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UniProtKB - Q56063 (PRPC_SALTY)

Entry version 117 (08 May 2019)
Sequence version 2 (23 Jan 2002)
Previous versions | rss
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Protein

2-methylcitrate synthase

Gene

prpC

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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 short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA or butyryl-CoA but with a lower specificity.2 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 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 1.4 sec(-1) for citrate synthase activity with acetyl-CoA as substrate. Kcat is 1.87 sec(-1) for citrate synthase activity with acetyl-CoA as substrate (at pH 8 and 30 degrees Celsius). Kcat is 7.4 sec(-1) for 2-methylcitrate synthase activity with propionyl-CoA as substrate. Kcat is 8.25 sec(-1) for 2-methylcitrate synthase activity with propionyl-CoA as substrate (at pH 8 and 30 degrees Celsius).2 Publications
  1. KM=12 µM for oxaloacetate (with propionyl-CoA)1 Publication
  2. KM=13 µM for oxaloacetate (with propionyl-CoA at pH 8 and 30 degrees Celsius)1 Publication
  3. KM=14 µM for oxaloacetate (with acetyl-CoA)1 Publication
  4. KM=15 µM for oxaloacetate (with acetyl-CoA at pH 8 and 30 degrees Celsius)1 Publication
  5. KM=45 µM for propionyl-CoA (at pH 8 and 30 degrees Celsius)1 Publication
  6. KM=48 µM for propionyl-CoA1 Publication
  7. KM=265 µM for acetyl-CoA (at pH 8 and 30 degrees Celsius)1 Publication
  8. KM=285 µM for acetyl-CoA1 Publication
  1. Vmax=2 µmol/min/mg enzyme with acetyl-CoA as substrate1 Publication
  2. Vmax=2.5 µmol/min/mg enzyme with acetyl-CoA as substrate (at pH 8 and 30 degrees Celsius)1 Publication
  3. Vmax=10 µmol/min/mg enzyme with propionyl-CoA as substrate1 Publication
  4. Vmax=11 µmol/min/mg enzyme with propionyl-CoA as substrate (at pH 8 and 30 degrees Celsius)1 Publication

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

This protein is involved in the pathway propanoate degradation, which is part of Organic acid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway propanoate degradation and in Organic acid metabolism.

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes isocitrate from oxaloacetate.1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Citrate synthase (gltA), 2-methylcitrate synthase (prpC)
  2. 2-methylcitrate dehydratase (prpD), Aconitate hydratase A (acnA), Aconitate hydratase B (acnB)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isocitrate from oxaloacetate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei82SubstrateBy similarity1
Binding sitei200SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei235By similarity1 Publication1
Active sitei274By similarity1 Publication1
Binding sitei283SubstrateBy similarity1
Active sitei325By similarity1 Publication1
Binding sitei350SubstrateBy similarity1
Binding sitei369SubstrateBy similarity1

<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 functionTransferase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:MONOMER-63
SENT99287:STM0369-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.3.5 5542

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

More...UniPathwayi		UPA00223;UER00717
UPA00946

<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:
2-methylcitrate synthase1 Publication (EC:2.3.3.52 Publications)
Short name:
2-MCS1 Publication
Short name:
mcs1 Publication
Alternative name(s):
Citrate synthase1 Publication (EC:2.3.3.162 Publications)
<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:prpC1 Publication
Ordered Locus Names:STM0369
<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>OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
<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 identifieri99287 [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 › Salmonella ›
<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
  • UP000001014 <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

<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 ...

<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

Cells lacking this gene are unable to accumulate propionyl-CoA.1 Publication

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001699821 – 3892-methylcitrate synthaseAdd BLAST389

Proteomic databases

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

More...PaxDbi		Q56063

PRoteomics IDEntifications database

More...PRIDEi		Q56063

<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 at low concentrations and converted to a larger oligomers at higher concentrations.

2 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

1389
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		Q56063

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		Q56063

<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>Regioni268 – 272Coenzyme A bindingBy similarity5

<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 citrate synthase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105BZN Bacteria
COG0372 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000021225

KEGG Orthology (KO)

More...KOi		K01659

Identification of Orthologs from Complete Genome Data

More...OMAi		NFLWMTF

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q56063

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.230.10, 1 hit
1.10.580.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR011278 2-MeCitrate/Citrate_synth_II
IPR016142 Citrate_synth-like_lrg_a-sub
IPR016143 Citrate_synth-like_sm_a-sub
IPR002020 Citrate_synthase
IPR019810 Citrate_synthase_AS
IPR024176 Citrate_synthase_bac-typ
IPR036969 Citrate_synthase_sf

The PANTHER Classification System

More...PANTHERi		PTHR11739 PTHR11739, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00285 Citrate_synt, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001369 Citrate_synth, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00143 CITRTSNTHASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48256 SSF48256, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01800 cit_synth_II, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00480 CITRATE_SYNTHASE, 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>. 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_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.

