sequences of Seven Thermophilic Sporeformers 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:KYD10287.1}.
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DR EMBL; LQYT01000119; KYD10287.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150LD74; -.
DR STRING; 301148.B4135_3462; -.
DR PATRIC; fig|301148.3.peg.1503; -.
DR Proteomes; UP000075683; Unassembled WGS sequence.
DR GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic 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 InterPro; IPR010102; Succ_semiAld_DH.
DR NCBIfam; TIGR01780; SSADH; 1.
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}.
FT DOMAIN 28..489
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 264
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
FT ACT_SITE 298
FT /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ SEQUENCE 493 AA; 53982 MW; 709FDB9AE15A997C CRC64;
MEEEKRKEVR WLAYHTVLLN RMYVNGKWVR AKGNQTFPVT NPATGKTIGS VPDGGKEDAR
LAVDAAHAAF PVWSGKTAEE RSYYLRKWHD AILDNKNEIA EILVLEQGKP MKEALGEITY
AASFLLWYAE EAKRIYGETI PASAPDKRIL VFRQPVGVTA AITPWNFPAA MITRKVAPAL
AAGCTVVIKP AEQTPLTALK LAEAAEMAGF PRGVINVVTG NPEEIGAAWL EDPRVRKITF
TGSTEVGKLL MKGAADTVKK ISLELGGHAP VIVFEDADLD LAVQGTILSK FRNAGQTCIC
ANRVYVQESI FEPFVEKLAE ETKKLVVGYG LEPETQIGPL IDESAYLKVK SHIENAVAMG
AKIVCGGNRV NDFEGGYFLE PTVLTDVKDD MKIMKEETFG PVAPVLTFRD MEEVIERAND
TPYGLAAYAF TSNLRTAFLV SERLEYGIVG INDPLPSVAQ APFGGFKESG LGREGGHHGI
DEFLEIKYVS MKL
//
