Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P32397 (CGOX_BACSU)

Entry version 150 (12 Aug 2020)
Sequence version 1 (01 Oct 1993)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Coproporphyrinogen III oxidase

Gene

cgoX

Organism
Bacillus subtilis (strain 168)
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 coproporphyrin-dependent heme b biosynthesis (PubMed:7928957, PubMed:9217019). Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III (PubMed:8288631, PubMed:7928957, PubMed:9217019, PubMed:9784236). Can also oxidize protoporphyrinogen IX to protoporphyrin-IX (PubMed:8288631, PubMed:7928957, PubMed:9217019, PubMed:9784236, PubMed:19944166). The specific activity for the oxidation of coproporphyrinogen III is much higher than that for the oxidation of protoporphyrinogen IX (PubMed:7928957, PubMed:9217019). Can also oxidize mesoporphyrinogen IX, but not uroporphyrinogen III (PubMed:8288631, PubMed:9784236, PubMed:7928957).5 Publications

<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

FAD4 PublicationsNote: Binds 1 FAD per subunit.1 Publication

<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

Only weakly inhibited by acifluorfen, in contrast to eukaryotic family members (PubMed:8288631, PubMed:9784236, PubMed:19944166). Weakly inhibited by methylacifluorfen (PubMed:9784236). Bilirubin, biliverdin and hemin are all competitive inhibitors (PubMed:9784236).3 Publications

<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 0.05 min(-1) with coproporphyrinogen III as substrate (PubMed:9784236). kcat is 0.19 min(-1) with protoporphyrinogen IX as substrate (PubMed:9784236). kcat is 2.69 min(-1) with mesoporphyrinogen IX as substrate (PubMed:9784236).1 Publication
  1. KM=0.56 µM for coproporphyrinogen III1 Publication
  2. KM=5.29 µM for coproporphyrinogen III1 Publication
  3. KM=0.95 µM for protoporphyrinogen IX1 Publication
  4. KM=10.4 µM for protoporphyrinogen IX1 Publication
  5. KM=1.0 µM for protoporphyrinogen IX1 Publication
  6. KM=21.1 µM for mesoporphyrinogen IX1 Publication
  7. KM=4.92 µM for mesoporphyrinogen IX1 Publication
  1. Vmax=7.0 nmol/min/mg enzyme with coproporphyrinogen III as substrate1 Publication
  2. Vmax=0.98 nmol/min/mg enzyme with coproporphyrinogen III as substrate1 Publication
  3. Vmax=0.85 nmol/min/mg enzyme with protoporphyrinogen IX as substrate1 Publication
  4. Vmax=3.7 nmol/min/mg enzyme with protoporphyrinogen IX as substrate1 Publication
  5. Vmax=45 nmol/min/mg enzyme with mesoporphyrinogen IX as substrate1 Publication

pH dependencei

Optimum pH is 8.7 (for protoporphyrinogen oxidation).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: protoheme biosynthesis

This protein is involved in the pathway protoheme biosynthesis, which is part of Porphyrin-containing compound metabolism.1 Publication2 Publications
View all proteins of this organism that are known to be involved in the pathway protoheme biosynthesis and in Porphyrin-containing compound metabolism.

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 sitei49FAD; via amide nitrogen1 Publication1
Binding sitei256FAD; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei409FAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi12 – 17FAD1 Publication6
Nucleotide bindingi41 – 42FAD1 Publication2
Nucleotide bindingi63 – 66FAD1 Publication4
Nucleotide bindingi448 – 450FAD1 Publication3

<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 functionOxidoreductase
Biological processHeme biosynthesis
LigandFAD, Flavoprotein

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		BSUB:BSU10140-MONOMER
MetaCyc:BSU10140-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.3.3.4, 658

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P32397

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

More...UniPathwayi		UPA00252

<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:
Coproporphyrinogen III oxidaseCurated (EC:1.3.3.154 Publications)
<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:cgoX1 Publication
Synonyms:hemG1 Publication, hemY1 Publication
Ordered Locus Names:BSU10140
<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>OrganismiBacillus subtilis (strain 168)
<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 identifieri224308 [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 › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›
<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
  • UP000001570 <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

<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

Complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutations cause the accumulation of coproporphyrinogen III or coproporphyrin III in the growth medium and the accumulation of trace amounts of other porphyrinogens or porphyrins intracellularly.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi64P → A: Decreased affinity for protoporphyrinogen-IX. 1 Publication1
Mutagenesisi71K → A: Strongly decreased catalytic activity. 1 Publication1
Mutagenesisi176I → A: Strongly decreased catalytic activity. 1 Publication1
Mutagenesisi227F → R: Decreased affinity for protoporphyrinogen-IX. 1 Publication1
Mutagenesisi366Y → A or H: Reduces protoporphyrinogen oxidation by 90%. 1 Publication1
Mutagenesisi366Y → E: Reduces protoporphyrinogen oxidation by 99%. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1075048

Drug and drug target database

More...DrugBanki		DB07338, Acifluorfen

<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_00001352631 – 470Coproporphyrinogen III oxidaseAdd BLAST470

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P32397

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

More...PaxDbi		P32397

PRoteomics IDEntifications database

More...PRIDEi		P32397

<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

Monomer.

