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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Pyropia katadae (Red alga) (Porphyra katadae)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei127 – 1271Substrate; in homodimeric partnerBy similarity
Binding sitei177 – 1771SubstrateBy similarity
Active sitei179 – 1791Proton acceptorBy similarity
Binding sitei181 – 1811SubstrateBy similarity
Metal bindingi205 – 2051Magnesium; via carbamate groupBy similarity
Metal bindingi207 – 2071MagnesiumBy similarity
Metal bindingi208 – 2081MagnesiumBy similarity
Active sitei297 – 2971Proton acceptorBy similarity
Binding sitei298 – 2981SubstrateBy similarity
Binding sitei330 – 3301SubstrateBy similarity
Sitei337 – 3371Transition state stabilizerBy similarity
Binding sitei382 – 3821SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:rbcL
Encoded oniPlastid; Chloroplast
OrganismiPyropia katadae (Red alga) (Porphyra katadae)
Taxonomic identifieri76161 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaBangiophyceaeBangialesBangiaceaePyropia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 488488Ribulose bisphosphate carboxylase large chainPRO_0000277428Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei205 – 2051N6-carboxylysineBy similarity

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ760R9.
SMRiQ760R9. Positions 9-481.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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.

Q760R9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQSVESRTR IKSERYESGV IPYAKMGYWD ADYVIKETDI LALFRITPQP
60 70 80 90 100
GVDPIEASAA IAGESSTATW TVVWTDLLTA CDLYRAKAYR VDPVPNVADQ
110 120 130 140 150
YFAYIAYDID LFEEGSIANL TASIIGNVFG FKAVKALRLE DMRMPVAYLK
160 170 180 190 200
TFQGPATGLI VERERMDKFG RPFLGATVKP KLGLSGKNYG RVVYEGLKGG
210 220 230 240 250
LDFLKDDENI NSQPFMRWRE RFLYSMEGVN KASASAGEIK GHYLNVTAAT
260 270 280 290 300
MEDMYERAEF SKEVGSIICM IDLVIGYTAI QSMAIWARKH DMILHLHRAG
310 320 330 340 350
NSTYSRQKNH GMNFRVICKW MRMAGVDHIH AGTVVGKLEG DPLMIKGFYN
360 370 380 390 400
TLLESDTDIN LPQGLFFAQN WASLRKVVPV ASGGIHAGQM HQLLDYLGDD
410 420 430 440 450
VVLQFGGGTI GHPDGIQAGA TANRVALESM VMARNEGRNY VAEGPQILRD
460 470 480
AAKTCGPLQT ALDLWKDISF NYTSTDTADF VETPTANI
Length:488
Mass (Da):54,060
Last modified:July 5, 2004 - v1
Checksum:iC1847D0EA11284DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB118583 Genomic DNA. Translation: BAC84933.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB118583 Genomic DNA. Translation: BAC84933.1.

3D structure databases

ProteinModelPortaliQ760R9.
SMRiQ760R9. Positions 9-481.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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. "Species determination utilizing Porphyra (Rhodophyta) plastid DNA RuBisCo sequences."
    Kito H., Kunimoto M., Mizukami Y., Murase N., Kuroki T., Taruta M., Levine I.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Thallus.

Entry informationi

Entry nameiRBL_PYRKA
AccessioniPrimary (citable) accession number: Q760R9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: July 5, 2004
Last modified: April 29, 2015
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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" (By similarity).By similarity

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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.