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Entry version 117 (12 Aug 2020)
Sequence version 1 (01 Feb 2005)
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Protein

Propionyl-CoA carboxylase alpha chain

Gene

pccA

Organism
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
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

This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), the enzyme catalyzing the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (PubMed:20725044). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then tranfers the carboxyl group from carboxylated biotin to propionyl-CoA (Probable).1 Publication1 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 the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: propanoyl-CoA degradation

This protein is involved in step 1 of the subpathway that synthesizes succinyl-CoA from propanoyl-CoA.1 Publication
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Propionyl-CoA carboxylase alpha chain (pccA)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway propanoyl-CoA degradation, which is itself part of Metabolic intermediate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinyl-CoA from propanoyl-CoA, the pathway propanoyl-CoA degradation and in Metabolic intermediate 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 sitei116ATPBy similarity1
Binding sitei200ATPBy similarity1
Binding sitei235ATPBy similarity1
<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 bindingi275Magnesium or manganese 1PROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei288By similarity1
Metal bindingi288Magnesium or manganese 1PROSITE-ProRule annotation1
Metal bindingi288Magnesium or manganese 2PROSITE-ProRule annotation1
Metal bindingi290Magnesium or manganese 2PROSITE-ProRule annotation1
Binding sitei348Biotin; via carbonyl oxygenCombined sources1 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 bindingi148 – 209ATPPROSITE-ProRule annotationAdd BLAST62

<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 functionLigase
Biological processLipid degradation, Lipid metabolism
LigandATP-binding, Biotin, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
RPOM246200:G1G48-1120-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.4.1.3, 8123

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

More...
UniPathwayi
UPA00945;UER00908

<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:
Propionyl-CoA carboxylase alpha chain1 Publication (EC:6.4.1.31 Publication)
<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:pccAImported
Ordered Locus Names:SPO1101Imported
<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>OrganismiRuegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
<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 identifieri246200 [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 lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria
<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
  • UP000001023 <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 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%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>Mutagenesisi515W → L: No effect on holoenzyme formation. 1 Publication1
Mutagenesisi599L → A: Loss of holoenzyme formation; when associated with A-602 and A-603. 1 Publication1
Mutagenesisi602L → A: Loss of holoenzyme formation; when associated with A-602 and A-603. 1 Publication1
Mutagenesisi603M → A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603. 1 Publication1

<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_00004485761 – 681Propionyl-CoA carboxylase alpha chainAdd BLAST681

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei647N6-biotinyllysinePROSITE-ProRule annotationCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The biotin cofactor is covalently attached to the C-terminal biotinyl-binding domain and is required for the catalytic activity.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

The holoenzyme is a dodecamer composed of 6 PccA/alpha subunits and 6 PccB/beta subunits.

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

Hide details

Protein-protein interaction databases

Database of interacting proteins

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DIPi
DIP-59242N

Protein interaction database and analysis system

More...
IntActi
Q5LUF3, 2 interactors

STRING: functional protein association networks

More...
STRINGi
246200.SPO1101

<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

1681
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
Q5LUF3

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
Q5LUF3

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 466Biotin carboxylationPROSITE-ProRule annotationAdd BLAST466
Domaini120 – 317ATP-graspPROSITE-ProRule annotationAdd BLAST198
Domaini602 – 681Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST80

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Consists of an N-terminal biotin carboxylation/carboxylase (BC) domain that catalyzes the transient carboxylation of the biotin covalently attached to the C-terminal biotinyl-binding/biotin carboxyl carrier (BCC) domain.1 Publication

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG4770, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000395_3_3_5

KEGG Orthology (KO)

More...
KOi
K01965

Identification of Orthologs from Complete Genome Data

More...
OMAi
YFPRVRH

Database of Orthologous Groups

More...
OrthoDBi
361205at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1490.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011761, ATP-grasp
IPR013815, ATP_grasp_subdomain_1
IPR005481, BC-like_N
IPR001882, Biotin_BS
IPR011764, Biotin_carboxylation_dom
IPR005482, Biotin_COase_C
IPR000089, Biotin_lipoyl
IPR005479, CbamoylP_synth_lsu-like_ATP-bd
IPR041265, PCC_BT
IPR016185, PreATP-grasp_dom_sf
IPR011054, Rudment_hybrid_motif
IPR011053, Single_hybrid_motif

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02785, Biotin_carb_C, 1 hit
PF00289, Biotin_carb_N, 1 hit
PF00364, Biotin_lipoyl, 1 hit
PF02786, CPSase_L_D2, 1 hit
PF18140, PCC_BT, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00878, Biotin_carb_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51230, SSF51230, 1 hit
SSF51246, SSF51246, 1 hit
SSF52440, SSF52440, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50975, ATP_GRASP, 1 hit
PS50979, BC, 1 hit
PS00188, BIOTIN, 1 hit
PS50968, BIOTINYL_LIPOYL, 1 hit
PS00866, CPSASE_1, 1 hit
PS00867, CPSASE_2, 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.

