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Database: UniProt/TrEMBL
Entry: A0A0B5ARC6_9BACL
LinkDB: A0A0B5ARC6_9BACL
Original site: A0A0B5ARC6_9BACL 
ID   A0A0B5ARC6_9BACL        Unreviewed;       506 AA.
AC   A0A0B5ARC6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Putative aldehyde dehydrogenase AldA {ECO:0000256|ARBA:ARBA00039869};
DE            EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
GN   ORFNames=JMA_17610 {ECO:0000313|EMBL:AJD91078.1};
OS   Jeotgalibacillus malaysiensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX   NCBI_TaxID=1508404 {ECO:0000313|EMBL:AJD91078.1, ECO:0000313|Proteomes:UP000031449};
RN   [1] {ECO:0000313|EMBL:AJD91078.1, ECO:0000313|Proteomes:UP000031449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D5 {ECO:0000313|EMBL:AJD91078.1,
RC   ECO:0000313|Proteomes:UP000031449};
RA   Yaakop A.S., Chan K.-G., Goh K.M.;
RT   "Complete genome of a marine bacteria Jeotgalibacillus malaysiensis.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00024149};
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP009416; AJD91078.1; -; Genomic_DNA.
DR   RefSeq; WP_039809031.1; NZ_CP009416.1.
DR   AlphaFoldDB; A0A0B5ARC6; -.
DR   STRING; 1508404.JMA_17610; -.
DR   KEGG; jeo:JMA_17610; -.
DR   HOGENOM; CLU_005391_0_2_9; -.
DR   OrthoDB; 9762913at2; -.
DR   BioCyc; JESP1508404:G14D9-11016-MONOMER; -.
DR   Proteomes; UP000031449; Chromosome.
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; cd07116; ALDH_ACDHII-AcoD; 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   PANTHER; PTHR43111; ALDEHYDE DEHYDROGENASE B-RELATED; 1.
DR   PANTHER; PTHR43111:SF1; ALDEHYDE DEHYDROGENASE B-RELATED; 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          27..493
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   506 AA;  56147 MW;  B0860298AA8EDAB5 CRC64;
     MTYANPNTDG SLVNFKEKYD NFIGGEWVAP VKGQYFDNPS PVDGKTFCQI ARSTEEDIEK
     ALDAAHAAKD AWGKTSVTER SVILNKIADR MEENLEMLAV AETWENGKAV RETLNADIPL
     AIDHFRYFAG VIRAQEGTLG EIDHDTVAYH FHEPLGVVGQ IIPWNFPLLM AVWKLAPALA
     AGNCVVLKPA EQTPSSILVL MELVGDLLPK GVVNIVNGFG LEAGKPLASS KRIAKIAFTG
     ETTTGRMIME YASQNLIPVT LELGGKSPNI FFKDIMDQDD EFVDKAVEGL LMFALNQGEV
     CTCPSRALIH EDIYDEFMAR VVKRVKEINT GNPLDPNTMM GAQASTEQME KIQKYLQIGK
     EEGAELVTGG DINKKEGEFA EGYYIQPTIF KGTNDMRIFQ EEIFGPVLSV TTFKTDEEAM
     EIANDTLYGL GAGIWTRNVN TAYRFGRGIQ AGRVWTNCYH QYPAHAAFGG YKMSGIGREN
     HKMMLDHYQQ TKNMLVSYSP KKLGFF
//
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