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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Galdieria partita
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotation
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei132 – 1321Substrate; in homodimeric partnerUniRule annotation
Binding sitei182 – 1821SubstrateUniRule annotation
Active sitei184 – 1841Proton acceptorUniRule annotation
Binding sitei186 – 1861SubstrateUniRule annotation
Metal bindingi210 – 2101MagnesiumCombined sources
Metal bindingi210 – 2101Magnesium; via carbamate groupUniRule annotation
Metal bindingi212 – 2121MagnesiumUniRule annotationCombined sources
Metal bindingi213 – 2131MagnesiumUniRule annotationCombined sources
Active sitei302 – 3021Proton acceptorUniRule annotation
Binding sitei303 – 3031SubstrateUniRule annotation
Binding sitei335 – 3351SubstrateUniRule annotation
Sitei342 – 3421Transition state stabilizerUniRule annotation
Binding sitei387 – 3871SubstrateUniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotation, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation, PhotorespirationUniRule annotation, PhotosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotationCombined sources, Metal-bindingUniRule annotationCombined sources

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunitUniRule annotation
Gene namesi
Name:rbcLUniRule annotation
Encoded oniPlastid; ChloroplastImported
OrganismiGaldieria partitaImported
Taxonomic identifieri83374 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaBangiophyceaeCyanidialesCyanidiaceaeGaldieria

Subcellular locationi

  1. Plastidchloroplast UniRule annotation

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

ChloroplastUniRule annotationImported, Plastid

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei210 – 2101N6-carboxylysineUniRule annotationCombined sources

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BWVX-ray2.40A/C/E/G1-493[»]
1IWAX-ray2.60A/C/E/G/I/K/M/O1-493[»]
ProteinModelPortaliO98949.
SMRiO98949. Positions 14-486.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO98949.

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO large chain family. Type I subfamily.UniRule annotation

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O98949-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQSIEEKSV QERTRIKNSR YESGVIPYAK MGYWNPDYQV KDTDVLALFR
60 70 80 90 100
VTPQPGVDPI EAAAAVAGES STATWTVVWT DLLTAADLYR AKAYKVDQVP
110 120 130 140 150
NNPEQYFAYI AYELDLFEEG SIANLTASII GNVFGFKAVK ALRLEDMRLP
160 170 180 190 200
LAYLKTFQGP ATGVILERER LDKFGRPLLG CTTKPKLGLS GKNYGRVVYE
210 220 230 240 250
ALKGGLDFVK DDENINSQPF MRWRERYLFT MEAVNKASAA TGEVKGHYLN
260 270 280 290 300
VTAATMEEMY ARANFAKELG SVIIMIDLVI GYTAIQTMAK WARDNDMILH
310 320 330 340 350
LHRAGNSTYS RQKNHGMNFR VICKWMRMAG VDHIHAGTVV GKLEGDPIIT
360 370 380 390 400
RGFYKTLLLP KLERNLQEGL FFDMEWASLR KVMPVASGGI HAGQMHQLIH
410 420 430 440 450
YLGEDVVLQF GGGTIGHPDG IQAGATANRV ALEAMILARN ENRDYLTEGP
460 470 480 490
EILREAAKTC GALRTALDLW KDITFNYTST DTSDFVETPT ANI
Length:493
Mass (Da):54,994
Last modified:May 1, 1999 - v1
Checksum:iFF86E3FF8C68C937
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018008 Genomic DNA. Translation: BAA75796.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018008 Genomic DNA. Translation: BAA75796.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BWVX-ray2.40A/C/E/G1-493[»]
1IWAX-ray2.60A/C/E/G/I/K/M/O1-493[»]
ProteinModelPortaliO98949.
SMRiO98949. Positions 14-486.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO98949.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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).

Entry informationi

Entry nameiO98949_9RHOD
AccessioniPrimary (citable) accession number: O98949
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: April 29, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

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".UniRule annotation

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.