PUUC_ECOLI
ID PUUC_ECOLI Reviewed; 495 AA.
AC P23883; P78250; Q5H774;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=NADP/NAD-dependent aldehyde dehydrogenase PuuC {ECO:0000303|PubMed:1840553};
DE Short=ALDH {ECO:0000303|PubMed:1840553};
DE EC=1.2.1.5 {ECO:0000269|PubMed:15590624, ECO:0000269|PubMed:18668238, ECO:0000305|PubMed:1840553};
DE AltName: Full=3-hydroxypropionaldehyde dehydrogenase {ECO:0000303|PubMed:18668238};
DE AltName: Full=Gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase {ECO:0000303|PubMed:15590624};
DE Short=Gamma-Glu-gamma-aminobutyraldehyde dehydrogenase {ECO:0000303|PubMed:15590624};
GN Name=puuC {ECO:0000303|PubMed:15590624};
GN Synonyms=aldH {ECO:0000303|PubMed:1840553};
GN OrderedLocusNames=b1300, JW1293;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS AN ALDEHYDE DEHYDROGENASE,
RP CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX PubMed=1840553; DOI=10.1016/0378-1119(91)90028-a;
RA Heim R., Strehler E.E.;
RT "Cloning an Escherichia coli gene encoding a protein remarkably similar to
RT mammalian aldehyde dehydrogenases.";
RL Gene 99:15-23(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A
RP GAMMA-GLUTAMYL-GAMMA-AMINOBUTYRALDEHYDE DEHYDROGENASE, CATALYTIC ACTIVITY,
RP PATHWAY, AND NOMENCLATURE.
RC STRAIN=K12;
RX PubMed=15590624; DOI=10.1074/jbc.m411114200;
RA Kurihara S., Oda S., Kato K., Kim H.G., Koyanagi T., Kumagai H., Suzuki H.;
RT "A novel putrescine utilization pathway involves gamma-glutamylated
RT intermediates of Escherichia coli K-12.";
RL J. Biol. Chem. 280:4602-4608(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION AS AN ALDEHYDE DEHYDROGENASE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND ACTIVITY
RP REGULATION.
RC STRAIN=K12;
RX PubMed=18668238; DOI=10.1007/s00253-008-1608-x;
RA Jo J.E., Mohan Raj S., Rathnasingh C., Selvakumar E., Jung W.C., Park S.;
RT "Cloning, expression, and characterization of an aldehyde dehydrogenase
RT from Escherichia coli K-12 that utilizes 3-Hydroxypropionaldehyde as a
RT substrate.";
RL Appl. Microbiol. Biotechnol. 81:51-60(2008).
CC -!- FUNCTION: Catalyzes the oxidation of 3-hydroxypropionaldehyde (3-HPA)
CC to 3-hydroxypropionic acid (3-HP) (PubMed:18668238). It acts
CC preferentially with NAD but can also use NADP (PubMed:18668238). 3-HPA
CC appears to be the most suitable substrate for PuuC followed by
CC isovaleraldehyde, propionaldehyde, butyraldehyde, and valeraldehyde
CC (PubMed:18668238). It might play a role in propionate and/or acetic
CC acid metabolisms (PubMed:18668238). Also involved in the breakdown of
CC putrescine through the oxidation of gamma-Glu-gamma-aminobutyraldehyde
CC to gamma-Glu-gamma-aminobutyrate (gamma-Glu-GABA) (PubMed:15590624).
CC {ECO:0000269|PubMed:15590624, ECO:0000269|PubMed:18668238,
CC ECO:0000305|PubMed:1840553}.
