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Protein

Aldehyde dehydrogenase PuuC

Gene

puuC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of 3-hydroxypropionaldehyde (3-HPA) to 3-hydroxypropionic acid (3-HP). It acts preferentially with NAD but can also use NADP. 3-HPA appears to be the most suitable substrate for PuuC followed by isovaleraldehyde, propionaldehyde, butyraldehyde, and valeraldehyde. It might play a role in propionate and/or acetic acid metabolisms. Also involved in the breakdown of putrescine through the oxidation of gamma-Glu-gamma-aminobutyraldehyde to gamma-Glu-gamma-aminobutyrate (gamma-Glu-GABA).2 Publications

Catalytic activityi

Gamma-glutamyl-gamma-aminobutyraldehyde + NAD+ + H2O = gamma-glutamyl-gamma-aminobutyrate + NADH.
An aldehyde + NAD(P)+ + H2O = a carboxylate + NAD(P)H.

Enzyme 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 bisulfite 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.
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. 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei267 – 2671By similarity
Active sitei302 – 3021By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi244 – 2496NAD or NAPDBy similarity

GO - Molecular functioni

GO - Biological processi

  • putrescine catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

BioCyciEcoCyc:ALDHDEHYDROG-MONOMER.
ECOL316407:JW1293-MONOMER.
MetaCyc:ALDHDEHYDROG-MONOMER.
BRENDAi1.2.1.B6. 2026.
UniPathwayiUPA00188; UER00882.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde dehydrogenase PuuC (EC:1.2.1.5)
Alternative name(s):
3-hydroxypropionaldehyde dehydrogenase
Gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase
Short name:
Gamma-Glu-gamma-aminobutyraldehyde dehydrogenase
Gene namesi
Name:puuC
Synonyms:aldH
Ordered Locus Names:b1300, JW1293
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10036. puuC.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Aldehyde dehydrogenase PuuCPRO_0000056448Add
BLAST

Proteomic databases

PaxDbiP23883.
PRIDEiP23883.

Interactioni

Protein-protein interaction databases

BioGridi4263528. 7 interactions.
DIPiDIP-9083N.
STRINGi511145.b1300.

Structurei

3D structure databases

ProteinModelPortaliP23883.
SMRiP23883. Positions 6-493.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271505.
InParanoidiP23883.
KOiK09472.
OMAiNELAMIV.
OrthoDBiEOG6BS8QW.
PhylomeDBiP23883.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. 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.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti313 – 3131S → R in AAA23428 (PubMed:1840553).Curated

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.
PATRICi32117872. VBIEscCol129921_1356.

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. Positions 6-493.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263528. 7 interactions.
DIPiDIP-9083N.
STRINGi511145.b1300.

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.
PATRICi32117872. VBIEscCol129921_1356.

Organism-specific databases

EchoBASEiEB0035.
EcoGeneiEG10036. puuC.

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271505.
InParanoidiP23883.
KOiK09472.
OMAiNELAMIV.
OrthoDBiEOG6BS8QW.
PhylomeDBiP23883.

Enzyme and pathway databases

UniPathwayiUPA00188; UER00882.
BioCyciEcoCyc:ALDHDEHYDROG-MONOMER.
ECOL316407:JW1293-MONOMER.
MetaCyc:ALDHDEHYDROG-MONOMER.
BRENDAi1.2.1.B6. 2026.

Miscellaneous databases

PROiP23883.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. 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.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning an Escherichia coli gene encoding a protein remarkably similar to mammalian aldehyde dehydrogenases."
    Heim R., Strehler E.E.
    Gene 99:15-23(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A novel putrescine utilization pathway involves gamma-glutamylated intermediates of Escherichia coli K-12."
    Kurihara S., Oda S., Kato K., Kim H.G., Koyanagi T., Kumagai H., Suzuki H.
    J. Biol. Chem. 280:4602-4608(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A GAMMA-GLUTAMYL-GAMMA-AMINOBUTYRALDEHYDE DEHYDROGENASE, NOMENCLATURE.
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Cloning, expression, and characterization of an aldehyde dehydrogenase from Escherichia coli K-12 that utilizes 3-Hydroxypropionaldehyde as a substrate."
    Jo J.E., Mohan Raj S., Rathnasingh C., Selvakumar E., Jung W.C., Park S.
    Appl. Microbiol. Biotechnol. 81:51-60(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ALDEHYDE DEHYDROGENASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ENZYME REGULATION.
    Strain: K12.

Entry informationi

Entry nameiPUUC_ECOLI
AccessioniPrimary (citable) accession number: P23883
Secondary accession number(s): P78250, Q5H774
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1997
Last modified: January 20, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.