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Entry version 115 (08 May 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Formyl-CoA:oxalate CoA-transferase

Gene

frc

Organism
Oxalobacter formigenes
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). Essential enzyme for the bacterium survival, as it relies on oxalic acid as its sole source of energy. Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate. It can also use succinate as acceptor.5 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

Inhibited by the sulfhydryl reagents N-ethylmaleimide and p-chloromercuribenzoate, and by chloride. Competitively inhibited by acetyl-CoA.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 5.3 sec(-1) for CoA-transferase activity with formyl-CoA as substrate (with oxalate as acceptor at pH 6.7 and 30 degrees Celsius). Kcat is 149 sec(-1) for CoA-transferase activity with formyl-CoA as substrate (with succinate as acceptor at pH 6.7 and 30 degrees Celsius).1 Publication
  1. KM=2 µM for formyl-CoA (with oxalate as acceptor at pH 6.7 and 30 degrees Celsius)2 Publications
  2. KM=8 µM for formyl-CoA (with oxalate as acceptor at pH 6.7 and 30 degrees Celsius)1 Publication
  3. KM=16 µM for formyl-CoA (with succinate as acceptor at pH 6.7 and 30 degrees Celsius)1 Publication
  4. KM=0.32 mM for succinate (with formyl-CoA as donor at pH 6.7 and 30 degrees Celsius)1 Publication
  5. KM=2.3 mM for succinate (with formyl-CoA as donor at pH 6.8 and 25 degrees Celsius)1 Publication
  6. KM=3 mM for formyl-CoA (with oxalate as acceptor at pH 6.8 and 25 degrees Celsius)1 Publication
  7. KM=3.9 mM for oxalate (with formyl-CoA as donor at pH 6.7 and 30 degrees Celsius)2 Publications
  8. KM=5.1 mM for oxalate1 Publication
  1. Vmax=6.4 µmol/min/mg enzyme with oxalate as substrate (with formyl-CoA as donor at pH 6.8 and 25 degrees Celsius)1 Publication
  2. Vmax=19.2 µmol/min/mg enzyme with succinate as substrate (with formyl-CoA as donor at pH 6.8 and 25 degrees Celsius)1 Publication
  3. Vmax=29.6 µmol/min/mg enzyme with formyl-CoA as substrate (with oxalate as acceptor at pH 6.8 and 25 degrees Celsius)1 Publication

pH dependencei

Optimum pH is between 6.5 and 7.5.4 Publications

<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: oxalate degradation

This protein is involved in step 1 of the subpathway that synthesizes CO(2) and formate from oxalate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Formyl-CoA:oxalate CoA-transferase (frc)
  2. Oxalyl-CoA decarboxylase (oxc)
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 ‘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 sitei38Coenzyme AUniRule annotation3 Publications1
Binding sitei104Coenzyme AUniRule annotation3 Publications1
<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 sitei169NucleophileUniRule annotation1 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

GO - Biological processi

<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 functionTransferase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-16179

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.8.3.16 4478

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

More...
UniPathwayi
UPA00540;UER00598

<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:
Formyl-CoA:oxalate CoA-transferase (EC:2.8.3.16UniRule annotation)
Short name:
FCOCT
Alternative name(s):
Formyl-coenzyme A transferaseUniRule annotation
<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:frcUniRule annotation
<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>OrganismiOxalobacter formigenes
<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 identifieri847 [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 lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceaeOxalobacter

<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

Keywords - Cellular componenti

Cytoplasm

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi17Q → A: 45-fold decrease of the catalytic effiency. 1 Publication1
Mutagenesisi48W → F: Little change in the affinity binding and catalytic efficiency, and it does not display major structural changes. 1 Publication1
Mutagenesisi48W → P: Little change in the affinity binding and catalytic efficiency. It exhibits substrate inhibition with oxalate. It does not display major structural changes. 1 Publication1
Mutagenesisi169D → A: Loss of CoA-transferase activity. 1 Publication1
Mutagenesisi169D → E: Loss of CoA-transferase activity. 1 Publication1
Mutagenesisi169D → S: Loss of CoA-transferase activity. 1 Publication1
Mutagenesisi259G → A: 2.5-fold decrease of the catalytic effiency. 1 Publication1
Mutagenesisi260G → A: 25-fold decrease of the catalytic effiency. Reduction of the affinity binding for both formyl-CoA and oxalate. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB01992 Coenzyme A
DB01846 Oxidized Coenzyme A

<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 methionineiRemoved
<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_00001947202 – 428Formyl-CoA:oxalate CoA-transferaseAdd BLAST427

