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UniProtKB - P0A9T0 (SERA_ECOLI)

Entry version 123 (13 Feb 2019)
Sequence version 2 (23 Jan 2007)
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Protein

D-3-phosphoglycerate dehydrogenase

Gene

serA

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 reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.1 Publication

<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

Displays feedback inhibition by L-serine. Inhibited by glycine.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

kcat is 0.55 sec(-1) for 3-phospho-D-glycerate oxidation. kcat is 27.8 sec(-1) for 3-phosphonooxypyruvate reduction. kcat is 33.3 sec(-1) for 2-oxoglutarate reduction. kcat is 0.71 sec(-1) for (R)-2-hydroxyglutarate oxidation. kcat is 0.25 sec(-1) for (S)-2-hydroxyglutarate oxidation.1 Publication
  1. KM=1.2 mM for 3-phospho-D-glycerate1 Publication
  2. KM=3.2 µM for 3-phosphonooxypyruvate1 Publication
  3. KM=88 µM for 2-oxoglutarate1 Publication
  4. KM=0.37 mM for (R)-2-hydroxyglutarate1 Publication
  5. KM=2.9 mM for (S)-2-hydroxyglutarate1 Publication
  1. Vmax=183 nmol/min/mg enzyme for 3-phospho-D-glycerate oxidation1 Publication
  2. Vmax=9.27 µmol/min/mg enzyme for 3-phosphonooxypyruvate reduction1 Publication
  3. Vmax=11.1 µmol/min/mg enzyme for 2-oxoglutarate reduction1 Publication
  4. Vmax=237 nmol/min/mg enzyme for (R)-2-hydroxyglutarate oxidation1 Publication
  5. Vmax=83.3 nmol/min/mg enzyme for (S)-2-hydroxyglutarate oxidation1 Publication

pH dependencei

Optimum pH is 8.5 for the reductase activities and 9.0 for the dehydrogenase activities.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: L-serine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-serine from 3-phospho-D-glycerate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. D-3-phosphoglycerate dehydrogenase (serA)
  2. Phosphoserine aminotransferase (serC)
  3. Phosphoserine phosphatase (serB)
This subpathway is part of the pathway L-serine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-serine from 3-phospho-D-glycerate, the pathway L-serine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei181NAD1 Publication1
<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 sitei2401
Binding sitei264NAD1 Publication1
Active sitei2691
Active sitei292Proton donor1

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 bindingi161 – 162NAD1 Publication2
Nucleotide bindingi238 – 240NAD1 Publication3
Nucleotide bindingi292 – 295NAD1 Publication4

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

  • L-serine biosynthetic process Source: EcoCyc
  • serine family amino acid biosynthetic process Source: GO_Central
View the complete GO annotation on QuickGO ...

<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
Biological processAmino-acid biosynthesis, Serine biosynthesis
LigandNAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:PGLYCDEHYDROG-MONOMER
ECOL316407:JW2880-MONOMER
MetaCyc:PGLYCDEHYDROG-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.1.1.95 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P0A9T0

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

More...UniPathwayi
UPA00135;UER00196

<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:
D-3-phosphoglycerate dehydrogenase (EC:1.1.1.951 Publication)
Short name:
PGDH
Alternative name(s):
2-oxoglutarate reductaseCurated (EC:1.1.1.3991 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:serA
Ordered Locus Names:b2913, JW2880
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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		EG10944 serA

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00000759992 – 410D-3-phosphoglycerate dehydrogenaseAdd BLAST409

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P0A9T0

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A9T0

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

More...PaxDbi		P0A9T0

PRoteomics IDEntifications database

More...PRIDEi		P0A9T0

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer.

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4261173, 27 interactors

Database of interacting proteins

More...DIPi		DIP-10851N

Protein interaction database and analysis system

More...IntActi		P0A9T0, 3 interactors

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_3088

<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

Secondary structure

1410
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PSDX-ray2.75A/B2-410[»]
1SC6X-ray2.09A/B/C/D7-410[»]
1YBAX-ray2.24A/B/C/D1-410[»]
2P9CX-ray2.46A/B1-410[»]
2P9EX-ray2.60A/B/C/D1-410[»]
2P9GX-ray2.80A/B1-410[»]
2PA3X-ray2.74A1-410[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P0A9T0

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

More...SMRi		P0A9T0

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0A9T0

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini339 – 410ACTPROSITE-ProRule annotationAdd BLAST72

<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 D-isomer specific 2-hydroxyacid dehydrogenase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4108JQ1 Bacteria
COG0111 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000136696

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A9T0

KEGG Orthology (KO)

More...KOi		K00058

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A9T0

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002912 ACT_dom
IPR006139 D-isomer_2_OHA_DH_cat_dom
IPR029753 D-isomer_DH_CS
IPR029752 D-isomer_DH_CS1
IPR006140 D-isomer_DH_NAD-bd
IPR036291 NAD(P)-bd_dom_sf
IPR029015 PGDH_2

