Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Dendrophthora clavata (Columbian mistletoe)
Status
Reviewed-Annotation score: Annotation score: 4 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.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)DescriptionActionsGraphical viewLength
Binding sitei122Substrate; in homodimeric partnerUniRule annotation1
Binding sitei172SubstrateUniRule annotation1
Active sitei174Proton acceptorUniRule annotation1
Binding sitei176SubstrateUniRule annotation1
Metal bindingi200Magnesium; via carbamate groupUniRule annotation1
Metal bindingi202MagnesiumUniRule annotation1
Metal bindingi203MagnesiumUniRule annotation1
Active sitei293Proton acceptorUniRule annotation1
Binding sitei294SubstrateUniRule annotation1
Binding sitei326SubstrateUniRule annotation1
Sitei333Transition state stabilizerUniRule annotation1
Binding sitei378SubstrateUniRule annotation1

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 chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunitUniRule annotation
Gene namesi
Name:rbcLUniRule annotation
Encoded oniPlastid; Chloroplast
OrganismiDendrophthora clavata (Columbian mistletoe)
Taxonomic identifieri3965 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeSantalalesViscaceaeDendrophthora

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000062439‹1 – 474Ribulose bisphosphate carboxylase large chainAdd BLAST›474

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei13N6,N6,N6-trimethyllysineUniRule annotation1
Modified residuei200N6-carboxylysineUniRule annotation1
Disulfide bondi246Interchain; in linked formUniRule annotation

Post-translational modificationi

The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.UniRule annotation

Keywords - PTMi

Disulfide bond, Methylation

Proteomic databases

PRIDEiP48699.

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP48699.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Family and domain databases

CDDicd08212. RuBisCO_large_I. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[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: Fragment.

P48699-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SPQXETKASV GFKAGVKDYK LTYYTPDYKT KDTDILAAFR VTPQPGVPPE
60 70 80 90 100
EAGAAVAAES STGTWTTVWT DGLTSLDRYK GRCYHIEPVA GEENHFIAYV
110 120 130 140 150
AYPLDLFEEG SVTNMFTSIV GNVFGFKALR ALRLEDLRIP PAYSKTFQGP
160 170 180 190 200
PHGIQVERDK LNKYGRPLLG CTIKPKLGLS AKNYGRAVYE CLRGGLDFTK
210 220 230 240 250
DDENVNSQPF MRWRDRFVFC AEAIYKAQAE TGEIKGHYLN ATAGTCEEMI
260 270 280 290 300
KRAVFARELG VPIIMHDYLT GGFTANTSLA HYCRDNGLLL HIHRAMHAVI
310 320 330 340 350
DRQKNHGIHF RVLAKALRMS GGDHIHSGTV VGKLEGERDI TLGFVDLLRD
360 370 380 390 400
DFIAKDRSRG IYFTQDWVSL PGVLPVASGG IHVWHMPALT EIFGDDSVLQ
410 420 430 440 450
FGGGTLGHPW GNAPGAVANR VALEACVQAR NEGRDLAREG NEIIREASKW
460 470
SPELAAACEV WKEIKFEFQA VDTL
Length:474
Mass (Da):52,452
Last modified:February 1, 1996 - v1
Checksum:i6E9F94ED90BBDFF3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26069 Genomic DNA. Translation: AAB97296.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26069 Genomic DNA. Translation: AAB97296.1.

3D structure databases

ProteinModelPortaliP48699.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP48699.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd08212. RuBisCO_large_I. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[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...

Entry informationi

Entry nameiRBL_DENCL
AccessioniPrimary (citable) accession number: P48699
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.