ALDH_PAENI
ID ALDH_PAENI Reviewed; 458 AA.
AC Q8GAK7;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Aldehyde dehydrogenase;
DE EC=1.2.1.3;
DE EC=1.2.1.4;
DE AltName: Full=NAD/NADP-dependent aldehyde dehydrogenase;
GN Name=aldh; Synonyms=adh; ORFNames=ORF39;
OS Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans).
OG Plasmid pAO1.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=29320;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49919 / DSM 420 / JCM 3874 / NBRC 15511; PLASMID=pAO1;
RX PubMed=12618462; DOI=10.1128/jb.185.6.1976-1986.2003;
RA Igloi G.L., Brandsch R.;
RT "Sequence of the 165-kilobase catabolic plasmid pAO1 from Arthrobacter
RT nicotinovorans and identification of a pAO1-dependent nicotine uptake
RT system.";
RL J. Bacteriol. 185:1976-1986(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP INDUCTION, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 49919 / DSM 420 / JCM 3874 / NBRC 15511; PLASMID=pAO1;
RX PubMed=23063486; DOI=10.1016/j.resmic.2012.10.003;
RA Mihasan M., Stefan M., Hritcu L., Artenie V., Brandsch R.;
RT "Evidence of a plasmid-encoded oxidative xylose-catabolic pathway in
RT Arthrobacter nicotinovorans pAO1.";
RL Res. Microbiol. 164:22-30(2013).
CC -!- FUNCTION: Aldehyde dehydrogenase able to oxidize various aldehydes such
CC as formaldehyde, glyceraldehyde, butyraldehyde, glutaraldehyde and
CC benzaldehyde (in vitro). Is likely involved in the oxidative D-xylose
CC degradation pathway, catalyzing the oxidation step of 2-oxoglutarate
CC semialdehyde to 2-oxoglutarate. Is able to use both NAD(+) and NADP(+);
CC however, shows a preference for NADP(+). Does not display succinate
CC semialdehyde dehydrogenase activity. {ECO:0000269|PubMed:23063486}.
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:0000269|PubMed:23063486};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NADP(+) = a carboxylate + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:11888, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.4;
CC Evidence={ECO:0000269|PubMed:23063486};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.022 mM for NADP(+) {ECO:0000269|PubMed:23063486};
CC KM=1.26 mM for NAD(+) {ECO:0000269|PubMed:23063486};
CC KM=4.2 mM for formaldehyde {ECO:0000269|PubMed:23063486};
CC KM=2.5 mM for acetaldehyde {ECO:0000269|PubMed:23063486};
CC KM=1.5 mM for propionaldehyde {ECO:0000269|PubMed:23063486};
CC KM=0.65 mM for glyceraldehyde {ECO:0000269|PubMed:23063486};
CC KM=0.15 mM for butyraldehyde {ECO:0000269|PubMed:23063486};
CC KM=0.11 mM for glutaraldehyde {ECO:0000269|PubMed:23063486};
CC KM=2.1 mM for benzaldehyde {ECO:0000269|PubMed:23063486};
CC Note=kcat is 0.38 sec(-1) with formaldehyde as substrate. kcat is
CC 0.75 sec(-1) with acetaldehyde as substrate. kcat is 1.2 sec(-1) with
CC propionaldehyde as substrate. kcat is 1.35 sec(-1) with
CC glyceraldehyde as substrate. kcat is 0.65 sec(-1) with butyraldehyde
CC as substrate. kcat is 3.92 sec(-1) with glutaraldehyde as substrate.
CC kcat is 4.52 sec(-1) with benzaldehyde as substrate.;
CC -!- PATHWAY: Carbohydrate metabolism; D-xylose degradation.
CC {ECO:0000269|PubMed:23063486}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23063486}.
CC -!- INDUCTION: Is induced by D-xylose. No significant levels of expression
CC can detected when the cells are grown on various other sugars such as
CC L-xylose, L-arabinose, D-galactose, D-tagatose and D-glucose.
CC {ECO:0000269|PubMed:23063486}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AJ507836; CAD47897.1; -; Genomic_DNA.
DR RefSeq; WP_016359408.1; NC_021229.1.
DR RefSeq; YP_007988723.1; NC_021229.1.
DR AlphaFoldDB; Q8GAK7; -.
DR SMR; Q8GAK7; -.
DR BioCyc; MetaCyc:MON-17149; -.
DR SABIO-RK; Q8GAK7; -.
DR UniPathway; UPA00810; -.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0033721; F:aldehyde dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IDA:UniProtKB.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0042843; P:D-xylose catabolic process; TAS:UniProtKB.
DR CDD; cd07100; ALDH_SSADH1_GabD1; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 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; IPR044148; ALDH_GabD1-like.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Plasmid.
FT CHAIN 1..458
FT /note="Aldehyde dehydrogenase"
FT /id="PRO_0000429427"
FT ACT_SITE 232
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 134..135
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 158..161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 210..211
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 458 AA; 49421 MW; 8ABCDD4C1E4E6CCD CRC64;
MAIATIDPTT GITLKTFDAH TPEEVENRIA RAEAAFRSLQ NTSFEERARW MHKAADILES
EADEVARLIA TEMGKTLTTA KYEALKSATG MRHFADHAQR YLSPETPVPA SEVNASNLHV
QFDPLGVVLA VMPWNYPLWQ AVRFAAPALM AGNTGLLKHA SNVPQCALYL GDLFARGGFP
EGAFQTLLVE GKDVIPLVDD ARIRAVTLTG SVAAGSAIAE AAGRNIKRSV LELGGMDVFI
VMPSADIEKA AAQAVIARLQ NSGQSCIAAK RFYVHEDVYD RFEHLFVTGM AEAVAGDPLD
ESTSFGPLAT ERGRQDVHEL VRDAREKGAA VQCGGEIPEG EGWYYPATVL TGVTEDMRIY
REECFGPVAC LYKVSSLQEA IALSNDSDFG LSSSVWTNDE TEATEAARSI EAGGVFINGL
TASFPAVPFG GLKDSGYGRE LSAYGIREFV NIKTVWTS
