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Q59460 (RBL1B_HYDMR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 61. 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 2
Short name=RuBisCO large subunit 2
EC=4.1.1.39
Gene names
Name:cbbL2
Synonyms:cbbL-2, cbbLS-2
OrganismHydrogenovibrio marinus
Taxonomic identifier28885 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Piscirickettsiaceae › Hydrogenovibrio

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
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_01338

Catalytic activity

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

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

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01338

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains Probable.

Induction

Both mRNA and protein accumulate at 0.15% and 0.03% CO2, but not at 15% or 2% CO2. HAMAP MF_01338

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. HAMAP MF_01338

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 471471Ribulose bisphosphate carboxylase large chain 2 HAMAP MF_01338
PRO_0000062625

Sites

Active site1681Proton acceptor By similarity
Active site2871Proton acceptor By similarity
Metal binding1941Magnesium; via carbamate group By similarity
Metal binding1961Magnesium By similarity
Metal binding1971Magnesium By similarity
Binding site1161Substrate; in homodimeric partner By similarity
Binding site1661Substrate By similarity
Binding site1701Substrate By similarity
Binding site2881Substrate By similarity
Binding site3201Substrate By similarity
Binding site3721Substrate By similarity
Site3271Transition state stabilizer By similarity

Amino acid modifications

Modified residue1941N6-carboxylysine By similarity

Experimental info

Sequence conflict731F → Y in BAD15312. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q59460 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: BAD462E46451AD60

FASTA47152,005
        10         20         30         40         50         60 
MASKTFDAGV QDYQLTYWTP DYTPLDTDLL ACFKVVPQEG VPREEAAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDLLTDM EFFKGRAYRI EDVPGDKNAF YAFIAYPLDL FEEGSVVNVL TSLVGNVFGF 

       130        140        150        160        170        180 
KAVRSLRLED LRFPIAFIKT CGGPPSGIQV ERDKLNKYGR PMLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DLTKDDENIN SQPFQRWRDR FEFVAEAVDK ATAETGERKG HYLNVTAGTV 

       250        260        270        280        290        300 
EEMMKRAEFA KELGQPIIMH DFLTAGFTAN TTLANWCREN GMLLHIHRAM HAVIDRNPLH 

       310        320        330        340        350        360 
GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRASTLGFVD QLRESFVPED RSRGVFFDQD 

       370        380        390        400        410        420 
WGSMPGVMAV ASGGIHVWHM PALVNIFGDD SVLQFGGGTQ GHPGGNAAGA AANRVALEAC 

       430        440        450        460        470 
VKARNEGRDL EREGGDILRE AARTSKELAV ALETWKEIKF EFDTVDKLDV Q

« Hide

References

[1]"Phylogenetic position of an obligately chemoautotrophic, marine hydrogen-oxidizing bacterium, Hydrogenovibrio marinus, on the basis of 16S rRNA gene sequences and two form I RuBisCO gene sequences."
Nishihara H., Yaguchi T., Chung S.-Y., Suzuki K., Yanagi M., Yamasato K., Kodama T., Igarashi Y.
Arch. Microbiol. 169:364-368(1998) [PubMed: 9531639] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 11271 / JCM 7688 / MH-110.
[2]"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.
[3]"Different properties of gene products of three sets ribulose 1,5-bisphosphate carboxylase/oxygenase from a marine obligately autotrophic hydrogen-oxidizing bacterium, Hydrogenovibrio marinus strain MH-110."
Hayashi N.R., Oguni A., Yaguchi T., Chung S.-Y., Nishihara H., Kodama T., Igarashi Y.
J. Ferment. Bioeng. 85:150-155(1998)
Cited for: CHARACTERIZATION IN E.COLI.
Strain: DSM 11271 / JCM 7688 / MH-110.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D43622 Genomic DNA. Translation: BAA07731.1.
AB122070 Genomic DNA. Translation: BAD15312.1.

3D structure databases

ProteinModelPortalQ59460.
SMRQ59460. Positions 16-460.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_01338. RuBisCO_L_type1.
[Tree]
InterProIPR020888. RuBisCO_lsu.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL1B_HYDMR
AccessionPrimary (citable) accession number: Q59460
Secondary accession number(s): Q75W40
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 28, 2011
This is version 61 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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