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F9ZLP0 (F9ZLP0_ACICS) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 15. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338

Short name=RuBisCO large subunit HAMAP-Rule MF_01338
EC=4.1.1.39 HAMAP-Rule MF_01338
Gene names
Name:cbbL HAMAP-Rule MF_01338
Ordered Locus Names:Atc_0926 EMBL AEK57575.1
OrganismAcidithiobacillus caldus (strain SM-1) [Complete proteome] [HAMAP] EMBL AEK57575.1
Taxonomic identifier990288 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus

Protein attributes

Sequence length472 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. HAMAP-Rule 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-Rule MF_01338

Sequence similarities

Belongs to the RuBisCO large chain family. Type I subfamily. HAMAP-Rule MF_01338

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1671Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2861Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1931Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding1951Magnesium By similarity HAMAP-Rule MF_01338
Metal binding1961Magnesium By similarity HAMAP-Rule MF_01338
Binding site1151Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1651Substrate By similarity HAMAP-Rule MF_01338
Binding site1691Substrate By similarity HAMAP-Rule MF_01338
Binding site2871Substrate By similarity HAMAP-Rule MF_01338
Binding site3191Substrate By similarity HAMAP-Rule MF_01338
Binding site3711Substrate By similarity HAMAP-Rule MF_01338
Site3261Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1931N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
F9ZLP0 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: 6B35F9C6839946EE

FASTA47252,672
        10         20         30         40         50         60 
MAGKYEAGVK EYRHTYWAPD YVPLDSDILA CFKIVPQPGV DREEAAAAVA AESSTGTWTT 

        70         80         90        100        110        120 
VWTDLLTDMD YYKGRAYRIE DVPGDDTAFY AFIAYPIDLF EEGSVVNVFT SLVGNVFGFK 

       130        140        150        160        170        180 
AVRSLRLEDV RFPLHYVMTC NGPAHGIQVE RDKMDKYGRP LLGCTIKPKL GLSAKNYGRA 

       190        200        210        220        230        240 
VYEALRGGLD FTKDDENVNS QPFMRWRDRF LFVADAIRNA EAQTGERKGH YLNVTAPSPE 

       250        260        270        280        290        300 
EMYERAEFAK ELGMPIIMHD FLTGGFCANT GLARWCRKNG VLLHIHRAMH AVIDRNPHHG 

       310        320        330        340        350        360 
IHFRVLTKAL RLSGGDHLHT GTVVGKLEGD RASTLGWIDL LRESYIPEDR SRGIFFDQDW 

       370        380        390        400        410        420 
GSMPGAFAVA SGGIHVWHMP ALVNIFGDDS VLQFGGGTLG HPWGNAAGAA ANRVALEACV 

       430        440        450        460        470 
EARNRGVEIE KEGKEVLMNA ARHSPELKIA LETWKEIKFE FDTVDKLDVQ NR 

« Hide

References

[1]"Unraveling the Acidithiobacillus caldus complete genome and its central metabolisms for carbon assimilation."
You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B., Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.
J. Genet. Genomics 38:243-252(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SM-1 EMBL AEK57575.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002573 Genomic DNA. Translation: AEK57575.1.
RefSeqYP_004748275.1. NC_015850.1.

3D structure databases

ProteinModelPortalF9ZLP0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEK57575; AEK57575; Atc_0926.
GeneID10988712.
KEGGacu:Atc_0926.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycACAL990288:GJBS-941-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 nameF9ZLP0_ACICS
AccessionPrimary (citable) accession number: F9ZLP0
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: February 19, 2014
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)