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F9ZF99 (F9ZF99_9PROT) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 17. 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
ORF Names:NAL212_0872 EMBL ADZ25799.1
OrganismNitrosomonas sp. AL212 [Complete proteome] EMBL ADZ25799.1
Taxonomic identifier153948 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

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. 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 site1681Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2871Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding1941Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding1961Magnesium By similarity HAMAP-Rule MF_01338
Metal binding1971Magnesium By similarity HAMAP-Rule MF_01338
Binding site1161Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1661Substrate By similarity HAMAP-Rule MF_01338
Binding site1701Substrate By similarity HAMAP-Rule MF_01338
Binding site2881Substrate By similarity HAMAP-Rule MF_01338
Binding site3201Substrate By similarity HAMAP-Rule MF_01338
Binding site3721Substrate By similarity HAMAP-Rule MF_01338
Site3271Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue1941N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
F9ZF99 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: B60FE80DB1D12792

FASTA47352,537
        10         20         30         40         50         60 
MAVKIYNAGV KEYRQTYWTP DYTPLDTDIL ACFKITPQPG VPREEVAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDLLTDL DYYKGRAYKI EDVPGDDTCF YAFVAYPIDL FEEGSVVNVL TSLVGNVFGF 

       130        140        150        160        170        180 
KALRALRLED VRFPIAYVKT CGGPPAGIQV ERDRFNKYGR ALLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DLTKDDENIN SQPFMRWRDR FQFVVEACQK AERETGERKG HYLNVTAPTP 

       250        260        270        280        290        300 
EEMYKRAEFA KELGAPIIMH DYLTGGLTAN TGLANWCRNN GMLLHIHRAM HAVLDRNPHH 

       310        320        330        340        350        360 
GIHFRVLTKV LRLSGGDHLH SGTVVGKLEG DRAATLGWID TMRDKFIKED RSRGLFFDQD 

       370        380        390        400        410        420 
WGSMPGVFPV ASGGIHVWHM PALVAIFGDD ACLQFGGGTL GHPWGNAAGA AANRVALEAC 

       430        440        450        460        470 
VEARNQGVEI EKEGKAILTK AAKSSPELKI AMETWKEIKF EFDTVDKLDI AHK 

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References

[1]"Complete sequence of chromosome of Nitrosomonas sp. AL212."
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Suwa Y. expand/collapse author list , Klotz M.G., Bollmann A., Stein L.Y., Laanbroek H.J., Arp D.J., Norton J.M., Woyke T.
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: AL212 EMBL ADZ25799.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002552 Genomic DNA. Translation: ADZ25799.1.
RefSeqYP_004293961.1. NC_015222.1.

3D structure databases

ProteinModelPortalF9ZF99.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADZ25799; ADZ25799; NAL212_0872.
GeneID10297382.
KEGGnit:NAL212_0872.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycNSP153948:GHZ8-718-MONOMER.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020888. 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.
ProtoNetSearch...

Entry information

Entry nameF9ZF99_9PROT
AccessionPrimary (citable) accession number: F9ZF99
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: June 11, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)