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Protein

NADP/NAD-dependent aldehyde dehydrogenase PuuC

Gene

puuC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei267PROSITE-ProRule annotation1 Publication1
Active sitei302PROSITE-ProRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi244 – 249NAD or NADPBy similarity6

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

GO - Biological processi

  • putrescine catabolic process Source: EcoCyc

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
LigandNAD, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:ALDHDEHYDROG-MONOMER
MetaCyc:ALDHDEHYDROG-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.2.1.B6 2026

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00188;UER00882

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:puuC1 Publication
Synonyms:aldH1 Publication
Ordered Locus Names:b1300, JW1293
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10036 puuC

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000564481 – 495NADP/NAD-dependent aldehyde dehydrogenase PuuCAdd BLAST495

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P23883

PRoteomics IDEntifications database

More...
PRIDEi
P23883

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4263528, 7 interactors

Database of interacting proteins

More...
DIPi
DIP-9083N

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_1417

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P23883

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P23883

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C26 Bacteria
COG1012 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000271505

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P23883

KEGG Orthology (KO)

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KOi
K09472

Database for complete collections of gene phylogenies

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PhylomeDBi
P23883

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.309.10, 1 hit
3.40.605.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View 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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00171 Aldedh, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53720 SSF53720, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00070 ALDEHYDE_DEHYDR_CYS, 1 hit
PS00687 ALDEHYDE_DEHYDR_GLU, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA20929C55F51C709
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti313S → R in AAA23428 (PubMed:1840553).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

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PIRi
G64878

NCBI Reference Sequences

More...
RefSeqi
NP_415816.1, NC_000913.3
WP_001009090.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74382; AAC74382; b1300
BAA14869; BAA14869; BAA14869

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947003

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1293
eco:b1300

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.979

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0035
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

Protein Ontology

More...
PROi
PR: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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPUUC_ECOLI
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P23883
Secondary accession number(s): P78250, Q5H774
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1997
Last modified: December 5, 2018
This is version 138 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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
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