ID   A0A0H4P4R0_9BACI        Unreviewed;       501 AA.
AC   A0A0H4P4R0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=aldehyde dehydrogenase (NAD(+)) {ECO:0000256|ARBA:ARBA00024226};
DE            EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
GN   ORFNames=BSM4216_2183 {ECO:0000313|EMBL:AKP47428.1};
OS   Bacillus smithii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1479 {ECO:0000313|EMBL:AKP47428.1, ECO:0000313|Proteomes:UP000036353};
RN   [1] {ECO:0000313|EMBL:AKP47428.1, ECO:0000313|Proteomes:UP000036353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4216 {ECO:0000313|EMBL:AKP47428.1,
RC   ECO:0000313|Proteomes:UP000036353};
RA   Bosma E.F., Koehorst J.J., van Hijum S.A.F.T., Renckens B., Vriesendorp B.,
RA   van de Weijer A.H.P., Schaap P.J., de Vos W.M., van der Oost J.,
RA   van Kranenburg R.;
RT   "Complete genome sequence of thermophilic Bacillus smithii type strain DSM
RT   4216T.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP012024; AKP47428.1; -; Genomic_DNA.
DR   RefSeq; WP_048623489.1; NZ_CP012024.1.
DR   AlphaFoldDB; A0A0H4P4R0; -.
DR   STRING; 1479.BSM4216_2183; -.
DR   KEGG; bsm:BSM4216_2183; -.
DR   eggNOG; COG1012; Bacteria.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000036353; Chromosome.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   CDD; cd07131; ALDH_AldH-CAJ73105; 1.
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   InterPro; IPR044638; ALDH7A1-like.
DR   PANTHER; PTHR43521; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43521:SF1; ALPHA-AMINOADIPIC SEMIALDEHYDE DEHYDROGENASE; 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}.
FT   DOMAIN          19..484
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   501 AA;  54462 MW;  75C214BD0CE3E899 CRC64;
     MANIQLSGEK VINYINGEWT SSKKAKFVTI VNPADGQPIG EVLQSSKEDV DLAVQAAKQA
     QKKWSRVPAP QRAQYLYRVG ELLKERKEKL ASILTQEMGK VIEEARGEVQ EGIDMAFYMA
     GEGRRLFGQT TTSELNDKFA MSIRVPIGVV GIITPWNFPI AIATWKSFPA IVAGNTVIWK
     PATETPLMAR ELVKILDEAG LPKGVMNLVC GSGSEVGSAI VEHPDIDVIS FTGSNEVGRT
     IAEKGGKLLK RVSLEMGGKN AVIVMEDADL SLAVEGIIWS AFGTSGQRCT ACSRVIVHEN
     VKAELEKRLL QEMKKLTIGN GLNEDVKIGP VINKSALKKI HEFVEMGQKE GADLLAGGYI
     VKEKNLDGGN YYAPTLFTNV RPDMRIAQEE IFGPVLSIIP VRSFEEAVEV NNSVAYGLSS
     SIYTRNVNRV FAAQRDLDTG IVYINAGTTG AEIHLPFGGT KGTGNGHRDS GVAALDVFTE
     WKSVYVDFSG KLQRAQIDVE S
//