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Database: UniProt
Entry: G7CKH1_MYCT3
LinkDB: G7CKH1_MYCT3
Original site: G7CKH1_MYCT3 
ID   G7CKH1_MYCT3            Unreviewed;       455 AA.
AC   G7CKH1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Betaine-aldehyde dehydrogenase {ECO:0000313|EMBL:EHI11681.1};
GN   ORFNames=KEK_12318 {ECO:0000313|EMBL:EHI11681.1};
OS   Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP
OS   105390 / JCM 6362 / NCTC 10409 / 316) (Mycobacterium thermoresistibile).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1078020 {ECO:0000313|EMBL:EHI11681.1, ECO:0000313|Proteomes:UP000004915};
RN   [1] {ECO:0000313|EMBL:EHI11681.1, ECO:0000313|Proteomes:UP000004915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 /
RC   316 {ECO:0000313|Proteomes:UP000004915};
RG   Tuberculosis Structural Genomics Consortium;
RA   Ioerger T.R.;
RL   Submitted (NOV-2011) 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   -!- 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:EHI11681.1}.
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DR   EMBL; AGVE01000046; EHI11681.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7CKH1; -.
DR   PATRIC; fig|1078020.3.peg.2419; -.
DR   eggNOG; COG1012; Bacteria.
DR   Proteomes; UP000004915; Unassembled WGS sequence.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProt.
DR   GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   PANTHER; PTHR42804; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42804:SF1; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004915}.
FT   DOMAIN          3..451
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   455 AA;  47938 MW;  A18C6C85921CD3D8 CRC64;
     MPNPATAAPI ATVNSASVAQ LDAAVAAARR AFDEGPWPRM SPKERSAALH RVADRLEQLH
     APLSAALVEE VGTPITLATT LQAQLPVQVL REYADAAADI GVTHLGPHFD PVPSSSYVAR
     RPMGVAAVIA AYNFPILLAI RSAGAALAAG CTVVLLPSPR TPLTTLLLHD IFSDLPPGTV
     NTVVGGPEIG RHLTTHPGVE KVAFTGSMAV GAQIMRQAAD TAKSLSLELG DKSPAVVLPD
     ADLAEQLPGI LLGYLANSGQ SCGATTRLIV PREKVEEFIA GSQAFIEGVL VGDPWDPATV
     IGPLIRPEHR DFVRSHVEKA IRNGADVIAR GRSVDALPGW YHEPVLLAGV DSRAEIAQQE
     LFGPVAVLLV YDDVEEAVKL ANDTPYGLHG KVFTADVRAG LEVAARIRAG SVQVNGGGFR
     ADAPFGGMKA SGIGREYGMW GIQEFSEVQH IQWAW
//
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