Q5LUF3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFNKILIANR GEIACRVIKT ARKMGISTVA IYSDADKQAL HVQMADEAVH
60 70 80 90 100
IGPPPANQSY IVIDKVMAAI RATGAQAVHP GYGFLSENSK FAEALEAEGV
110 120 130 140 150
IFVGPPKGAI EAMGDKITSK KIAQEANVST VPGYMGLIED ADEAVKISNQ
160 170 180 190 200
IGYPVMIKAS AGGGGKGMRI AWNDQEAREG FQSSKNEAAN SFGDDRIFIE
210 220 230 240 250
KFVTQPRHIE IQVLCDSHGN GIYLGERECS IQRRNQKVVE EAPSPFLDEA
260 270 280 290 300
TRRAMGEQAV ALAKAVGYAS AGTVEFIVDG QKNFYFLEMN TRLQVEHPVT
310 320 330 340 350
ELITGVDLVE QMIRVAAGEP LSITQGDVKL TGWAIENRLY AEDPYRGFLP
360 370 380 390 400
SIGRLTRYRP PAETAAGPLL VNGKWQGDAP SGEAAVRNDT GVYEGGEISM
410 420 430 440 450
YYDPMIAKLC TWAPTRAAAI EAMRIALDSF EVEGIGHNLP FLSAVMDHPK
460 470 480 490 500
FISGDMTTAF IAEEYPEGFE GVNLPETDLR RVAAAAAAMH RVAEIRRTRV
510 520 530 540 550
SGRMDNHERR VGTEWVVTLQ GADFPVTIAA DHDGSTVSFD DGSSMRVTSD
560 570 580 590 600
WTPGDQLANL MVDGAPLVLK VGKISGGFRI RTRGADLKVH VRTPRQAELA
610 620 630 640 650
RLMPEKLPPD TSKMLLCPMP GLIVKVDVEV GQEVQEGQAL CTIEAMKMEN
660 670 680
ILRAEKKGVV AKINASAGNS LAVDDVIMEF E
Length:681
Mass (Da):73,862
Last modified:February 1, 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:iE9621118EF90D008
GO

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
CP000031 Genomic DNA Translation: AAV94401.1

NCBI Reference Sequences

More...
RefSeqi
WP_011046848.1, NC_003911.12

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAV94401; AAV94401; SPO1101

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sil:SPO1101

<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
CP000031 Genomic DNA Translation: AAV94401.1
RefSeqiWP_011046848.1, NC_003911.12

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
3N6RX-ray3.20A/C/E/G/I/K1-681[»]
SMRiQ5LUF3
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-59242N
IntActiQ5LUF3, 2 interactors
STRINGi246200.SPO1101

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
3193848

Genome annotation databases

EnsemblBacteriaiAAV94401; AAV94401; SPO1101
KEGGisil:SPO1101

Phylogenomic databases

eggNOGiCOG4770, Bacteria
HOGENOMiCLU_000395_3_3_5
KOiK01965
OMAiYFPRVRH
OrthoDBi361205at2

Enzyme and pathway databases

UniPathwayiUPA00945;UER00908
BioCyciRPOM246200:G1G48-1120-MONOMER
BRENDAi6.4.1.3, 8123

Miscellaneous databases

EvolutionaryTraceiQ5LUF3

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
InterProiView protein in InterPro
IPR011761, ATP-grasp
IPR013815, ATP_grasp_subdomain_1
IPR005481, BC-like_N
IPR001882, Biotin_BS
IPR011764, Biotin_carboxylation_dom
IPR005482, Biotin_COase_C
IPR000089, Biotin_lipoyl
IPR005479, CbamoylP_synth_lsu-like_ATP-bd
IPR041265, PCC_BT
IPR016185, PreATP-grasp_dom_sf
IPR011054, Rudment_hybrid_motif
IPR011053, Single_hybrid_motif
PfamiView protein in Pfam
PF02785, Biotin_carb_C, 1 hit
PF00289, Biotin_carb_N, 1 hit
PF00364, Biotin_lipoyl, 1 hit
PF02786, CPSase_L_D2, 1 hit
PF18140, PCC_BT, 1 hit
SMARTiView protein in SMART
SM00878, Biotin_carb_C, 1 hit
SUPFAMiSSF51230, SSF51230, 1 hit
SSF51246, SSF51246, 1 hit
SSF52440, SSF52440, 1 hit
PROSITEiView protein in PROSITE
PS50975, ATP_GRASP, 1 hit
PS50979, BC, 1 hit
PS00188, BIOTIN, 1 hit
PS50968, BIOTINYL_LIPOYL, 1 hit
PS00866, CPSASE_1, 1 hit
PS00867, CPSASE_2, 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 nameiPCCA_RUEPO
<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: Q5LUF3
<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: November 13, 2019
Last sequence update: February 1, 2005
Last modified: August 12, 2020
This is version 117 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
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