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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Zea mays (Maize)
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 sitei123Substrate; in homodimeric partnerUniRule annotation1
Binding sitei173SubstrateUniRule annotation1
Active sitei175Proton acceptorUniRule annotation1
Binding sitei177SubstrateUniRule annotation1
Metal bindingi201Magnesium; via carbamate groupUniRule annotation1
Metal bindingi203MagnesiumUniRule annotation1
Metal bindingi204MagnesiumUniRule annotation1
Active sitei294Proton acceptorUniRule annotation1
Binding sitei295SubstrateUniRule annotation1
Binding sitei327SubstrateUniRule annotation1
Sitei334Transition state stabilizerUniRule annotation1
Binding sitei379SubstrateUniRule 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

SABIO-RKP00874.

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
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
Proteomesi
  • UP000007305 Componenti: Chloroplast

Organism-specific databases

MaizeGDBi69185.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000312951 – 2UniRule annotation2
ChainiPRO_00000312963 – 476Ribulose bisphosphate carboxylase large chainAdd BLAST474

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3N-acetylprolineUniRule annotation1
Modified residuei14N6,N6,N6-trimethyllysineUniRule annotation1
Modified residuei201N6-carboxylysineUniRule annotation1
Disulfide bondi247Interchain; 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

Acetylation, Disulfide bond, Methylation

Proteomic databases

PaxDbiP00874.
PRIDEiP00874.

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

Protein-protein interaction databases

STRINGi4577.GRMZM5G815453_P01.

Structurei

3D structure databases

ProteinModelPortaliP00874.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410IIVP. Eukaryota.
COG1850. LUCA.
HOGENOMiHOG000230831.
KOiK01601.

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.

P00874-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKDTDILAAF RVTPQLGVPP
60 70 80 90 100
EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV PGDPDQYICY
110 120 130 140 150
VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PPAYSKTFQG
160 170 180 190 200
PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRACY ECLRGGLDFT
210 220 230 240 250
KDDENVNSQP FMRWRDRFVF CAEAIYKAQA ETGEIKGHYL NATAGTCEEM
260 270 280 290 300
IKRAVFAREL GVPIVMHDYL TGGFTANTTL SHYCRDNGLL LHIHRAMHAV
310 320 330 340 350
IDRQKNHGMH FRVLAKALRM SGGDHIHSGT VVGKLEGERE ITLGFVDLLR
360 370 380 390 400
DDFIEKDRSR GIFFTQDWVS MPGVIPVASG GIHVWHMPAL TEIFGDDSVL
410 420 430 440 450
QFGGGTLGHP WGNAPGAAAN RVALEACVQA RNEGRDLARE GNEIIKAACK
460 470
WSAELAAACE IWKEIKFDGF KAMDTI
Length:476
Mass (Da):52,701
Last modified:November 1, 1995 - v2
Checksum:i07ECB650E0C8F6E3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti63T → AA in CAA23474 (Ref. 1) Curated1
Sequence conflicti153H → R (Ref. 1) Curated1
Sequence conflicti155I → M (Ref. 1) Curated1
Sequence conflicti228A → S in CAA23474 (Ref. 1) Curated1
Sequence conflicti248E → D in CAA23474 (Ref. 1) Curated1
Sequence conflicti253R → G in CAA23474 (Ref. 1) Curated1
Sequence conflicti259E → Q in CAA23474 (Ref. 1) Curated1
Sequence conflicti291Missing in CAA23474 (Ref. 1) Curated1
Sequence conflicti394F → L in CAA23474 (Ref. 1) Curated1
Sequence conflicti415P → H in CAA23474 (Ref. 1) Curated1
Sequence conflicti441 – 443GNE → VQ in CAA23474 (Ref. 1) Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00171 Genomic DNA. Translation: CAA23474.1.
Z11973 Genomic DNA. Translation: CAA78027.1.
X86563 Genomic DNA. Translation: CAA60294.1.
PIRiA01093. RKZML.
S58560.
RefSeqiNP_043033.1. NC_001666.2.

Genome annotation databases

GeneIDi845212.
KEGGizma:845212.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00171 Genomic DNA. Translation: CAA23474.1.
Z11973 Genomic DNA. Translation: CAA78027.1.
X86563 Genomic DNA. Translation: CAA60294.1.
PIRiA01093. RKZML.
S58560.
RefSeqiNP_043033.1. NC_001666.2.

3D structure databases

ProteinModelPortaliP00874.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4577.GRMZM5G815453_P01.

Proteomic databases

PaxDbiP00874.
PRIDEiP00874.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi845212.
KEGGizma:845212.

Organism-specific databases

MaizeGDBi69185.

Phylogenomic databases

eggNOGiENOG410IIVP. Eukaryota.
COG1850. LUCA.
HOGENOMiHOG000230831.
KOiK01601.

Enzyme and pathway databases

SABIO-RKP00874.

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_MAIZE
AccessioniPrimary (citable) accession number: P00874
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 118 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".UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

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.