Q56063-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTDTTILQNN THVIKPKKSV ALSGVPAGNT ALCTVGKSGN DLHYRGYDIL 
        60         70         80         90        100
DLAEHCEFEE VAHLLIHGKL PTRDELNAYK SKLKALRGLP ANVRTVLEAL 
       110        120        130        140        150
PAASHPMDVM RTGVSALGCT LPEKEGHTVS GARDIADKLL ASLSSILLYW 
       160        170        180        190        200
YHYSHNGERI QPETDDDSIG GHFLHLLHGE KPTQSWEKAM HISLVLYAEH 
       210        220        230        240        250
EFNASTFTSR VIAGTGSDVY SAIIGAIGAL RGPKHGGANE VSLEIQQRYE 
       260        270        280        290        300
TPDEAEADIR KRVENKEVVI GFGHPVYTIA DPRHQVIKRV AKQLSEEGGS 
       310        320        330        340        350
LKMYHIADRL ETVMWETKKM FPNLDWFSAV SYNMMGVPTE MFTPLFVIAR 
       360        370        380 
VTGWAAHIIE QRQDNKIIRP SANYTGPEDR PFVSIDDRC
Length:389
Mass (Da):43,173
Last modified:January 23, 2002 - 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:i0927008F1E5F38D4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti144S → N in AAC44815 (PubMed:9006051).Curated1

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
U51879 Genomic DNA Translation: AAC44815.1
AE006468 Genomic DNA Translation: AAL19323.1

NCBI Reference Sequences

More...RefSeqi		NP_459364.1, NC_003197.2
WP_000132749.1, NC_003197.2

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAL19323; AAL19323; STM0369

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1251888

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		stm:STM0369

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|99287.12.peg.391

<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
U51879 Genomic DNA Translation: AAC44815.1
AE006468 Genomic DNA Translation: AAL19323.1
RefSeqiNP_459364.1, NC_003197.2
WP_000132749.1, NC_003197.2

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
3O8JX-ray2.41A/B/C/D/E/F/G/H/I/J1-389[»]
SMRiQ56063
ModBaseiSearch...
PDBe-KBiSearch...

Proteomic databases

PaxDbiQ56063
PRIDEiQ56063

Genome annotation databases

EnsemblBacteriaiAAL19323; AAL19323; STM0369
GeneIDi1251888
KEGGistm:STM0369
PATRICifig|99287.12.peg.391

Phylogenomic databases

eggNOGiENOG4105BZN Bacteria
COG0372 LUCA
HOGENOMiHOG000021225
KOiK01659
OMAiNFLWMTF
PhylomeDBiQ56063

Enzyme and pathway databases

UniPathwayiUPA00223;UER00717
UPA00946
BioCyciMetaCyc:MONOMER-63
SENT99287:STM0369-MONOMER
BRENDAi2.3.3.5 5542

Miscellaneous databases

EvolutionaryTraceiQ56063

Family and domain databases

Gene3Di1.10.230.10, 1 hit
1.10.580.10, 1 hit
InterProiView protein in InterPro
IPR011278 2-MeCitrate/Citrate_synth_II
IPR016142 Citrate_synth-like_lrg_a-sub
IPR016143 Citrate_synth-like_sm_a-sub
IPR002020 Citrate_synthase
IPR019810 Citrate_synthase_AS
IPR024176 Citrate_synthase_bac-typ
IPR036969 Citrate_synthase_sf
PANTHERiPTHR11739 PTHR11739, 1 hit
PfamiView protein in Pfam
PF00285 Citrate_synt, 1 hit
PIRSFiPIRSF001369 Citrate_synth, 1 hit
PRINTSiPR00143 CITRTSNTHASE
SUPFAMiSSF48256 SSF48256, 1 hit
TIGRFAMsiTIGR01800 cit_synth_II, 1 hit
PROSITEiView protein in PROSITE
PS00480 CITRATE_SYNTHASE, 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 nameiPRPC_SALTY
<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: Q56063
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2002
Last modified: May 8, 2019
This is version 117 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, Reference proteome

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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