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Q59462 (RBL2_HYDMR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 63. 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
Synonyms:cbbL-3
OrganismHydrogenovibrio marinus
Taxonomic identifier28885 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Piscirickettsiaceae › Hydrogenovibrio

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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. 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. Ref.2

Induction

mRNA expression is constant at all CO2 concentrations tested, however more protein accumulates at 15% and 2% CO2 than at 0.15% and 0.03% CO2. 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

Initiator methionine11Removed Ref.2
Chain2 – 463462Ribulose bisphosphate carboxylase HAMAP MF_01339
PRO_0000062662

Sites

Active site1711Proton acceptor By similarity
Active site2941Proton acceptor By similarity
Metal binding1961Magnesium; via carbamate group By similarity
Metal binding1981Magnesium By similarity
Metal binding1991Magnesium By similarity
Binding site1161Substrate; in homodimeric partner By similarity
Binding site1731Substrate By similarity
Binding site2951Substrate By similarity
Binding site3281Substrate By similarity
Binding site3751Substrate By similarity
Site3361Transition state stabilizer By similarity

Amino acid modifications

Modified residue1961N6-carboxylysine By similarity

Experimental info

Sequence conflict3791D → N in BAD15326. Ref.3
Sequence conflict4221A → D in BAD15326. Ref.3
Sequence conflict4291E → D in BAD15326. Ref.3
Sequence conflict433 – 4353APR → YAKEHP in BAD15326. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q59462 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A7F8E289FF92E996

FASTA46350,729
        10         20         30         40         50         60 
MDQSNRYADL TLTEEKLVAD GNHLLVAYRL KPAAGYGFLE VAAHVAAESS TGTNVEVSTT 

        70         80         90        100        110        120 
DDFTRGVDAL VYEIDEAAFG DKGGLMKIAY PVDLFDPNLI DGHYNVSHMW SLILGNNQGM 

       130        140        150        160        170        180 
GDHEGLRMLD FLVPEKMVKR FDGPATDISD LWKVLGRPEV DGGYIAGTII KPKLGLRPEP 

       190        200        210        220        230        240 
FAKACYDFWL GGDFIKNDEP QANQNFCPME VVIPKVAEAM DRAQQATGQA KLFSANVTAD 

       250        260        270        280        290        300 
FHEEMIKRGE YVLGEFAKYG NEKHVAFLVD GFVTGPAGVT TSRRAFPDTY LHFHRAGHGA 

       310        320        330        340        350        360 
VTSYKSPMGM DPLCYMKLAR LMGASGIHTG TMGYGKMEGH NDERVLAYML ERDECQGPYF 

       370        380        390        400        410        420 
YQKWYGMKPT TPIISGGMDA LRLPGFFENL GHGNVINTCG GGSFGHIDSP AAGGISLGQA 

       430        440        450        460 
YACWKTGAEP IEAPREFARA FESFPGDADK IFPGWREKLG VHK

« Hide

References

[1]"Cloning and sequence of the L2 form of RubisCO from a marine obligately autotrophic hydrogen-oxidizing bacterium, Hydrogenovibrio marinus strain MH-110."
Yaguchi T., Chung S.Y., Igarashi Y., Kodama T.
Biosci. Biotechnol. Biochem. 58:1733-1737(1994) [PubMed: 7765489] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON ORGANIZATION.
Strain: DSM 11271 / JCM 7688 / MH-110.
[2]"Purification of form L2 RubisCO from a marine obligately autotrophic hydrogen-oxidizing bacterium, Hydrogenovibrio marinus strain MH-110."
Chung S.Y., Yaguchi T., Nishihara H., Igarashi Y., Kodama T.
FEMS Microbiol. Lett. 109:49-53(1993) [PubMed: 8319883] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-31, SUBUNIT.
Strain: DSM 11271 / JCM 7688 / MH-110.
[3]"CO2-responsive expression and gene organization of three ribulose-1,5-bisphosphate carboxylase/oxygenase enzymes and carboxysomes in Hydrogenovibrio marinus strain MH-110."
Yoshizawa Y., Toyoda K., Arai H., Ishii M., Igarashi Y.
J. Bacteriol. 186:5685-5691(2004) [PubMed: 15317772] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CONTROL OF EXPRESSION BY CO(2) IN H.MARINUS.
Strain: DSM 11271 / JCM 7688 / MH-110.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D28135 Genomic DNA. Translation: BAA05677.1.
AB122071 Genomic DNA. Translation: BAD15326.1.
PIRJC2307.

3D structure databases

ProteinModelPortalQ59462.
SMRQ59462. Positions 2-461.
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_HYDMR
AccessionPrimary (citable) accession number: Q59462
Secondary accession number(s): Q75W26
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: June 28, 2011
This is version 63 of the entry and version 3 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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