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Q31IK3 (RBL2_THICR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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
Short name=RuBisCO
EC=4.1.1.39
Gene names
Name:cbbM
Ordered Locus Names:Tcr_0424
OrganismThiomicrospira crunogena (strain XCL-2) [Complete proteome] [HAMAP]
Taxonomic identifier317025 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Piscirickettsiaceae › Thiomicrospira

Protein attributes

Sequence length459 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 MF_01339

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP MF_01339

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP MF_01339

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01339

Subunit structure

Homodimer By similarity. HAMAP MF_01339

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits By similarity. HAMAP MF_01339

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Ribulose bisphosphate carboxylase HAMAP MF_01339
PRO_0000251414

Sites

Active site1661Proton acceptor By similarity
Active site2871Proton acceptor By similarity
Metal binding1911Magnesium; via carbamate group By similarity
Metal binding1931Magnesium By similarity
Metal binding1941Magnesium By similarity
Binding site1111Substrate; in homodimeric partner By similarity
Binding site1681Substrate By similarity
Binding site2881Substrate By similarity
Binding site3211Substrate By similarity
Binding site3681Substrate By similarity
Site3291Transition state stabilizer By similarity

Amino acid modifications

Modified residue1911N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q31IK3 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: CA55D3D2306EA579

FASTA45950,281
        10         20         30         40         50         60 
MDQSNRYADL SLKEEDLIAG QNHILVAYTM EPAAGYGYLE VAAHIAAESS TGTNVEVCTT 

        70         80         90        100        110        120 
DDFTKGVDAI VYDIDEANGI MKVAYPFDLF DRNGLDGKTM IVSFLTLAIG NNQGMGDVKN 

       130        140        150        160        170        180 
LQMFDFWVPE TKLHLFDGPA VDITNMWKML GRDKDNGGYI AGTIIKPKLG LRPEPFADAA 

       190        200        210        220        230        240 
YQFWLGGDFI KNDEPQGNQT FCPMKKVIPL VADAMKRAQD ETGETKLFSA NITADDHHEM 

       250        260        270        280        290        300 
CYRADYILET FGADAPQVAF LVDGYVGGPG MITTARRNYP SQYLHYHRAG HGAITSPSAK 

       310        320        330        340        350        360 
RGYTAFVLAK ISRLQGASGI HVGTMGYGKM EGDASDKNIA YMIERDECQG PAFYQKWNGM 

       370        380        390        400        410        420 
KPTTPIISGG MNALRLPGFF ENLGHGNVIN TSGGGSYGHI DSPAAGATSL RQSYECWKSG 

       430        440        450 
ADPIEFAKDH KEFARAFESF PADADKIYPG WREKLGVHK

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000109 Genomic DNA. Translation: ABB41020.1.
RefSeqYP_390694.1. NC_007520.2.

3D structure databases

ProteinModelPortalQ31IK3.
SMRQ31IK3. Positions 2-457.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ31IK3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3761243.
GenomeReviewsGene locus Tcr_0424 in contig CP000109_GR.
KEGGtcx:Tcr_0424.
NMPDRfig|317025.3.peg.600.
PATRIC23972740. VBIThiCru83387_0436.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
HOGENOMHBG405441.
OMANVEVCTT.
ProtClustDBPRK13475.

Enzyme and pathway databases

BioCycTCRU317025:TCR_0424-MONOMER.

Family and domain databases

HAMAPMF_01339. RuBisCO_L_type2.
[Tree]
InterProIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
Gene3DG3DSA:3.20.20.110. RuBisCO_large. 1 hit.
G3DSA:3.30.70.150. RuBisCO_large. 1 hit.
KOK01601.
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL2_THICR
AccessionPrimary (citable) accession number: Q31IK3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: December 6, 2005
Last modified: January 25, 2012
This is version 45 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

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