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Reviewed, UniProtKB/Swiss-Prot Q59458 (RBL1A_HYDMR)

Last modified January 19, 2010. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Ribulose bisphosphate carboxylase large chain 1
      Short name=RuBisCO large subunit 1
    EC=4.1.1.39
Gene names
Name: cbbL1
Synonyms: cbbL-1, cbbLS-1
OrganismHydrogenovibrio marinus
Taxonomic identifier28885 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Piscirickettsiaceae › Hydrogenovibrio

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Protein attributes

Sequence length472 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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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. HAMAP MF_01338

Induction

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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 472472Ribulose bisphosphate carboxylase large chain 1 HAMAP MF_01338
PRO_0000062624

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

Experimental info

Sequence conflict2981L → M in BAD15307. Ref.2
Sequence conflict332 – 3343GSD → EAT in BAD15307. Ref.2
Sequence conflict3991I → L in BAD15307. Ref.2
Sequence conflict4071V → A in BAD15307. Ref.2
Sequence conflict411 – 4133VNL → ANR in BAD15307. Ref.2
Sequence conflict440 – 4412DG → AA in BAD15307. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q59458-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 71FCAE86F7CF2530

FASTA47252,488
        10         20         30         40         50         60 
MAKTYNAGVK EYRETYWMPE YEPKDSDFLA CFKVVPQPGV PREEIAAAVA AESSTGTWTT 

        70         80         90        100        110        120 
VWTDLLTDLD YYKGRAYRIE DVPGDDSAFY AFIAYPIDLF EEGSIVSVMT SLVGNVFGFK 

       130        140        150        160        170        180 
ALRSIRLEDI RFPLAYVMTC GGPPHGIQVE RDKMDKYGRP MLGCTIKPKL GLSAKNYGRA 

       190        200        210        220        230        240 
VYECLRGGLD FTKDDENVTS QPFMRWRDRF LFCQDAIEKA QDETGERTGH YLNATAGTPE 

       250        260        270        280        290        300 
EMYERAEFAK EIGSPIVMHD FLTGGLTANT GLANYCRKNG LLLHIHRAMH GVIDRNPLHG 

       310        320        330        340        350        360 
IHFRVLSKVL RLSGGDHLHS GTVVGKLEGD RGSDLGWIDI MRDSFIAEDR SRGIMFDQDF 

       370        380        390        400        410        420 
GEMPGVIPVA SGGIHVWHMP ALVAIFGDDS VLQFGGGTIG HPWGNAVGAA VNLVALEACV 

       430        440        450        460        470 
QARNEGQEIE KNGKEILTND GKHSPELKIA METWKEIKFE FDTVDKLDLS HK

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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], EXPRESSION IN E.COLI.
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.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D43621 Genomic DNA. Translation: BAA07729.1.
AB122069 Genomic DNA. Translation: BAD15307.1.

3D structure databases

SMRQ59458. Positions 15-459.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.1.1.39. 2848.

Family and domain databases

HAMAPMF_01338. RuBisCO_L_type1.
[Tree]
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. 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]
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameRBL1A_HYDMR
AccessionPrimary (citable) accession number: Q59458
Secondary accession number(s): Q75W45
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: January 19, 2010
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents