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UniProtKB - P0AFI0 (OXC_ECOLI)

Entry version 119 (25 May 2022)
Sequence version 1 (20 Dec 2005)
Previous versions | rss
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Protein

Oxalyl-CoA decarboxylase

Gene

oxc

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

Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the decarboxylation of oxalyl-CoA to yield carbon dioxide and formyl-CoA.

1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Activated by ADP.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 69.7 sec(-1) for decarboxylase activity with oxalyl-CoA as substrate (with 300 µM ADP at pH 6.5 and 30 degrees Celsius). kcat is 60.7 sec(-1) for decarboxylase activity with oxalyl-CoA as substrate (at pH 6.5 and 30 degrees Celsius).
  1. KM=3.17 µM for oxalyl-CoA (with 300 µM ADP at pH 6.5 and 30 degrees Celsius)1 Publication
  2. KM=4.8 µM for oxalyl-CoA (at pH 6.5 and 30 degrees Celsius)1 Publication

pH dependencei

Optimum pH is between 5.5 and 7.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: oxalate degradation

This protein is involved in step 2 of the subpathway that synthesizes CO(2) and formate from oxalate. This subpathway is part of the pathway oxalate degradation, which is itself part of Metabolic intermediate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CO(2) and formate from oxalate, the pathway oxalate degradation and in Metabolic intermediate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei32Substrate; via amide nitrogenBy similarity1
Binding sitei118SubstrateBy similarity1
Binding sitei158ADP1 Publication1
Binding sitei220ADP1 Publication1
Binding sitei280ADP1 Publication1
Binding sitei302ADP1 Publication1
Binding sitei322ADP; via amide nitrogen1 Publication1
Binding sitei355Substrate1
Binding sitei372Thiamine pyrophosphate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi447Magnesium1 Publication1
Metal bindingi474Magnesium1 Publication1
Metal bindingi476Magnesium; via carbonyl oxygen1 Publication1
Binding sitei478Thiamine pyrophosphate; via amide nitrogen1 Publication1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

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 functionDecarboxylase, Lyase
LigandMagnesium, Metal-binding, Nucleotide-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:G7236-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		4.1.1.8, 2026

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

More...UniPathwayi		UPA00540;UER00599

<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%5Fand%5Ftaxonomy%5Fsection">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:
Oxalyl-CoA decarboxylase (EC:4.1.1.8)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:oxc
Synonyms:yfdU
Ordered Locus Names:b2373, JW2370
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000908241 – 564Oxalyl-CoA decarboxylaseAdd BLAST564

Proteomic databases

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

More...PaxDbi		P0AFI0

PRoteomics IDEntifications database

More...PRIDEi		P0AFI0

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By the acid response regulator EvgA.1 Publication

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer; dimer of dimers.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

P0AFI0
With#Exp.IntAct
itself4EBI-557143,EBI-557143

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4260862, 15 interactors
851186, 1 interactor

Database of interacting proteins

More...DIPi		DIP-48075N

Protein interaction database and analysis system

More...IntActi		P0AFI0, 6 interactors

Molecular INTeraction database

More...MINTi		P0AFI0

STRING: functional protein association networks

More...STRINGi		511145.b2373

<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

1564
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P0AFI0

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

More...SMRi		P0AFI0

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0AFI0

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni261 – 265Substrate bindingCurated5
Regioni396 – 398Thiamine pyrophosphate binding3
Regioni403 – 404Substrate binding2
Regioni421 – 423Thiamine pyrophosphate binding3
Regioni448 – 449Thiamine pyrophosphate binding2
Regioni550 – 552Substrate bindingBy similarity3

<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 TPP enzyme family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0028, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0AFI0

Identification of Orthologs from Complete Genome Data

More...OMAi		PGPYGCL

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0AFI0

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029035, DHS-like_NAD/FAD-binding_dom
IPR045025, HACL1-like
IPR017660, Oxalyl-CoA_decarboxylase
IPR029061, THDP-binding
IPR012000, Thiamin_PyroP_enz_cen_dom
IPR012001, Thiamin_PyroP_enz_TPP-bd_dom
IPR011766, TPP_enzyme-bd_C

The PANTHER Classification System

More...PANTHERi		PTHR43710, PTHR43710, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02775, TPP_enzyme_C, 1 hit
PF00205, TPP_enzyme_M, 1 hit
PF02776, TPP_enzyme_N, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52467, SSF52467, 1 hit
SSF52518, SSF52518, 2 hits