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=1.2.1.5; Evidence={ECO:0000269|PubMed:15590624,
CC ECO:0000269|PubMed:18668238, ECO:0000305|PubMed:1840553};
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=1.2.1.5; Evidence={ECO:0000269|PubMed:15590624,
CC ECO:0000269|PubMed:18668238, ECO:0000305|PubMed:1840553};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-(gamma-L-glutamylamino)butanal + H2O + NADP(+) = 4-(gamma-L-
CC glutamylamino)butanoate + 2 H(+) + NADPH; Xref=Rhea:RHEA:28410,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58800, ChEBI:CHEBI:61508;
CC Evidence={ECO:0000269|PubMed:15590624};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-(gamma-L-glutamylamino)butanal + H2O + NAD(+) = 4-(gamma-L-
CC glutamylamino)butanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:42340,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58800, ChEBI:CHEBI:61508;
CC Evidence={ECO:0000269|PubMed:15590624};
CC -!- ACTIVITY REGULATION: Lithium ions exhibits the highest inhibition
CC (97%). To a lesser extent (5-20%), potassium, sodium, and ammonium ions
CC also inhibit PuuC activity. Transition metals, such as copper and zinc
CC ions inhibit PuuC activity by more than 90%. The presence of heavy
CC metals (mercury, silver) or sodium hydrogensulfite in the reaction
CC mixture completely inactivate PuuC; in contrast, disulfide reductants
CC such as DTT and 2-mercaptoethanol significantly increase its activity
CC by 75% and 27%, respectively. {ECO:0000269|PubMed:18668238}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.06 mM for 3-hydroxypropionaldehyde (with NAD at ph 8 and at 37
CC degrees Celsius) {ECO:0000269|PubMed:18668238};
CC KM=0.12 mM for 3-hydroxypropionic acid (with NADH at ph 8 and at 37
CC degrees Celsius) {ECO:0000269|PubMed:18668238};
CC KM=0.24 mM for valeraldehyde (with NAD at ph 8 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:18668238};
CC KM=0.29 mM for 3-hydroxypropionaldehyde (with NADP at ph 8 and at 37
CC degrees Celsius) {ECO:0000269|PubMed:18668238};
CC KM=0.49 mM for 3-hydroxypropionaldehyde (with NAD at ph 8 and at 37
CC degrees Celsius) {ECO:0000269|PubMed:18668238};
CC KM=0.68 mM for isovaleraldehyde (with NAD at ph 8 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:18668238};
CC KM=0.97 mM for butyraldehyde (with NAD at ph 8 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:18668238};
CC KM=1.00 mM for acetaldehyde (with NAD at ph 8 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:18668238};
CC KM=1.21 mM for propionaldehyde (with NAD at ph 8 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:18668238};
CC KM=5.37 mM for benzaldehyde (with NADP at ph 8 and at 37 degrees
CC Celsius) {ECO:0000269|PubMed:18668238};
CC Vmax=0.3 umol/min/mg enzyme with 3-hydroxypropionic acid as substrate
CC (with NADH at ph 8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18668238};
CC Vmax=5.5 umol/min/mg enzyme with 3-hydroxypropionaldehyde as
CC substrate (with NADP at ph 8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18668238};
CC Vmax=12.39 umol/min/mg enzyme with acetaldehyde as substrate (with
CC NAD at ph 8 and at 37 degrees Celsius) {ECO:0000269|PubMed:18668238};
CC Vmax=19.51 umol/min/mg enzyme with benzaldehyde as substrate (with
CC NADP at ph 8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18668238};
CC Vmax=27.35 umol/min/mg enzyme with propionaldehyde as substrate (with
CC NAD at ph 8 and at 37 degrees Celsius) {ECO:0000269|PubMed:18668238};
CC Vmax=29.47 umol/min/mg enzyme with valeraldehyde as substrate (with
CC NAD at ph 8 and at 37 degrees Celsius) {ECO:0000269|PubMed:18668238};
CC Vmax=30.07 umol/min/mg enzyme with butyraldehyde as substrate (with
CC NAD at ph 8 and at 37 degrees Celsius) {ECO:0000269|PubMed:18668238};
CC Vmax=30.10 umol/min/mg enzyme with 3-hydroxypropionaldehyde as
CC substrate (with NAD at ph 8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18668238};
CC Vmax=30.67 umol/min/mg enzyme with isovaleraldehyde as substrate
CC (with NAD at ph 8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18668238};
CC Vmax=32.1 umol/min/mg enzyme with 3-hydroxypropionaldehyde as
CC substrate (with NAD at ph 8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:18668238};
CC pH dependence:
CC Optimum pH is 8. Activity is highly sensitive to pH variation, and an
CC increase or decrease of one pH unit from the optimal attenuates more
CC than 70% of activity. At pH 6.0, only 6% of the activity remains. At
CC pH.5.0, the activity is completely abolished.