The PANTHER Classification System

More...PANTHERi		PTHR10996:SF165 PTHR10996:SF165, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00389 2-Hacid_dh, 1 hit
PF02826 2-Hacid_dh_C, 1 hit
PF01842 ACT, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51735 SSF51735, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51671 ACT, 1 hit
PS00065 D_2_HYDROXYACID_DH_1, 1 hit
PS00670 D_2_HYDROXYACID_DH_2, 1 hit
PS00671 D_2_HYDROXYACID_DH_3, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0A9T0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKVSLEKDK IKFLLVEGVH QKALESLRAA GYTNIEFHKG ALDDEQLKES 
        60         70         80         90        100
IRDAHFIGLR SRTHLTEDVI NAAEKLVAIG CFCIGTNQVD LDAAAKRGIP 
       110        120        130        140        150
VFNAPFSNTR SVAELVIGEL LLLLRGVPEA NAKAHRGVWN KLAAGSFEAR 
       160        170        180        190        200
GKKLGIIGYG HIGTQLGILA ESLGMYVYFY DIENKLPLGN ATQVQHLSDL 
       210        220        230        240        250
LNMSDVVSLH VPENPSTKNM MGAKEISLMK PGSLLINASR GTVVDIPALC 
       260        270        280        290        300
DALASKHLAG AAIDVFPTEP ATNSDPFTSP LCEFDNVLLT PHIGGSTQEA 
       310        320        330        340        350
QENIGLEVAG KLIKYSDNGS TLSAVNFPEV SLPLHGGRRL MHIHENRPGV 
       360        370        380        390        400
LTALNKIFAE QGVNIAAQYL QTSAQMGYVV IDIEADEDVA EKALQAMKAI 
       410
PGTIRARLLY
Length:410
Mass (Da):44,176
Last modified:January 23, 2007 - 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:i61EF5EFC304DF6F0
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
L29397 Genomic DNA Translation: AAA24625.1
U28377 Genomic DNA Translation: AAA69080.1
U00096 Genomic DNA Translation: AAC75950.1
AP009048 Genomic DNA Translation: BAE76977.1
X66836 Genomic DNA Translation: CAA47308.1
M64630 Genomic DNA Translation: AAA73016.1

Protein sequence database of the Protein Information Resource

More...PIRi		A25200 DEECPG

NCBI Reference Sequences

More...RefSeqi		NP_417388.1, NC_000913.3
WP_001151604.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75950; AAC75950; b2913
BAE76977; BAE76977; BAE76977

Database of genes from NCBI RefSeq genomes

More...GeneIDi		945258

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW2880
eco:b2913

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.3820

<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
L29397 Genomic DNA Translation: AAA24625.1
U28377 Genomic DNA Translation: AAA69080.1
U00096 Genomic DNA Translation: AAC75950.1
AP009048 Genomic DNA Translation: BAE76977.1
X66836 Genomic DNA Translation: CAA47308.1
M64630 Genomic DNA Translation: AAA73016.1
PIRiA25200 DEECPG
RefSeqiNP_417388.1, NC_000913.3
WP_001151604.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PSDX-ray2.75A/B2-410[»]
1SC6X-ray2.09A/B/C/D7-410[»]
1YBAX-ray2.24A/B/C/D1-410[»]
2P9CX-ray2.46A/B1-410[»]
2P9EX-ray2.60A/B/C/D1-410[»]
2P9GX-ray2.80A/B1-410[»]
2PA3X-ray2.74A1-410[»]
ProteinModelPortaliP0A9T0
SMRiP0A9T0
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261173, 27 interactors
DIPiDIP-10851N
IntActiP0A9T0, 3 interactors
STRINGi316385.ECDH10B_3088

Proteomic databases

EPDiP0A9T0
jPOSTiP0A9T0
PaxDbiP0A9T0
PRIDEiP0A9T0

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75950; AAC75950; b2913
BAE76977; BAE76977; BAE76977
GeneIDi945258
KEGGiecj:JW2880
eco:b2913
PATRICifig|1411691.4.peg.3820

Organism-specific databases

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

More...EchoBASEi		EB0937
EcoGeneiEG10944 serA

Phylogenomic databases

eggNOGiENOG4108JQ1 Bacteria
COG0111 LUCA
HOGENOMiHOG000136696
InParanoidiP0A9T0
KOiK00058
PhylomeDBiP0A9T0

Enzyme and pathway databases

UniPathwayi
UPA00135;UER00196

BioCyciEcoCyc:PGLYCDEHYDROG-MONOMER
ECOL316407:JW2880-MONOMER
MetaCyc:PGLYCDEHYDROG-MONOMER
BRENDAi1.1.1.95 2026
SABIO-RKiP0A9T0

Miscellaneous databases

EvolutionaryTraceiP0A9T0

Protein Ontology

More...PROi		PR:P0A9T0

Family and domain databases

InterProiView protein in InterPro
IPR002912 ACT_dom
IPR006139 D-isomer_2_OHA_DH_cat_dom
IPR029753 D-isomer_DH_CS
IPR029752 D-isomer_DH_CS1
IPR006140 D-isomer_DH_NAD-bd
IPR036291 NAD(P)-bd_dom_sf
IPR029015 PGDH_2
PANTHERiPTHR10996:SF165 PTHR10996:SF165, 1 hit
PfamiView protein in Pfam
PF00389 2-Hacid_dh, 1 hit
PF02826 2-Hacid_dh_C, 1 hit
PF01842 ACT, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS51671 ACT, 1 hit
PS00065 D_2_HYDROXYACID_DH_1, 1 hit
PS00670 D_2_HYDROXYACID_DH_2, 1 hit
PS00671 D_2_HYDROXYACID_DH_3, 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 nameiSERA_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: P0A9T0
Secondary accession number(s): P08328, Q2M9S9, Q47633
<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: August 1, 1988
Last sequence update: January 23, 2007
Last modified: February 13, 2019
This is version 123 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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