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR03254, oxalate_oxc, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P0AFI0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDQLQMTDG MHIIVEALKQ NNIDTIYGVV GIPVTDMARH AQAEGIRYIG 
        60         70         80         90        100
FRHEQSAGYA AAASGFLTQK PGICLTVSAP GFLNGLTALA NATVNGFPMI 
       110        120        130        140        150
MISGSSDRAI VDLQQGDYEE LDQMNAAKPY AKAAFRVNQP QDLGIALARA 
       160        170        180        190        200
IRVSVSGRPG GVYLDLPANV LAATMEKDEA LTTIVKVENP SPALLPCPKS 
       210        220        230        240        250
VTSAISLLAK AERPLIILGK GAAYSQADEQ LREFIESAQI PFLPMSMAKG 
       260        270        280        290        300
ILEDTHPLSA AAARSFALAN ADVVMLVGAR LNWLLAHGKK GWAADTQFIQ 
       310        320        330        340        350
LDIEPQEIDS NRPIAVPVVG DIASSMQGML AELKQNTFTT PLVWRDILNI 
       360        370        380        390        400
HKQQNAQKMH EKLSTDTQPL NYFNALSAVR DVLRENQDIY LVNEGANTLD 
       410        420        430        440        450
NARNIIDMYK PRRRLDCGTW GVMGIGMGYA IGASVTSGSP VVAIEGDSAF 
       460        470        480        490        500
GFSGMEIETI CRYNLPVTIV IFNNGGIYRG DGVDLSGAGA PSPTDLLHHA 
       510        520        530        540        550
RYDKLMDAFR GVGYNVTTTD ELRHALTTGI QSRKPTIINV VIDPAAGTES 
       560 
GHITKLNPKQ VAGN
Length:564
Mass (Da):60,581
Last modified:December 20, 2005 - v1
<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:i94418B2BE7D40C17
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
U00096 Genomic DNA Translation: AAC75432.1
AP009048 Genomic DNA Translation: BAA16245.1

Protein sequence database of the Protein Information Resource

More...PIRi		B65011

NCBI Reference Sequences

More...RefSeqi		NP_416874.1, NC_000913.3
WP_001283490.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75432; AAC75432; b2373
BAA16245; BAA16245; BAA16245

Database of genes from NCBI RefSeq genomes

More...GeneIDi		946845

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW2370
eco:b2373

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.4356

<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
U00096 Genomic DNA Translation: AAC75432.1
AP009048 Genomic DNA Translation: BAA16245.1
PIRiB65011
RefSeqiNP_416874.1, NC_000913.3
WP_001283490.1, NZ_LN832404.1

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
2Q27X-ray2.12A/B1-564[»]
2Q28X-ray1.74A/B1-564[»]
2Q29X-ray1.82A/B1-564[»]
AlphaFoldDBiP0AFI0
SMRiP0AFI0
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4260862, 15 interactors
851186, 1 interactor
DIPiDIP-48075N
IntActiP0AFI0, 6 interactors
MINTiP0AFI0
STRINGi511145.b2373

Proteomic databases

PaxDbiP0AFI0
PRIDEiP0AFI0

Genome annotation databases

EnsemblBacteriaiAAC75432; AAC75432; b2373
BAA16245; BAA16245; BAA16245
GeneIDi946845
KEGGiecj:JW2370
eco:b2373
PATRICifig|1411691.4.peg.4356

Organism-specific databases

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

More...EchoBASEi		EB3895

Phylogenomic databases

eggNOGiCOG0028, Bacteria
InParanoidiP0AFI0
OMAiPGPYGCL
PhylomeDBiP0AFI0

Enzyme and pathway databases

UniPathwayiUPA00540;UER00599
BioCyciEcoCyc:G7236-MONOMER
BRENDAi4.1.1.8, 2026

Miscellaneous databases

EvolutionaryTraceiP0AFI0

Protein Ontology

More...PROi		PR:P0AFI0

Family and domain databases

InterProiView protein in InterPro
IPR029035, DHS-like_NAD/FAD-binding_dom
IPR045025, HACL1-like
IPR017660, Oxalyl-CoA_decarboxylase
IPR029061, THDP-binding
IPR012000, Thiamin_PyroP_enz_cen_dom
IPR012001, Thiamin_PyroP_enz_TPP-bd_dom
IPR011766, TPP_enzyme-bd_C
PANTHERiPTHR43710, PTHR43710, 1 hit
PfamiView protein in Pfam
PF02775, TPP_enzyme_C, 1 hit
PF00205, TPP_enzyme_M, 1 hit
PF02776, TPP_enzyme_N, 1 hit
SUPFAMiSSF52467, SSF52467, 1 hit
SSF52518, SSF52518, 2 hits
TIGRFAMsiTIGR03254, oxalate_oxc, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiOXC_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: P0AFI0
Secondary accession number(s): P78093, P78194, P78195
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 25, 2022
This is version 119 of the entry and version 1 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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