<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

Homodimer.UniRule annotation5 Publications

<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

1428
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
1P5HX-ray2.20A/B1-428[»]
1P5RX-ray2.50A/B1-428[»]
1T3ZX-ray2.30A/B2-428[»]
1T4CX-ray2.61A/B2-428[»]
1VGQX-ray2.13A/B2-428[»]
1VGRX-ray2.10A/B2-428[»]
2VJKX-ray1.97A/B1-428[»]
2VJLX-ray2.00A/B1-428[»]
2VJMX-ray1.89A/B1-428[»]
2VJNX-ray2.00A/B1-428[»]
2VJOX-ray2.20A/B1-428[»]
2VJPX-ray1.95A/B1-428[»]
2VJQX-ray1.80A/B/C/D1-428[»]

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

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SMRi
O06644

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
O06644

<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>Regioni15 – 18Coenzyme A binding4
Regioni72 – 75Coenzyme A binding4
Regioni96 – 98Coenzyme A binding3
Regioni137 – 140Coenzyme A binding4
Regioni260 – 262Substrate binding3

<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 CaiB/BaiF CoA-transferase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C04 Bacteria
COG1804 LUCA

KEGG Orthology (KO)

More...
KOi
K07749

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.10540, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00742 Formyl_CoA_transfer, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003673 CoA-Trfase_fam_III
IPR023606 CoA-Trfase_III_dom_sf
IPR017659 Formyl_CoA_transfer

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02515 CoA_transf_3, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF89796 SSF89796, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03253 oxalate_frc, 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.

O06644-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTKPLDGINV LDFTHVQAGP ACTQMMGFLG ANVIKIERRG SGDMTRGWLQ
60 70 80 90 100
DKPNVDSLYF TMFNCNKRSI ELDMKTPEGK ELLEQMIKKA DVMVENFGPG
110 120 130 140 150
ALDRMGFTWE YIQELNPRVI LASVKGYAEG HANEHLKVYE NVAQCSGGAA
160 170 180 190 200
ATTGFWDGPP TVSGAALGDS NSGMHLMIGI LAALEMRHKT GRGQKVAVAM
210 220 230 240 250
QDAVLNLVRI KLRDQQRLER TGILAEYPQA QPNFAFDRDG NPLSFDNITS
260 270 280 290 300
VPRGGNAGGG GQPGWMLKCK GWETDADSYV YFTIAANMWP QICDMIDKPE
310 320 330 340 350
WKDDPAYNTF EGRVDKLMDI FSFIETKFAD KDKFEVTEWA AQYGIPCGPV
360 370 380 390 400
MSMKELAHDP SLQKVGTVVE VVDEIRGNHL TVGAPFKFSG FQPEITRAPL
410 420
LGEHTDEVLK ELGLDDAKIK ELHAKQVV
Length:428
Mass (Da):47,327
Last modified:January 23, 2007 - v3
<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:i386E87C19EA0C8AC
GO

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 47196 Da from positions 1 - 428. Determined by ESI. 1 Publication

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
U82167 Genomic DNA Translation: AAC45298.1

NCBI Reference Sequences

More...
RefSeqi
WP_005880857.1, NZ_CP018787.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:AAC45298
ofo:BRW83_1110

<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
U82167 Genomic DNA Translation: AAC45298.1
RefSeqiWP_005880857.1, NZ_CP018787.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P5HX-ray2.20A/B1-428[»]
1P5RX-ray2.50A/B1-428[»]
1T3ZX-ray2.30A/B2-428[»]
1T4CX-ray2.61A/B2-428[»]
1VGQX-ray2.13A/B2-428[»]
1VGRX-ray2.10A/B2-428[»]
2VJKX-ray1.97A/B1-428[»]
2VJLX-ray2.00A/B1-428[»]
2VJMX-ray1.89A/B1-428[»]
2VJNX-ray2.00A/B1-428[»]
2VJOX-ray2.20A/B1-428[»]
2VJPX-ray1.95A/B1-428[»]
2VJQX-ray1.80A/B/C/D1-428[»]
SMRiO06644
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB01992 Coenzyme A
DB01846 Oxidized Coenzyme A

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC45298
ofo:BRW83_1110

Phylogenomic databases

eggNOGiENOG4105C04 Bacteria
COG1804 LUCA
KOiK07749

Enzyme and pathway databases

UniPathwayi
UPA00540;UER00598

BioCyciMetaCyc:MONOMER-16179
BRENDAi2.8.3.16 4478

Miscellaneous databases

EvolutionaryTraceiO06644

Family and domain databases

Gene3Di3.40.50.10540, 1 hit
HAMAPiMF_00742 Formyl_CoA_transfer, 1 hit
InterProiView protein in InterPro
IPR003673 CoA-Trfase_fam_III
IPR023606 CoA-Trfase_III_dom_sf
IPR017659 Formyl_CoA_transfer
PfamiView protein in Pfam
PF02515 CoA_transf_3, 2 hits
SUPFAMiSSF89796 SSF89796, 1 hit
TIGRFAMsiTIGR03253 oxalate_frc, 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 nameiFCTA_OXAFO
<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: O06644
<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: June 20, 2002
Last sequence update: January 23, 2007
Last modified: May 8, 2019
This is version 115 of the entry and version 3 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

Documents

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