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Entry version 159 (02 Jun 2021)
Sequence version 2 (15 Feb 2005)
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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
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

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.

2 Publications

Miscellaneous

RuBisCO folding and assembly commences when the nascent large subunit folds with the help of the chaperonin GroEL-GroES. Monomers require chaperone RbcX2 to assemble into RbcL8 octamers yielding RbcL8-(RbcX2)8 (PubMed:17574029) (Probable). RbcX2 is displaced by RbcS; as RbcX2 is removed RbcS mediates the ordering of an internal RbcL loop (Thr-64-Leu-70) in a catalytically active conformation (PubMed:17574029, PubMed:21765418) (Probable).2 Publications2 Publications
The basic functional RuBisCO is composed of a large chain homodimer in a 'head-to-tail' conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric 'cap' on each end of the 'barrel'.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

The CO2/O2 specificity factor (tau) is 39.
  1. KM=39 µM for ribulose 1,5-bisphosphate1 Publication
  2. KM=173 µM for CO21 Publication
  1. Vmax=2.5 µmol/min/mg enzyme with CO2 as substrate1 Publication

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 sitei120Substrate; in homodimeric partner1
Binding sitei170Substrate1
<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 sitei172Proton acceptor1
Binding sitei174Substrate1
<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 bindingi198Magnesium; via carbamate group1 Publication1
Metal bindingi200Magnesium1 Publication1
Metal bindingi201Magnesium1 Publication1
Active sitei291Proton acceptor1
Binding sitei292Substrate1
Binding sitei324Substrate1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei331Transition state stabilizer1
Binding sitei376Substrate1

<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 functionLyase, Monooxygenase, Oxidoreductase
Biological processCalvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
SELO269084:G1G2F-139-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P00880

<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:
Ribulose bisphosphate carboxylase large chain (EC:4.1.1.392 Publications)
Short name:
RuBisCO large subunit
<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:cbbL
Synonyms:rbcA, rbcL
Ordered Locus Names:syc0130_c
<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>OrganismiSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
<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 identifieri269084 [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 lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
<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
  • UP000001175 <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

Keywords - Cellular componenti

Bacterial microcompartment, Carboxysome

<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>Mutagenesisi49E → A or C: Does not form the RbcL8-(RbcX2)8 complex. 1 Publication1
Mutagenesisi53A → H: Wild-type formation of the RbcL8-(RbcX2)8 complex. 1 Publication1
Mutagenesisi67 – 71WTDLL → ATDGA: Alters the RbcL-RbcS interface, RbcS cannot displace RbcX2 from assembly intermediate. 1 Publication5
Mutagenesisi106E → Q: Protein aggregates, forms RbcL2-RbcX(2)2 homodimer intermediate poorly. 1 Publication1
Mutagenesisi126A → Y: Reduced formation of the RbcL8-(RbcX2)8 complex. 1 Publication1
Mutagenesisi212R → S: Forms stable homodimer in presence of RbcX2 but does not form RbcL8 form. 1 Publication1
Mutagenesisi461 – 472Missing : Remains bound to GroEL. 1 PublicationAdd BLAST12
Mutagenesisi464F → A: Remains bound to GroEL. 1 Publication1
Mutagenesisi466F → A: Remains bound to GroEL. 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_00000626511 – 472Ribulose bisphosphate carboxylase large chainAdd BLAST472

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 residuei198N6-carboxylysine1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi244Interchain; in linked form1 Publication

<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 disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.1 Publication

Keywords - PTMi

Disulfide bond

<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

Heterohexadecamer of 8 large chains and 8 small chains (PubMed:9882445, PubMed:17574029, PubMed:7922027); disulfide-linked (PubMed:8245022). The disulfide link is formed within the large subunit homodimers (PubMed:8245022, PubMed:7922027, PubMed:17574029) (Probable). The exposed C-terminus binds in a cleft in the RbcX2 (shown with endogenous and Anabaena strain CA protein) (PubMed:20075914, PubMed:21765418). RbcX2 is displaced by RbcS; as RbcX2 is removed RbcS mediates the ordering of an internal RbcL loop (Thr-64-Leu-70) in a catalytically active conformation (PubMed:17574029, PubMed:21765418) (Probable).

3 Publications5 Publications

<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

More...
DIPi
DIP-6210N

Protein interaction database and analysis system

More...
IntActi
P00880, 2 interactors

STRING: functional protein association networks

More...
STRINGi
269084.syc0130_c

<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

1472
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

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SMRi
P00880

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
P00880

<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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi461 – 467Interacts with RbcX21 Publication7

<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

Binding of RbcS probably induces a conformation change that displaces RbcX2 and triggers the final mature conformation.1 Publication1 Publication

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1850, Bacteria

Identification of Orthologs from Complete Genome Data

More...
OMAi
IHGHPDG

Family and domain databases

Conserved Domains Database

More...
CDDi
cd08212, RuBisCO_large_I, 1 hit

Database of protein disorder

More...
DisProti
DP02960

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.110, 1 hit
3.30.70.150, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01338, RuBisCO_L_type1, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR033966, RuBisCO
IPR020878, RuBisCo_large_chain_AS
IPR000685, RuBisCO_lsu_C
IPR036376, RuBisCO_lsu_C_sf
IPR017443, RuBisCO_lsu_fd_N
IPR036422, RuBisCO_lsu_N_sf
IPR020888, RuBisCO_lsuI

The PANTHER Classification System

More...
PANTHERi
PTHR42704, PTHR42704, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00016, RuBisCO_large, 1 hit
PF02788, RuBisCO_large_N, 1 hit

Structure-Function Linkage Database

More...
SFLDi
SFLDS00014, RuBisCO, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51649, SSF51649, 1 hit
SSF54966, SSF54966, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00157, RUBISCO_LARGE, 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.

