ID   A0A0K0GBJ3_9FIRM        Unreviewed;       475 AA.
AC   A0A0K0GBJ3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   ORFNames=WH51_08050 {ECO:0000313|EMBL:KKE79440.1};
OS   Bacilli bacterium VT-13-104.
OC   Bacteria; Bacillota; Bacilli.
OX   NCBI_TaxID=1637974 {ECO:0000313|EMBL:KKE79440.1, ECO:0000313|Proteomes:UP000034981};
RN   [1] {ECO:0000313|Proteomes:UP000034981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VT-13-104 {ECO:0000313|Proteomes:UP000034981};
RA   Tetz V., Tetz G.;
RT   "Bacilli bacterium VT-13-104.";
RL   Submitted (APR-2015) 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|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
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:KKE79440.1}.
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DR   EMBL; LAZH01000032; KKE79440.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K0GBJ3; -.
DR   PATRIC; fig|1637974.4.peg.1689; -.
DR   OrthoDB; 9762913at2; -.
DR   Proteomes; UP000034981; Unassembled WGS sequence.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProt.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR   CDD; cd07138; ALDH_CddD_SSP0762; 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; IPR012394; Aldehyde_DH_NAD(P).
DR   PANTHER; PTHR42804; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42804:SF1; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 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|PIRNR:PIRNR036492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034981}.
FT   DOMAIN          13..470
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        279
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   475 AA;  51307 MW;  68FBDAFC1F81B183 CRC64;
     MRKFLKHFIN GEWVESTGTK TVDVINPATE EVIGQISDGT KEDLDKAVAA ARAAFPSFSQ
     TTKEERIDLL NRIADEYENR KNDIVEVITE ELGAPISISE NTHYVLGLSH FRQAAKELES
     FEFTERRGNT VIRKEPIGVS GLITPWNFPT NQPSTKLASA FAAGSTVVLK PSELTPFAAI
     ILAEIFQAVG LPKGVFNLVN GTGEVVGNGI SSHPDIDFVS FTGSGPVGQK ITENAAKNIK
     KVALELGGKS PLIILDDVDM KKAAKIAVTN VVLNSGQVCS AATRTLVPKS KINEFTDAVK
     EVLPNFPFGD PQNATNFFGP LVSEKQYNRV QGYIKKGIEE GATLLIGGTG KPEGLEKGYY
     VKPTVFTNVK NDMVIAQEEI FGPVMSILTY DDLDEAIEIA NDTVYGLAGY VVGEDKEKVR
     KVATSIRAGL INVNGAPFDF AACFGGYKQS GIGREWGAFG IEEYLEIKSV VGMPS
//