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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score: Annotation score: 5 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 (PubMed:3681999, PubMed:2928307). Both reactions occur simultaneously and in competition at the same active site.Curated2 Publications

Catalytic activityi

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

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei123Substrate; in homodimeric partner1
Binding sitei173Substrate1
Active sitei175Proton acceptor1
Binding sitei177Substrate1
Metal bindingi201Magnesium; via carbamate group1
Metal bindingi203Magnesium1
Metal bindingi204Magnesium1
Active sitei294Proton acceptor1
Binding sitei295Substrate1
Binding sitei327Substrate1
Sitei334Transition state stabilizer1
Binding sitei379Substrate1

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

SABIO-RKP00876.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain (EC:4.1.1.391 Publication)
Short name:
RuBisCO large subunit
Gene namesi
Name:rbcL
Synonyms:rbcA
Encoded oniPlastid; Chloroplast
OrganismiNicotiana tabacum (Common tobacco)
Taxonomic identifieri4097 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000314271 – 21 Publication2
ChainiPRO_00000314283 – 477Ribulose bisphosphate carboxylase large chainAdd BLAST475

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3N-acetylproline1 Publication1
Modified residuei14N6,N6,N6-trimethyllysine1 Publication1
Modified residuei201N6-carboxylysine1 Publication1
Disulfide bondi247Interchain; in linked form3 Publications

Post-translational modificationi

The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 3RUB and 4RUB may be the result of oxidation during crystallization (PubMed:1512238).By similarity1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, Methylation

Proteomic databases

PRIDEiP00876.

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.2 Publications

Protein-protein interaction databases

DIPiDIP-42221N.
MINTiMINT-1176576.

Structurei

Secondary structure

1477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 24Combined sources4
Beta strandi36 – 44Combined sources9
Helixi50 – 59Combined sources10
Turni60 – 62Combined sources3
Helixi71 – 73Combined sources3
Helixi77 – 80Combined sources4
Beta strandi83 – 89Combined sources7
Beta strandi91 – 95Combined sources5
Beta strandi97 – 103Combined sources7
Helixi105 – 107Combined sources3
Helixi113 – 121Combined sources9
Helixi124 – 126Combined sources3
Beta strandi130 – 139Combined sources10
Helixi142 – 145Combined sources4
Beta strandi151 – 153Combined sources3
Helixi155 – 162Combined sources8
Beta strandi169 – 173Combined sources5
Beta strandi175 – 178Combined sources4
Helixi182 – 194Combined sources13
Beta strandi198 – 201Combined sources4
Beta strandi207 – 209Combined sources3
Beta strandi210 – 212Combined sources3
Helixi214 – 232Combined sources19
Beta strandi237 – 241Combined sources5
Helixi247 – 260Combined sources14
Beta strandi263 – 268Combined sources6
Helixi269 – 272Combined sources4
Helixi274 – 287Combined sources14
Beta strandi290 – 294Combined sources5
Helixi298 – 302Combined sources5
Beta strandi307 – 309Combined sources3
Helixi311 – 321Combined sources11
Beta strandi324 – 327Combined sources4
Beta strandi332 – 334Combined sources3
Helixi336 – 350Combined sources15
Beta strandi352 – 354Combined sources3
Helixi358 – 360Combined sources3
Beta strandi375 – 381Combined sources7
Helixi384 – 386Combined sources3
Helixi387 – 394Combined sources8
Beta strandi396 – 403Combined sources8
Turni404 – 408Combined sources5
Helixi413 – 432Combined sources20
Helixi437 – 451Combined sources15
Helixi453 – 466Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EJ7X-ray2.45L3-477[»]
1RLCX-ray2.70L1-477[»]
1RLDX-ray2.50A/B22-467[»]
3RUBX-ray2.00L1-477[»]
4RUBX-ray2.70A/B/C/D1-477[»]
ProteinModelPortaliP00876.
SMRiP00876.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00876.

Family & Domainsi

Sequence similaritiesi

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00876-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPQTETKAS VGFKAGVKEY KLTYYTPEYQ TKDTDILAAF RVTPQPGVPP
60 70 80 90 100
EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYRIERV VGEKDQYIAY
110 120 130 140 150
VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PPAYVKTFQG
160 170 180 190 200
PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT
210 220 230 240 250
KDDENVNSQP FMRWRDRFLF CAEALYKAQA ETGEIKGHYL NATAGTCEEM
260 270 280 290 300
IKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV
310 320 330 340 350
IDRQKNHGIH FRVLAKALRM SGGDHIHSGT VVGKLEGERD ITLGFVDLLR
360 370 380 390 400
DDFVEQDRSR GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL
410 420 430 440 450
QFGGGTLGHP WGNAPGAVAN RVALEACVKA RNEGRDLAQE GNEIIREACK
460 470
WSPELAAACE VWKEIVFNFA AVDVLDK
Length:477
Mass (Da):52,898
Last modified:June 1, 2001 - v2
Checksum:i232D54E42263198F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti284C → G AA sequence (Ref. 3) Curated1
Sequence conflicti377V → E in AAD15025 (PubMed:7160620).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti394F → V.1 Publication1
Natural varianti405G → M.1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01450 Genomic DNA. Translation: AAD15025.1.
Z00044 Genomic DNA. Translation: CAA77361.1.
PIRiA01095. RKNTL.
RefSeqiNP_054507.1. NC_001879.2.

Genome annotation databases

GeneIDi800513.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01450 Genomic DNA. Translation: AAD15025.1.
Z00044 Genomic DNA. Translation: CAA77361.1.
PIRiA01095. RKNTL.
RefSeqiNP_054507.1. NC_001879.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EJ7X-ray2.45L3-477[»]
1RLCX-ray2.70L1-477[»]
1RLDX-ray2.50A/B22-467[»]
3RUBX-ray2.00L1-477[»]
4RUBX-ray2.70A/B/C/D1-477[»]
ProteinModelPortaliP00876.
SMRiP00876.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-42221N.
MINTiMINT-1176576.

Proteomic databases

PRIDEiP00876.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi800513.

Enzyme and pathway databases

SABIO-RKP00876.

Miscellaneous databases

EvolutionaryTraceiP00876.

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_TOBAC
AccessioniPrimary (citable) accession number: P00876
Secondary accession number(s): Q32716
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 1, 2001
Last modified: November 30, 2016
This is version 128 of the entry and version 2 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".1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.