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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Galdieria sulphuraria (Red alga)
Status
Reviewed-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)DescriptionActionsGraphical viewLength
Binding sitei132Substrate; in homodimeric partnerUniRule annotation1
Binding sitei182SubstrateUniRule annotation1
Active sitei184Proton acceptorUniRule annotation1
Binding sitei186SubstrateUniRule annotation1
Metal bindingi210Magnesium; via carbamate groupUniRule annotation1
Metal bindingi212MagnesiumUniRule annotation1
Metal bindingi213MagnesiumUniRule annotation1
Active sitei302Proton acceptorUniRule annotation1
Binding sitei303SubstrateUniRule annotation1
Binding sitei335SubstrateUniRule annotation1
Sitei342Transition state stabilizerUniRule annotation1
Binding sitei387SubstrateUniRule 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

Enzyme and pathway databases

BRENDAi4.1.1.39. 2381.

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
OrganismiGaldieria sulphuraria (Red alga)
Taxonomic identifieri130081 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaBangiophyceaeCyanidialesCyanidiaceaeGaldieria

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000624761 – 493Ribulose bisphosphate carboxylase large chainAdd BLAST493

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei210N6-carboxylysineUniRule annotation1

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-60089N.

Structurei

Secondary structure

1493
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 33Combined sources5
Beta strandi45 – 53Combined sources9
Helixi59 – 69Combined sources11
Helixi79 – 83Combined sources5
Helixi86 – 89Combined sources4
Beta strandi92 – 99Combined sources8
Beta strandi102 – 112Combined sources11
Helixi114 – 116Combined sources3
Helixi122 – 130Combined sources9
Helixi133 – 135Combined sources3
Turni136 – 138Combined sources3
Beta strandi139 – 148Combined sources10
Helixi151 – 154Combined sources4
Helixi163 – 171Combined sources9
Beta strandi178 – 182Combined sources5
Beta strandi184 – 187Combined sources4
Helixi191 – 204Combined sources14
Beta strandi207 – 210Combined sources4
Beta strandi216 – 218Combined sources3
Helixi223 – 241Combined sources19
Beta strandi246 – 250Combined sources5
Helixi256 – 269Combined sources14
Beta strandi272 – 277Combined sources6
Helixi278 – 280Combined sources3
Helixi282 – 294Combined sources13
Beta strandi298 – 302Combined sources5
Turni304 – 306Combined sources3
Helixi307 – 310Combined sources4
Beta strandi311 – 317Combined sources7
Helixi319 – 329Combined sources11
Beta strandi332 – 335Combined sources4
Beta strandi339 – 341Combined sources3
Helixi347 – 358Combined sources12
Beta strandi360 – 362Combined sources3
Turni366 – 369Combined sources4
Beta strandi383 – 386Combined sources4
Helixi392 – 394Combined sources3
Helixi395 – 402Combined sources8
Beta strandi407 – 411Combined sources5
Helixi412 – 415Combined sources4
Helixi421 – 440Combined sources20
Helixi445 – 458Combined sources14
Helixi461 – 469Combined sources9
Turni470 – 473Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4F0HX-ray1.96A1-493[»]
4F0KX-ray2.05A1-493[»]
4F0MX-ray2.25A1-493[»]
ProteinModelPortaliP23755.
SMRiP23755.
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: Complete.

P23755-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQSLEEKSV 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
FAYIKTFQGP ATGVILERER LDKFGRPLLG CTTKPKLGLS GKNYGRVVYE
210 220 230 240 250
ALKGGLDFVK DDENINSQPF MRWRERYLFV MEAVNKAAAA TGEVKGHYLN
260 270 280 290 300
VTAATMEEMY ARAQLAKELG SVIIMIDLVI GYTAIQTMAK WARDNDMILH
310 320 330 340 350
LHRAGNSTYS RQKNHGMNFR VICKWMRMAG VDHIHAGTVV GKLEGDPIIT
360 370 380 390 400
RGFYKTLLLP KLERNLQEGL FFDMDWASLR KVMPVASGGI HAGQMHQLIH
410 420 430 440 450
YLGEDVVLQF GGGTIGHPDG IQSGATANRV ALEAMILARN ENRDFLTEGP
460 470 480 490
EILREAAKNC GALRTALDLW KDITFNYTST DTSDFVETPT ANI
Length:493
Mass (Da):54,989
Last modified:November 1, 1991 - v1
Checksum:iB69EE280D47C6FA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55524 Genomic DNA. Translation: CAA39140.1.
AF233069 Genomic DNA. Translation: AAF81681.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55524 Genomic DNA. Translation: CAA39140.1.
AF233069 Genomic DNA. Translation: AAF81681.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4F0HX-ray1.96A1-493[»]
4F0KX-ray2.05A1-493[»]
4F0MX-ray2.25A1-493[»]
ProteinModelPortaliP23755.
SMRiP23755.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60089N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi4.1.1.39. 2381.

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_GALSU
AccessioniPrimary (citable) accession number: P23755
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 30, 2016
This is version 96 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".UniRule annotation

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.