ID ALDH_DEIRA Reviewed; 515 AA.
AC Q9RYG9; O32502;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Aldehyde dehydrogenase;
DE EC=1.2.1.3;
GN Name=aldA; OrderedLocusNames=DR_A0348;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC
RC 15346 / NCIMB 9279 / VKM B-1422 / R1;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-258.
RC STRAIN=KD8301;
RA Narumi I., Du Z., Alatas Z., Kitayama S., Watanabe H.;
RT "Isolation and characterization of pprA, a novel Deinococcus radiodurans
RT gene involved in DNA repair.";
RL Submitted (APR-1997) 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 -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AE001825; AAF12436.1; -; Genomic_DNA.
DR EMBL; AB003475; BAA21372.1; -; Genomic_DNA.
DR PIR; H75589; H75589.
DR RefSeq; NP_285671.1; NC_001264.1.
DR RefSeq; WP_010889607.1; NZ_JMLF01000033.1.
DR AlphaFoldDB; Q9RYG9; -.
DR SMR; Q9RYG9; -.
DR STRING; 243230.DR_A0348; -.
DR PaxDb; 243230-DR_A0348; -.
DR EnsemblBacteria; AAF12436; AAF12436; DR_A0348.
DR GeneID; 69519234; -.
DR KEGG; dra:DR_A0348; -.
DR PATRIC; fig|243230.17.peg.3240; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_2_0; -.
DR InParanoid; Q9RYG9; -.
DR OrthoDB; 9762913at2; -.
DR Proteomes; UP000002524; Chromosome II.
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 NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..515
FT /note="Aldehyde dehydrogenase"
FT /id="PRO_0000056447"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 272
FT /evidence="ECO:0000250"
FT ACT_SITE 311
FT /evidence="ECO:0000250"
FT BINDING 228..234
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 515 AA; 56409 MW; D8BB5DDF7D2DBBC0 CRC64;
MTVAEQQPQH QGYANPGTPG SVVTFKKRYD NFIGGQWVPP VKGQYFDNAS PVDGKVFTQA
ARSTAEDVEL ALDAAHRAAP AWGRTSVTER SNILLKIADR MEQNLEMLAV AETWDNGKPV
RETLAADLPL AIDHFRYFAG CIRAQEGGLS QIDDSTVAYH FHEPLGVVGQ IIPWNFPLLM
GVWKLAPALA AGNAVVLKPA EQTPASIMVL MELIADLLPE GVVNVVNGFG LEAGKPLASS
PRIAKIAFTG ETNTGRLIMG YAADNLIPVT LELGGKSPNI FFDDVMMEDD AFLDKAVEGM
VMFALNQGEV CTCPSRALIQ ESIYDRFMER AVQRVEAITM GHPLDPGTMI GAQASTEQLD
KILSYLDIGR AEGAEVLTGG ERGQREGLEE GFYVKPTIFK GHNKMRIFQE EIFGPVLAAA
TFKDEAEALE LANDTLYGLG AGLWTRDISR AYRMGRGIQA GRVWTNCYHV YPAHAAFGGY
KQSGIGRENH RMMLDHYQQT KNLLVSYSPN KMGFF
//
