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Protein

NADP/NAD-dependent aldehyde dehydrogenase PuuC

Gene

puuC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of 3-hydroxypropionaldehyde (3-HPA) to 3-hydroxypropionic acid (3-HP) (PubMed:18668238). It acts preferentially with NAD but can also use NADP (PubMed:18668238). 3-HPA appears to be the most suitable substrate for PuuC followed by isovaleraldehyde, propionaldehyde, butyraldehyde, and valeraldehyde (PubMed:18668238). It might play a role in propionate and/or acetic acid metabolisms (PubMed:18668238). Also involved in the breakdown of putrescine through the oxidation of gamma-Glu-gamma-aminobutyraldehyde to gamma-Glu-gamma-aminobutyrate (gamma-Glu-GABA) (PubMed:15590624).1 Publication2 Publications

Catalytic activityi

An aldehyde + NAD(P)+ + H2O = a carboxylate + NAD(P)H.1 Publication2 Publications
Gamma-glutamyl-gamma-aminobutyraldehyde + NAD(P)+ + H2O = gamma-glutamyl-gamma-aminobutyrate + NAD(P)H.1 Publication

Activity regulationi

Lithium ions exhibits the highest inhibition (97%). To a lesser extent (5-20%), potassium, sodium, and ammonium ions also inhibit PuuC activity. Transition metals, such as copper and zinc ions inhibit PuuC activity by more than 90%. The presence of heavy metals (mercury, silver) or sodium hydrogensulfite in the reaction mixture completely inactivate PuuC; in contrast, disulfide reductants such as DTT and 2-mercaptoethanol significantly increase its activity by 75% and 27%, respectively.1 Publication

Kineticsi

  1. KM=0.06 mM for 3-hydroxypropionaldehyde (with NAD at ph 8 and at 37 degrees Celsius)1 Publication
  2. KM=0.12 mM for 3-hydroxypropionic acid (with NADH at ph 8 and at 37 degrees Celsius)1 Publication
  3. KM=0.24 mM for valeraldehyde (with NAD at ph 8 and at 37 degrees Celsius)1 Publication
  4. KM=0.29 mM for 3-hydroxypropionaldehyde (with NADP at ph 8 and at 37 degrees Celsius)1 Publication
  5. KM=0.49 mM for 3-hydroxypropionaldehyde (with NAD at ph 8 and at 37 degrees Celsius)1 Publication
  6. KM=0.68 mM for isovaleraldehyde (with NAD at ph 8 and at 37 degrees Celsius)1 Publication
  7. KM=0.97 mM for butyraldehyde (with NAD at ph 8 and at 37 degrees Celsius)1 Publication
  8. KM=1.00 mM for acetaldehyde (with NAD at ph 8 and at 37 degrees Celsius)1 Publication
  9. KM=1.21 mM for propionaldehyde (with NAD at ph 8 and at 37 degrees Celsius)1 Publication
  10. KM=5.37 mM for benzaldehyde (with NADP at ph 8 and at 37 degrees Celsius)1 Publication
  1. Vmax=0.3 µmol/min/mg enzyme with 3-hydroxypropionic acid as substrate (with NADH at ph 8 and at 37 degrees Celsius)1 Publication
  2. Vmax=5.5 µmol/min/mg enzyme with 3-hydroxypropionaldehyde as substrate (with NADP at ph 8 and at 37 degrees Celsius)1 Publication
  3. Vmax=12.39 µmol/min/mg enzyme with acetaldehyde as substrate (with NAD at ph 8 and at 37 degrees Celsius)1 Publication
  4. Vmax=19.51 µmol/min/mg enzyme with benzaldehyde as substrate (with NADP at ph 8 and at 37 degrees Celsius)1 Publication
  5. Vmax=27.35 µmol/min/mg enzyme with propionaldehyde as substrate (with NAD at ph 8 and at 37 degrees Celsius)1 Publication
  6. Vmax=29.47 µmol/min/mg enzyme with valeraldehyde as substrate (with NAD at ph 8 and at 37 degrees Celsius)1 Publication
  7. Vmax=30.07 µmol/min/mg enzyme with butyraldehyde as substrate (with NAD at ph 8 and at 37 degrees Celsius)1 Publication
  8. Vmax=30.10 µmol/min/mg enzyme with 3-hydroxypropionaldehyde as substrate (with NAD at ph 8 and at 37 degrees Celsius)1 Publication
  9. Vmax=30.67 µmol/min/mg enzyme with isovaleraldehyde as substrate (with NAD at ph 8 and at 37 degrees Celsius)1 Publication
  10. Vmax=32.1 µmol/min/mg enzyme with 3-hydroxypropionaldehyde as substrate (with NAD at ph 8 and at 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 8. Activity is highly sensitive to pH variation, and an increase or decrease of one pH unit from the optimal attenuates more than 70% of activity. At pH 6.0, only 6% of the activity remains. At pH.5.0, the activity is completely abolished.1 Publication

