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Q7V6F8 (RBL_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain

Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:cbbL
Synonyms:rbcL
Ordered Locus Names:PMT_1205
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length470 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 in the photorespiration process. 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 – 470470Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000062638

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
Q7V6F8 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 341368654FDD59C3

FASTA47052,573
        10         20         30         40         50         60 
MSKKYDAGVK EYRDTYWTPD YVPLDTDLLA CFKCTGQEGV PREEVAAAVA AESSTGTWST 

        70         80         90        100        110        120 
VWSELLTDLE FYKGRCYRIE DVPGDKESFY AFIAYPLDLF EEGSITNVLT SLVGNVFGFK 

       130        140        150        160        170        180 
ALRHLRLEDI RFPMAFIKTC GGPPNGIVVE RDRLNKYGRP LLGCTIKPKL GLSGKNYGRV 

       190        200        210        220        230        240 
VYECLRGGLD LTKDDENINS QPFQRWRERF EFVAEAVKLA QQETGEVKGH YLNCTATTPE 

       250        260        270        280        290        300 
EMYERAEFAK ELDMPIIMHD YITGGFTANT GLANWCRKNG MLLHIHRAMH AVIDRHPKHG 

       310        320        330        340        350        360 
IHFRVLAKCL RLSGGDQLHT GTVVGKLEGD RQTTLGYIDN LRESFVPEDR SRGNFFDQDW 

       370        380        390        400        410        420 
GSMPGVFAVA SGGIHVWHMP ALLAIFGDDS CLQFGGGTHG HPWGSAAGAA ANRVALEACV 

       430        440        450        460        470 
KARNAGREIE KESRDILMEA AKHSPELAIA LETWKEIKFE FDTVDKLDVQ 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE21380.1.
RefSeqNP_895035.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7V6F8.
SMRQ7V6F8. Positions 15-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING74547.PMT1205.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE21380; CAE21380; PMT_1205.
GeneID1728877.
KEGGpmt:PMT1205.
PATRIC23010821. VBIProMar135351_1559.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1850.
KOK01601.
OMAFTQDWAS.
OrthoDBEOG6ZKXMS.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020888. 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.
ProtoNetSearch...

Entry information

Entry nameRBL_PROMM
AccessionPrimary (citable) accession number: Q7V6F8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 65 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