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Q8RTI2 (RBL2_MAGMG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 44. 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
OrganismMagnetospirillum magnetotacticum (Aquaspirillum magnetotacticum)
Taxonomic identifier188 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Magnetospirillum

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_0000062663

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
Q8RTI2 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 7BAF901EE932774F

FASTA45950,217
        10         20         30         40         50         60 
MDQSKRYVNL ALSEADLIKG GRHVLCAYRM RPRPGHGYVE TAAHFAAESS TGTNVEVCTT 

        70         80         90        100        110        120 
DDFTRGVDAL VYEVDEAEGL MKIAYPVDLF DRNIIDGKAM IASFLTLTVG NNQGMSDVEN 

       130        140        150        160        170        180 
AKMEDFYVPP EFLKLFDGPA CNISHMWKVL GRPEVNGGMV VGTIIKPKLG LRPKPFADAC 

       190        200        210        220        230        240 
HQFWLGGDFI KNDEPQGNQV FAPLKETMRL VADAMRRAQD ETGVPKLLSA NITADDPAEM 

       250        260        270        280        290        300 
IARGNFILET FGENASHVAF LVDGFVAGPT AVTTCRRNFP DTFLHYHRAG HGAITSRQSK 

       310        320        330        340        350        360 
RGYTVLVHMK MARLLGASGI HTGTMGYGKM EGAPDEKMVA YMLERQIAEG PYYRQDWGGM 

       370        380        390        400        410        420 
ASCTPIISGG MSALRLPGFF DNLGHSNVIQ TSGGGAFGHK DGAIAGALSL RQAHEAWLKK 

       430        440        450 
IDLVDYAQTH AELRGAFESF ASDADRLYPG WRDRLRIAA

« Hide

References

[1]"Chemolithoautotrophy in the marine, magnetotactic bacterial strains MV-1 and MV-2."
Bazylinski D.A., Dean A.J., Williams T.J., Long L.K., Middleton S.L., Dubbels B.L.
Arch. Microbiol. 182:373-387(2004) [PubMed: 15338111] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MS-1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF442517 Genomic DNA. Translation: AAL76920.1.

3D structure databases

ProteinModelPortalQ8RTI2.
SMRQ8RTI2. Positions 2-457.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
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_MAGMG
AccessionPrimary (citable) accession number: Q8RTI2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: June 1, 2002
Last modified: June 28, 2011
This is version 44 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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