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Q9ZHZ1 (RBL1_THIK1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. 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
Ordered Locus Names:Tint_0115
OrganismThiomonas intermedia (strain K12) (Thiobacillus intermedius) [Complete proteome] [HAMAP]
Taxonomic identifier75379 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesThiomonas

Protein attributes

Sequence length473 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-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 – 473473Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000062659

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

Sequences

Sequence LengthMass (Da)Tools
Q9ZHZ1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 46EAF8F4C060ADF4

FASTA47352,787
        10         20         30         40         50         60 
MAVKTYQAGV KEYRQTYWMP EYTPLDTDLL ACFKITPQAG VDREEAAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDLLTDM DYYKGRAYRI EDVPGDDTCF YAFIAYPIDL FEEGSVVNVF TSLVGNVFGF 

       130        140        150        160        170        180 
KAIRALRLED IRFPIAYVKT CNGPPNGIQV ERDVINKYGR PLLGCTIKPK LGLSGKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DFTKDDENIN SQPFMRWKQR FDFVQEATLK AEQETGERKG HYLNVTAPTP 

       250        260        270        280        290        300 
DEMFKRAEYA KEIGAPIIMH DYITGGFCAN TGLAQWCRDN GMLLHIHRAM HAVLDRNPHH 

       310        320        330        340        350        360 
GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESYVPED RSRGIFFDQD 

       370        380        390        400        410        420 
WGSMPGAFAV ASGGIHVWHM PALVTIFGDD SVLQFGGGTL GHPWGNAAGA AANRVALEAC 

       430        440        450        460        470 
VQARNEGRQV EKEGREILTA AAQHSPELKI AMETWKEIKF EFDTVDKLDV TNK 

« Hide

References

« Hide 'large scale' references
[1]"Organization of carboxysome genes in the thiobacilli."
Cannon G.C., Baker S.H., Soyer F., Johnson D.R., Bradburne C.E., Mehlman J.L., Davies P.S., Jiang Q.L., Heinhorst S., Shively J.M.
Curr. Microbiol. 46:115-119(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of Thiomonas intermedia K12."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C., Heinhorst S., Woyke T.
Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF046933 Genomic DNA. Translation: AAD02445.1.
CP002021 Genomic DNA. Translation: ADG29528.1.
RefSeqYP_003641858.1. NC_014153.1.

3D structure databases

ProteinModelPortalQ9ZHZ1.
SMRQ9ZHZ1. Positions 16-460.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADG29528; ADG29528; Tint_0115.
GeneID9150845.
KEGGtin:Tint_0115.
PATRIC38290688. VBIThiInt85915_0120.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.

Enzyme and pathway databases

BioCycTINT75379:GH6C-115-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. 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.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL1_THIK1
AccessionPrimary (citable) accession number: Q9ZHZ1
Secondary accession number(s): D5X330
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 71 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