Temperature dependencei

Optimum temperature is 37 degrees Celsius. It appears to be stable between 20 and 50 degrees Celsius but becomes very unstable at or above 50 degrees Celsius.1 Publication

Pathwayi: putrescine degradation

This protein is involved in step 3 of the subpathway that synthesizes 4-aminobutanoate from putrescine.1 Publication
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Gamma-glutamylputrescine synthetase PuuA (puuA)
  2. Gamma-glutamylputrescine oxidoreductase (puuB)
  3. NADP/NAD-dependent aldehyde dehydrogenase PuuC (puuC)
  4. Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (puuD)
This subpathway is part of the pathway putrescine degradation, which is itself part of Amine and polyamine degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 4-aminobutanoate from putrescine, the pathway putrescine degradation and in Amine and polyamine degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei267PROSITE-ProRule annotation1 Publication1
Active sitei302PROSITE-ProRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi244 – 249NAD or NADPBy similarity6

GO - Molecular functioni

  • aldehyde dehydrogenase [NAD(P)+] activity Source: UniProtKB

GO - Biological processi

  • putrescine catabolic process Source: EcoCyc

Keywordsi

Molecular functionOxidoreductase
LigandNAD, NADP

Enzyme and pathway databases

BioCyciEcoCyc:ALDHDEHYDROG-MONOMER
MetaCyc:ALDHDEHYDROG-MONOMER
BRENDAi1.2.1.B6 2026
UniPathwayi
UPA00188;UER00882

Names & Taxonomyi

Protein namesi
Recommended name:
NADP/NAD-dependent aldehyde dehydrogenase PuuC1 Publication (EC:1.2.1.51 Publication2 Publications)
Short name:
ALDH1 Publication
Alternative name(s):
3-hydroxypropionaldehyde dehydrogenase1 Publication
Gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase1 Publication
Short name:
Gamma-Glu-gamma-aminobutyraldehyde dehydrogenase1 Publication
Gene namesi
Name:puuC1 Publication
Synonyms:aldH1 Publication
Ordered Locus Names:b1300, JW1293
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10036 puuC

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000564481 – 495NADP/NAD-dependent aldehyde dehydrogenase PuuCAdd BLAST495

Proteomic databases

PaxDbiP23883
PRIDEiP23883

Interactioni

Protein-protein interaction databases

BioGridi4263528, 7 interactors
DIPiDIP-9083N
STRINGi316385.ECDH10B_1417

Structurei

3D structure databases

ProteinModelPortaliP23883
SMRiP23883
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiENOG4105C26 Bacteria
COG1012 LUCA
HOGENOMiHOG000271505
InParanoidiP23883
KOiK09472
PhylomeDBiP23883

Family and domain databases

Gene3Di3.40.309.10, 1 hit
3.40.605.10, 1 hit
InterProiView protein in InterPro
IPR016161 Ald_DH/histidinol_DH
IPR016163 Ald_DH_C
IPR016160 Ald_DH_CS_CYS
IPR029510 Ald_DH_CS_GLU
IPR016162 Ald_DH_N
IPR015590 Aldehyde_DH_dom
PfamiView protein in Pfam
PF00171 Aldedh, 1 hit
SUPFAMiSSF53720 SSF53720, 1 hit
PROSITEiView protein in PROSITE
PS00070 ALDEHYDE_DEHYDR_CYS, 1 hit
PS00687 ALDEHYDE_DEHYDR_GLU, 1 hit

Sequencei

Sequence statusi: Complete.

P23883-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNFHHLAYWQ DKALSLAIEN RLFINGEYTA AAENETFETV DPVTQAPLAK
60 70 80 90 100
IARGKSVDID RAMSAARGVF ERGDWSLSSP AKRKAVLNKL ADLMEAHAEE
110 120 130 140 150
LALLETLDTG KPIRHSLRDD IPGAARAIRW YAEAIDKVYG EVATTSSHEL
160 170 180 190 200
AMIVREPVGV IAAIVPWNFP LLLTCWKLGP ALAAGNSVIL KPSEKSPLSA
210 220 230 240 250
IRLAGLAKEA GLPDGVLNVV TGFGHEAGQA LSRHNDIDAI AFTGSTRTGK
260 270 280 290 300
QLLKDAGDSN MKRVWLEAGG KSANIVFADC PDLQQAASAT AAGIFYNQGQ
310 320 330 340 350
VCIAGTRLLL EESIADEFLA LLKQQAQNWQ PGHPLDPATT MGTLIDCAHA
360 370 380 390 400
DSVHSFIREG ESKGQLLLDG RNAGLAAAIG PTIFVDVDPN ASLSREEIFG
410 420 430 440 450
PVLVVTRFTS EEQALQLAND SQYGLGAAVW TRDLSRAHRM SRRLKAGSVF
460 470 480 490
VNNYNDGDMT VPFGGYKQSG NGRDKSLHAL EKFTELKTIW ISLEA
Length:495
Mass (Da):53,419
Last modified:November 1, 1997 - v2
Checksum:iA20929C55F51C709
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti313S → R in AAA23428 (PubMed:1840553).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38433 Genomic DNA Translation: AAA23428.1
AB200319 Genomic DNA Translation: BAD88708.1
U00096 Genomic DNA Translation: AAC74382.1
AP009048 Genomic DNA Translation: BAA14869.1
PIRiG64878
RefSeqiNP_415816.1, NC_000913.3
WP_001009090.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74382; AAC74382; b1300
BAA14869; BAA14869; BAA14869
GeneIDi947003
KEGGiecj:JW1293
eco:b1300
PATRICifig|1411691.4.peg.979

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38433 Genomic DNA Translation: AAA23428.1
AB200319 Genomic DNA Translation: BAD88708.1
U00096 Genomic DNA Translation: AAC74382.1
AP009048 Genomic DNA Translation: BAA14869.1
PIRiG64878
RefSeqiNP_415816.1, NC_000913.3
WP_001009090.1, NZ_LN832404.1

3D structure databases

ProteinModelPortaliP23883
SMRiP23883
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263528, 7 interactors
DIPiDIP-9083N
STRINGi316385.ECDH10B_1417

Proteomic databases

PaxDbiP23883
PRIDEiP23883

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74382; AAC74382; b1300
BAA14869; BAA14869; BAA14869
GeneIDi947003
KEGGiecj:JW1293
eco:b1300
PATRICifig|1411691.4.peg.979

Organism-specific databases

EchoBASEiEB0035
EcoGeneiEG10036 puuC

Phylogenomic databases

eggNOGiENOG4105C26 Bacteria
COG1012 LUCA
HOGENOMiHOG000271505
InParanoidiP23883
KOiK09472
PhylomeDBiP23883

Enzyme and pathway databases

UniPathwayi
UPA00188;UER00882

BioCyciEcoCyc:ALDHDEHYDROG-MONOMER
MetaCyc:ALDHDEHYDROG-MONOMER
BRENDAi1.2.1.B6 2026

Miscellaneous databases

PROiPR:P23883

Family and domain databases

Gene3Di3.40.309.10, 1 hit
3.40.605.10, 1 hit
InterProiView protein in InterPro
IPR016161 Ald_DH/histidinol_DH
IPR016163 Ald_DH_C
IPR016160 Ald_DH_CS_CYS
IPR029510 Ald_DH_CS_GLU
IPR016162 Ald_DH_N
IPR015590 Aldehyde_DH_dom
PfamiView protein in Pfam
PF00171 Aldedh, 1 hit
SUPFAMiSSF53720 SSF53720, 1 hit
PROSITEiView protein in PROSITE
PS00070 ALDEHYDE_DEHYDR_CYS, 1 hit
PS00687 ALDEHYDE_DEHYDR_GLU, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPUUC_ECOLI
AccessioniPrimary (citable) accession number: P23883
Secondary accession number(s): P78250, Q5H774
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1997
Last modified: November 7, 2018
This is version 137 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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