ID   Q46UZ8_CUPPJ            Unreviewed;       506 AA.
AC   Q46UZ8;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=Aldehyde dehydrogenase (NAD+) {ECO:0000313|EMBL:AAZ63036.1};
DE            EC=1.2.1.3 {ECO:0000313|EMBL:AAZ63036.1};
GN   OrderedLocusNames=Reut_B3678 {ECO:0000313|EMBL:AAZ63036.1};
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198 {ECO:0000313|EMBL:AAZ63036.1};
RN   [1] {ECO:0000313|EMBL:AAZ63036.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 {ECO:0000313|EMBL:AAZ63036.1};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP000091; AAZ63036.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46UZ8; -.
DR   STRING; 264198.Reut_B3678; -.
DR   KEGG; reu:Reut_B3678; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_0_2_4; -.
DR   OrthoDB; 6187633at2; -.
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; 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;  55086 MW;  D87C7E7EF29B130D CRC64;
     MNMAEIAQLG VTNPYKQQYE NYIGGAWVPP AGGEYFEAIT PITGKPFTRV PRSKQEDVDA
     ALDAAHAAKA AWGRTSTTER ANILNRIADR IEANLTLLAV AETIDNGKPV RETMAADLPL
     AVDHFRYFAG CIRAQEGGIS EIDAETIAYH FHEPLGVVGQ IIPWNFPLLM ATWKLAPALA
     AGNCVVLKPA EQTPASILAL MEVIGDLLPP GVVNVINGFG LEAGKPLASS PRISKVAFTG
     ETTTGRLIMQ YASQNLIPVT LELGGKSPNI FFEDVLAADD AYFDKALEGF AMFALNQGEV
     CTCPSRALIQ ESIYDRFMER ALKRVAAIRQ GHPLDKGTMI GAQASAEQLE KILSYIDLGR
     KEGAQCLAGG ERNQFDGDLA GGYYVKPTVF KGHNKMRIFQ EEIFGPVVSV TTFKDEEEAL
     AIANDTLYGL GAGVWTRDGA RAFRMGRGIQ AGRVWTNCYH AYPAHAAFGG YKQSGIGREN
     HRMMLDHYQQ TKNLLVSYSP NALGFF
//