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
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei123 – 1231Substrate; in homodimeric partnerUniRule annotation
Binding sitei173 – 1731SubstrateUniRule annotation
Active sitei175 – 1751Proton acceptorUniRule annotation
Binding sitei177 – 1771SubstrateUniRule annotation
Metal bindingi201 – 2011Magnesium; via carbamate groupUniRule annotation
Metal bindingi203 – 2031MagnesiumUniRule annotation
Metal bindingi204 – 2041MagnesiumUniRule annotation
Active sitei294 – 2941Proton acceptorUniRule annotation
Binding sitei295 – 2951SubstrateUniRule annotation
Binding sitei327 – 3271SubstrateUniRule annotation
Sitei334 – 3341Transition state stabilizerUniRule annotation
Binding sitei379 – 3791SubstrateUniRule annotation

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
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea
ProteomesiUP000007305 Componenti: Chloroplast

Organism-specific databases

GrameneiP00874.
MaizeGDBi69185.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22UniRule annotationPRO_0000031295
Chaini3 – 476474Ribulose bisphosphate carboxylase large chainPRO_0000031296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylprolineUniRule annotation
Modified residuei14 – 141N6,N6,N6-trimethyllysineUniRule annotation
Modified residuei201 – 2011N6-carboxylysineUniRule annotation
Disulfide bondi247 – 247Interchain; 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

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.
SMRiP00874. Positions 11-476.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631T → AA in CAA23474 (Ref. 1) Curated
Sequence conflicti153 – 1531H → R (Ref. 1) Curated
Sequence conflicti155 – 1551I → M (Ref. 1) Curated
Sequence conflicti228 – 2281A → S in CAA23474 (Ref. 1) Curated
Sequence conflicti248 – 2481E → D in CAA23474 (Ref. 1) Curated
Sequence conflicti253 – 2531R → G in CAA23474 (Ref. 1) Curated
Sequence conflicti259 – 2591E → Q in CAA23474 (Ref. 1) Curated
Sequence conflicti291 – 2911Missing in CAA23474 (Ref. 1) Curated
Sequence conflicti394 – 3941F → L in CAA23474 (Ref. 1) Curated
Sequence conflicti415 – 4151P → H in CAA23474 (Ref. 1) Curated
Sequence conflicti441 – 4433GNE → VQ in CAA23474 (Ref. 1) Curated

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.
SMRiP00874. Positions 11-476.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4577.GRMZM5G815453_P01.

Proteomic databases

PRIDEiP00874.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi845212.
KEGGizma:845212.

Organism-specific databases

GrameneiP00874.
MaizeGDBi69185.

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.

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

« Hide 'large scale' publications
  1. "Chloroplast gene sequence for the large subunit of ribulose bisphosphatecarboxylase of maize."
    McIntosh L., Poulsen C., Bogorad L.
    Nature 288:556-560(1980)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Relative rates of nucleotide substitution at the rbcL locus of monocotyledonous plants."
    Gaut B.S., Muse S.V., Clark W.D., Clegg M.T.
    J. Mol. Evol. 35:292-303(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Leaf.
  3. "Complete sequence of the maize chloroplast genome: gene content, hotspots of divergence and fine tuning of genetic information by transcript editing."
    Maier R.M., Neckermann K., Igloi G.L., Koessel H.
    J. Mol. Biol. 251:614-628(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. B73.

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: June 24, 2015
This is version 110 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

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.