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O98949 (O98949_9RHOD) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 73. 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:rbcL HAMAP-Rule MF_01338
Encoded onPlastid; Chloroplast EMBL BAA75796.1
OrganismGaldieria partita EMBL BAA75796.1
Taxonomic identifier83374 [NCBI]
Taxonomic lineageEukaryotaRhodophytaBangiophyceaeCyanidialesCyanidiaceaeGaldieria

Protein attributes

Sequence length493 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 in the photorespiration process. 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

Subcellular location

Plastidchloroplast By similarity HAMAP-Rule MF_01338 RuleBase RU000303.

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

Regions

Region411 – 4122Sulfate 2 binding

Sites

Active site1841Proton acceptor By similarity HAMAP-Rule MF_01338
Active site3021Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2101Magnesium PDB 1BWV
Metal binding2101Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2121Magnesium PDB 1BWV
Metal binding2121Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2131Magnesium PDB 1BWV
Metal binding2131Magnesium By similarity HAMAP-Rule MF_01338
Binding site741Sulfate 1
Binding site1321Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1821Substrate By similarity HAMAP-Rule MF_01338
Binding site1841Sulfate 2
Binding site1861Substrate By similarity HAMAP-Rule MF_01338
Binding site3031Substrate By similarity HAMAP-Rule MF_01338
Binding site3351Substrate By similarity HAMAP-Rule MF_01338
Binding site3421Sulfate 2
Binding site3871Substrate By similarity HAMAP-Rule MF_01338
Binding site3891Sulfate 2; via amide nitrogen
Site3421Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2101N6-carboxylysine PDB 1BWV
Modified residue2101N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
O98949 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: FF86E3FF8C68C937

FASTA49354,994
        10         20         30         40         50         60 
MSQSIEEKSV QERTRIKNSR YESGVIPYAK MGYWNPDYQV KDTDVLALFR VTPQPGVDPI 

        70         80         90        100        110        120 
EAAAAVAGES STATWTVVWT DLLTAADLYR AKAYKVDQVP NNPEQYFAYI AYELDLFEEG 

       130        140        150        160        170        180 
SIANLTASII GNVFGFKAVK ALRLEDMRLP LAYLKTFQGP ATGVILERER LDKFGRPLLG 

       190        200        210        220        230        240 
CTTKPKLGLS GKNYGRVVYE ALKGGLDFVK DDENINSQPF MRWRERYLFT MEAVNKASAA 

       250        260        270        280        290        300 
TGEVKGHYLN VTAATMEEMY ARANFAKELG SVIIMIDLVI GYTAIQTMAK WARDNDMILH 

       310        320        330        340        350        360 
LHRAGNSTYS RQKNHGMNFR VICKWMRMAG VDHIHAGTVV GKLEGDPIIT RGFYKTLLLP 

       370        380        390        400        410        420 
KLERNLQEGL FFDMEWASLR KVMPVASGGI HAGQMHQLIH YLGEDVVLQF GGGTIGHPDG 

       430        440        450        460        470        480 
IQAGATANRV ALEAMILARN ENRDYLTEGP EILREAAKTC GALRTALDLW KDITFNYTST 

       490 
DTSDFVETPT ANI 

« Hide

References

[1]"Structure and function study of ribulose-1,5-bisphosphate carboxylase/oxygenase of the red algae, Galdieria partita Tokara."
Tomizawa K.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Crystal structure of carboxylase reaction-oriented ribulose 1, 5-bisphosphate carboxylase/oxygenase from a thermophilic red alga, Galdieria partita."
Sugawara H., Yamamoto H., Shibata N., Inoue T., Okada S., Miyake C., Yokota A., Kai Y.
J. Biol. Chem. 274:15655-15661(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, CARBOXYLATION AT LYS-210.
[3]"X-ray structure of Galdieria Rubisco complexed with one sulfate ion per active site."
Okano Y., Mizohata E., Xie Y., Matsumura H., Sugawara H., Inoue T., Yokota A., Kai Y.
FEBS Lett. 527:33-36(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH SULFATE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB018008 Genomic DNA. Translation: BAA75796.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BWVX-ray2.40A/C/E/G1-493[»]
1IWAX-ray2.60A/C/E/G/I/K/M/O1-493[»]
ProteinModelPortalO98949.
SMRO98949. Positions 14-486.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Other

EvolutionaryTraceO98949.

Entry information

Entry nameO98949_9RHOD
AccessionPrimary (citable) accession number: O98949
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)