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Q31IK0 (RBL1A_THICR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain 1

Short name=RuBisCO large subunit 1
EC=4.1.1.39
Gene names
Name:cbbL1
Ordered Locus Names:Tcr_0427
OrganismThiomicrospira crunogena (strain XCL-2) [Complete proteome] [HAMAP]
Taxonomic identifier317025 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesPiscirickettsiaceaeThiomicrospira

Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. Both reactions occur simultaneously and in competition at the same active site By similarity. HAMAP-Rule MF_01338

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01338

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01338

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains By similarity.

Miscellaneous

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" By similarity.

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 472472Ribulose bisphosphate carboxylase large chain 1 HAMAP-Rule MF_01338
PRO_0000251466

Sites

Active site1671Proton acceptor By similarity
Active site2861Proton acceptor By similarity
Metal binding1931Magnesium; via carbamate group By similarity
Metal binding1951Magnesium By similarity
Metal binding1961Magnesium By similarity
Binding site1151Substrate; in homodimeric partner By similarity
Binding site1651Substrate By similarity
Binding site1691Substrate By similarity
Binding site2871Substrate By similarity
Binding site3191Substrate By similarity
Binding site3711Substrate By similarity
Site3261Transition state stabilizer By similarity

Amino acid modifications

Modified residue1931N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q31IK0 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 5E70D6B51D425EC2

FASTA47252,568
        10         20         30         40         50         60 
MAKTYNAGVK EYRETYWMPE YEPKDSDFLA CFKVIPQDGV PREEIAAAVA AESSTGTWTT 

        70         80         90        100        110        120 
VWTDLLTDLD YYKGRAYKIE DVPGDDAAFY AFIAYPIDLF EEGSVVSVMT SLVGNVFGFK 

       130        140        150        160        170        180 
ALRACRLEDI RFPLAYVMTC GGPPHGIQVE RDKMDKYGRP MLGCTIKPKL GLSAKNYGRA 

       190        200        210        220        230        240 
VYECLRGGLD FTKDDENVTS QPFMRWRDRF LFCQDAIEKA QAETGERKGH YLNCTAGTPE 

       250        260        270        280        290        300 
EMYERAEFAK EIGTPIIMHD YLTGGFTANT GLANYCRKNG LLLHIHRAMH GVIDRNPHHG 

       310        320        330        340        350        360 
IHFRVLTKAL RLSGGDHLHS GTVVGKLEGD REATLGWIDL MRDSFIPEDR SRGIMFDQDF 

       370        380        390        400        410        420 
GAMPGVMPVA SGGIHVWHMP ALVSIFGDDS VLQFGGGTLG HPWGNAAGAA ANRVALEACV 

       430        440        450        460        470 
QARNEGKEVE KEGKEILTNA AKHSPELKIA METWKEIKFE FDTVDKLDVK HK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000109 Genomic DNA. Translation: ABB41023.1.
RefSeqYP_390697.1. NC_007520.2.

3D structure databases

ProteinModelPortalQ31IK0.
SMRQ31IK0. Positions 15-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING317025.Tcr_0427.

Proteomic databases

PRIDEQ31IK0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB41023; ABB41023; Tcr_0427.
GeneID3761246.
KEGGtcx:Tcr_0427.
PATRIC23972746. VBIThiCru83387_0439.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHOG000230831.
KOK01601.
OMADTDILAC.
OrthoDBEOG6ZKXMS.
ProtClustDBPRK04208.

Enzyme and pathway databases

BioCycTCRU317025:GHE8-433-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL1A_THICR
AccessionPrimary (citable) accession number: Q31IK0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: December 6, 2005
Last modified: February 19, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families