3 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		224308.BSU10140

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P32397

<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

1470
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P32397

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		P32397

<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 protoporphyrinogen/coproporphyrinogen oxidase family. Coproporphyrinogen III oxidase subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1232, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P32397

KEGG Orthology (KO)

More...KOi		K00231

Identification of Orthologs from Complete Genome Data

More...OMAi		IFDSCCF

Database for complete collections of gene phylogenies

More...PhylomeDBi		P32397

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.50.50.60, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002937, Amino_oxidase
IPR036188, FAD/NAD-bd_sf
IPR004572, Protoporphyrinogen_oxidase

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01593, Amino_oxidase, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51905, SSF51905, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00562, proto_IX_ox, 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.

P32397-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDGKKHVVI IGGGITGLAA AFYMEKEIKE KNLPLELTLV EASPRVGGKI 
        60         70         80         90        100
QTVKKDGYII ERGPDSFLER KKSAPQLVKD LGLEHLLVNN ATGQSYVLVN 
       110        120        130        140        150
RTLHPMPKGA VMGIPTKIAP FVSTGLFSLS GKARAAMDFI LPASKTKDDQ 
       160        170        180        190        200
SLGEFFRRRV GDEVVENLIE PLLSGIYAGD IDKLSLMSTF PQFYQTEQKH 
       210        220        230        240        250
RSLILGMKKT RPQGSGQQLT AKKQGQFQTL STGLQTLVEE IEKQLKLTKV 
       260        270        280        290        300
YKGTKVTKLS HSGSCYSLEL DNGVTLDADS VIVTAPHKAA AGMLSELPAI 
       310        320        330        340        350
SHLKNMHSTS VANVALGFPE GSVQMEHEGT GFVISRNSDF AITACTWTNK 
       360        370        380        390        400
KWPHAAPEGK TLLRAYVGKA GDESIVDLSD NDIINIVLED LKKVMNINGE 
       410        420        430        440        450
PEMTCVTRWH ESMPQYHVGH KQRIKELREA LASAYPGVYM TGASFEGVGI 
       460        470
PDCIDQGKAA VSDALTYLFS
Length:470
Mass (Da):51,203
Last modified:October 1, 1993 - 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:i95CC4E5847686D2E
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
M97208 Genomic DNA Translation: AAA22519.1
Y14083 Genomic DNA Translation: CAA74520.1
AL009126 Genomic DNA Translation: CAB12854.1

Protein sequence database of the Protein Information Resource

More...PIRi		D47045

NCBI Reference Sequences

More...RefSeqi		NP_388895.1, NC_000964.3
WP_003245394.1, NZ_JNCM01000035.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		CAB12854; CAB12854; BSU10140

Database of genes from NCBI RefSeq genomes

More...GeneIDi		936311

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		bsu:BSU10140

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|224308.179.peg.1090

<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
M97208 Genomic DNA Translation: AAA22519.1
Y14083 Genomic DNA Translation: CAA74520.1
AL009126 Genomic DNA Translation: CAB12854.1
PIRiD47045
RefSeqiNP_388895.1, NC_000964.3
WP_003245394.1, NZ_JNCM01000035.1

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
3I6DX-ray2.90A/B1-470[»]
SMRiP32397
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU10140

Chemistry databases

BindingDBiP32397
ChEMBLiCHEMBL1075048
DrugBankiDB07338, Acifluorfen

Proteomic databases

jPOSTiP32397
PaxDbiP32397
PRIDEiP32397

Genome annotation databases

EnsemblBacteriaiCAB12854; CAB12854; BSU10140
GeneIDi936311
KEGGibsu:BSU10140
PATRICifig|224308.179.peg.1090

Phylogenomic databases

eggNOGiCOG1232, Bacteria
InParanoidiP32397
KOiK00231
OMAiIFDSCCF
PhylomeDBiP32397

Enzyme and pathway databases

UniPathwayiUPA00252
BioCyciBSUB:BSU10140-MONOMER
MetaCyc:BSU10140-MONOMER
BRENDAi1.3.3.4, 658
SABIO-RKiP32397

Miscellaneous databases

EvolutionaryTraceiP32397

Protein Ontology

More...PROi		PR:P32397

Family and domain databases

Gene3Di3.50.50.60, 1 hit
InterProiView protein in InterPro
IPR002937, Amino_oxidase
IPR036188, FAD/NAD-bd_sf
IPR004572, Protoporphyrinogen_oxidase
PfamiView protein in Pfam
PF01593, Amino_oxidase, 1 hit
SUPFAMiSSF51905, SSF51905, 1 hit
TIGRFAMsiTIGR00562, proto_IX_ox, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiCGOX_BACSU
<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: P32397
<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: October 1, 1993
Last sequence update: October 1, 1993
Last modified: August 12, 2020
This is version 150 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, Direct protein sequencing, 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again