P00880-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPKTQSAAGY KAGVKDYKLT YYTPDYTPKD TDLLAAFRFS PQPGVPADEA
60 70 80 90 100
GAAIAAESST GTWTTVWTDL LTDMDRYKGK CYHIEPVQGE ENSYFAFIAY
110 120 130 140 150
PLDLFEEGSV TNILTSIVGN VFGFKAIRSL RLEDIRFPVA LVKTFQGPPH
160 170 180 190 200
GIQVERDLLN KYGRPMLGCT IKPKLGLSAK NYGRAVYECL RGGLDFTKDD
210 220 230 240 250
ENINSQPFQR WRDRFLFVAD AIHKSQAETG EIKGHYLNVT APTCEEMMKR
260 270 280 290 300
AEFAKELGMP IIMHDFLTAG FTANTTLAKW CRDNGVLLHI HRAMHAVIDR
310 320 330 340 350
QRNHGIHFRV LAKCLRLSGG DHLHSGTVVG KLEGDKASTL GFVDLMREDH
360 370 380 390 400
IEADRSRGVF FTQDWASMPG VLPVASGGIH VWHMPALVEI FGDDSVLQFG
410 420 430 440 450
GGTLGHPWGN APGATANRVA LEACVQARNE GRDLYREGGD ILREAGKWSP
460 470
ELAAALDLWK EIKFEFETMD KL
Length:472
Mass (Da):52,448
Last modified:February 15, 2005 - 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:iCDD8519AA9D493C9
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 conflicti38 – 39RF → PV in K00486 (PubMed:6307620).Curated2
Sequence conflicti353A → R in K00486 (PubMed:6307620).Curated1

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
K00486 Genomic DNA No translation available.
X03220 Genomic DNA Translation: CAA26972.1
AP008231 Genomic DNA Translation: BAD78320.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A90941, RKYCL

NCBI Reference Sequences

More...
RefSeqi
WP_011242444.1, NC_006576.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
BAD78320; BAD78320; syc0130_c

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
syc:syc0130_c

<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
K00486 Genomic DNA No translation available.
X03220 Genomic DNA Translation: CAA26972.1
AP008231 Genomic DNA Translation: BAD78320.1
PIRiA90941, RKYCL
RefSeqiWP_011242444.1, NC_006576.1

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
1RBLX-ray2.20A/B/C/D/E/F/G/H6-472[»]
1RSCX-ray2.30A/B/C/D/E/F/G/H1-472[»]
2WVWelectron microscopy9.00A/B/C/D/E/F/G/H1-472[»]
3RG6X-ray3.20A/B1-472[»]
SMRiP00880
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-6210N
IntActiP00880, 2 interactors
STRINGi269084.syc0130_c

Genome annotation databases

EnsemblBacteriaiBAD78320; BAD78320; syc0130_c
KEGGisyc:syc0130_c

Phylogenomic databases

eggNOGiCOG1850, Bacteria
OMAiIHGHPDG

Enzyme and pathway databases

BioCyciSELO269084:G1G2F-139-MONOMER
SABIO-RKiP00880

Miscellaneous databases

EvolutionaryTraceiP00880

Family and domain databases

CDDicd08212, RuBisCO_large_I, 1 hit
DisProtiDP02960
Gene3Di3.20.20.110, 1 hit
3.30.70.150, 1 hit
HAMAPiMF_01338, RuBisCO_L_type1, 1 hit
InterProiView protein in InterPro
IPR033966, RuBisCO
IPR020878, RuBisCo_large_chain_AS
IPR000685, RuBisCO_lsu_C
IPR036376, RuBisCO_lsu_C_sf
IPR017443, RuBisCO_lsu_fd_N
IPR036422, RuBisCO_lsu_N_sf
IPR020888, RuBisCO_lsuI
PANTHERiPTHR42704, PTHR42704, 1 hit
PfamiView protein in Pfam
PF00016, RuBisCO_large, 1 hit
PF02788, RuBisCO_large_N, 1 hit
SFLDiSFLDS00014, RuBisCO, 1 hit
SUPFAMiSSF51649, SSF51649, 1 hit
SSF54966, SSF54966, 1 hit
PROSITEiView protein in PROSITE
PS00157, RUBISCO_LARGE, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRBL_SYNP6
<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: P00880
<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: July 21, 1986
Last sequence update: February 15, 2005
Last modified: June 2, 2021
This is version 159 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, 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
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