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Database: UniProt
Entry: A0A2T4U2C2_9BACI
LinkDB: A0A2T4U2C2_9BACI
Original site: A0A2T4U2C2_9BACI 
ID   A0A2T4U2C2_9BACI        Unreviewed;       506 AA.
AC   A0A2T4U2C2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Putative aldehyde dehydrogenase AldA {ECO:0000256|ARBA:ARBA00039869};
DE            EC=1.2.1.3 {ECO:0000256|ARBA:ARBA00024226};
GN   ORFNames=C6Y45_15895 {ECO:0000313|EMBL:PTL37550.1};
OS   Alkalicoccus saliphilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalicoccus.
OX   NCBI_TaxID=200989 {ECO:0000313|EMBL:PTL37550.1, ECO:0000313|Proteomes:UP000240509};
RN   [1] {ECO:0000313|EMBL:PTL37550.1, ECO:0000313|Proteomes:UP000240509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6AG {ECO:0000313|EMBL:PTL37550.1,
RC   ECO:0000313|Proteomes:UP000240509};
RA   Zhao B.;
RT   "Alkalicoccus saliphilus sp. nov., isolated from a mineral pool.";
RL   Submitted (MAR-2018) 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}.
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:PTL37550.1}.
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DR   EMBL; PZJJ01000044; PTL37550.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4U2C2; -.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000240509; 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   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          32..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;  56040 MW;  E4DC45125A719384 CRC64;
     MKYAVPNSEG SVVQFREKYD NYIGGKFQPP ANGEYFDNVT PVTGKAFTKI ARSSKEDIES
     ALDAAHEAKA DWGMMSVTDR ANILNKIADR MEANLEKLAV AETWENGKAV RETLAADIPL
     AIDHYRYFAS AIRTQEGGIS QIDKDTVAYH FHEPVGVVGQ IIPWNFPLLM AAWKIAPALA
     GGNCIVLKPA EQTPSSIFVW LELIEDLLPP GVLNVVSGFG VEAGKPLASN PRIDKIAFTG
     ETTTGRLIMQ YASENIIPVT LELGGKSPNL FFEDVMQQDD SYLDKAFEGF AMFALNQGEV
     CTCPSRALIQ ESIYDKFMEK AVERVKKIKV GDPLDTETMM GAQASKEQFD KILSYLDIGK
     QEGAKLLCGG ERAELEGHLS GGYYVQPTIF EGHNKMRIFQ EEIFGPVLSV TSFKDKEEAL
     ETANDTLYGL GAGLWTRNVN TAYHFGRAIQ SGRVWTNCFH DYPAHAAFGG YKKSGIGREN
     HLMMLSHYQQ TKNLLVSYSE EPKGFF
//
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