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P00874 (RBL_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain

Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:rbcL
Encoded onPlastid; Chloroplast
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01338

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP-Rule MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP-Rule MF_01338

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01338

Subunit structure

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

Subcellular location

Plastidchloroplast HAMAP-Rule MF_01338.

Post-translational modification

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 By similarity. HAMAP-Rule MF_01338

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" By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 22 By similarity
PRO_0000031295
Chain3 – 476474Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338
PRO_0000031296

Sites

Active site1751Proton acceptor By similarity
Active site2941Proton acceptor By similarity
Metal binding2011Magnesium; via carbamate group By similarity
Metal binding2031Magnesium By similarity
Metal binding2041Magnesium By similarity
Binding site1231Substrate; in homodimeric partner By similarity
Binding site1731Substrate By similarity
Binding site1771Substrate By similarity
Binding site2951Substrate By similarity
Binding site3271Substrate By similarity
Binding site3791Substrate By similarity
Site3341Transition state stabilizer By similarity

Amino acid modifications

Modified residue31N-acetylproline By similarity
Modified residue141N6,N6,N6-trimethyllysine By similarity
Modified residue2011N6-carboxylysine By similarity
Disulfide bond247Interchain; in linked form By similarity

Experimental info

Sequence conflict631T → AA in CAA23474. Ref.1
Sequence conflict1531H → R Ref.1
Sequence conflict1551I → M Ref.1
Sequence conflict2281A → S in CAA23474. Ref.1
Sequence conflict2481E → D in CAA23474. Ref.1
Sequence conflict2531R → G in CAA23474. Ref.1
Sequence conflict2591E → Q in CAA23474. Ref.1
Sequence conflict2911Missing in CAA23474. Ref.1
Sequence conflict3941F → L in CAA23474. Ref.1
Sequence conflict4151P → H in CAA23474. Ref.1
Sequence conflict441 – 4433GNE → VQ in CAA23474. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P00874 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 07ECB650E0C8F6E3

FASTA47652,701
        10         20         30         40         50         60 
MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKDTDILAAF RVTPQLGVPP EEAGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV PGDPDQYICY VAYPLDLFEE GSVTNMFTSI 

       130        140        150        160        170        180 
VGNVFGFKAL RALRLEDLRI PPAYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 

       190        200        210        220        230        240 
SAKNYGRACY ECLRGGLDFT KDDENVNSQP FMRWRDRFVF CAEAIYKAQA ETGEIKGHYL 

       250        260        270        280        290        300 
NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTTL SHYCRDNGLL LHIHRAMHAV 

       310        320        330        340        350        360 
IDRQKNHGMH FRVLAKALRM SGGDHIHSGT VVGKLEGERE ITLGFVDLLR DDFIEKDRSR 

       370        380        390        400        410        420 
GIFFTQDWVS MPGVIPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAAAN 

       430        440        450        460        470 
RVALEACVQA RNEGRDLARE GNEIIKAACK WSAELAAACE IWKEIKFDGF KAMDTI 

« Hide

References

« Hide 'large scale' references
[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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V00171 Genomic DNA. Translation: CAA23474.1.
Z11973 Genomic DNA. Translation: CAA78027.1.
X86563 Genomic DNA. Translation: CAA60294.1.
PIRRKZML. A01093.
S58560.
RefSeqNP_043033.1. NC_001666.2.

3D structure databases

ProteinModelPortalP00874.
SMRP00874. Positions 11-476.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP00874.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID845212.
KEGGzma:845212.

Organism-specific databases

GrameneP00874.
MaizeGDB69185.

Phylogenomic databases

HOGENOMHOG000230831.
KOK01601.
ProtClustDBCHL00040.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL_MAIZE
AccessionPrimary (citable) accession number: P00874
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families