CC {ECO:0000269|PubMed:18668238};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. It appears to be stable
CC between 20 and 50 degrees Celsius but becomes very unstable at or
CC above 50 degrees Celsius. {ECO:0000269|PubMed:18668238};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4-
CC aminobutanoate from putrescine: step 3/4.
CC {ECO:0000305|PubMed:15590624}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M38433; AAA23428.1; -; Genomic_DNA.
DR EMBL; AB200319; BAD88708.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74382.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14869.1; -; Genomic_DNA.
DR PIR; G64878; G64878.
DR RefSeq; NP_415816.1; NC_000913.3.
DR RefSeq; WP_001009090.1; NZ_SSZK01000012.1.
DR AlphaFoldDB; P23883; -.
DR SMR; P23883; -.
DR BioGRID; 4263528; 7.
DR DIP; DIP-9083N; -.
DR STRING; 511145.b1300; -.
DR PaxDb; P23883; -.
DR PRIDE; P23883; -.
DR EnsemblBacteria; AAC74382; AAC74382; b1300.
DR EnsemblBacteria; BAA14869; BAA14869; BAA14869.
DR GeneID; 947003; -.
DR KEGG; ecj:JW1293; -.
DR KEGG; eco:b1300; -.
DR PATRIC; fig|1411691.4.peg.979; -.
DR EchoBASE; EB0035; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_2_6; -.
DR InParanoid; P23883; -.
DR OMA; RRMDTGQ; -.
DR PhylomeDB; P23883; -.
DR BioCyc; EcoCyc:ALDHDEHYDROG-MON; -.
DR BioCyc; MetaCyc:ALDHDEHYDROG-MON; -.
DR BRENDA; 1.2.1.99; 2026.
DR UniPathway; UPA00188; UER00882.
DR PRO; PR:P23883; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0033721; F:aldehyde dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IDA:UniProtKB.
DR GO; GO:0009447; P:putrescine catabolic process; IMP:EcoCyc.
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 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 NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..495
FT /note="NADP/NAD-dependent aldehyde dehydrogenase PuuC"
FT /id="PRO_0000056448"
FT ACT_SITE 267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000305|PubMed:1840553"
FT ACT_SITE 302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008,
FT ECO:0000305|PubMed:1840553"
FT BINDING 244..249
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 313
FT /note="S -> R (in Ref. 1; AAA23428)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 53419 MW; A20929C55F51C709 CRC64;
MNFHHLAYWQ DKALSLAIEN RLFINGEYTA AAENETFETV DPVTQAPLAK IARGKSVDID
RAMSAARGVF ERGDWSLSSP AKRKAVLNKL ADLMEAHAEE LALLETLDTG KPIRHSLRDD
IPGAARAIRW YAEAIDKVYG EVATTSSHEL AMIVREPVGV IAAIVPWNFP LLLTCWKLGP
ALAAGNSVIL KPSEKSPLSA IRLAGLAKEA GLPDGVLNVV TGFGHEAGQA LSRHNDIDAI
AFTGSTRTGK QLLKDAGDSN MKRVWLEAGG KSANIVFADC PDLQQAASAT AAGIFYNQGQ
VCIAGTRLLL EESIADEFLA LLKQQAQNWQ PGHPLDPATT MGTLIDCAHA DSVHSFIREG
ESKGQLLLDG RNAGLAAAIG PTIFVDVDPN ASLSREEIFG PVLVVTRFTS EEQALQLAND
SQYGLGAAVW TRDLSRAHRM SRRLKAGSVF VNNYNDGDMT VPFGGYKQSG NGRDKSLHAL
EKFTELKTIW ISLEA
