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P00874

- RBL_MAIZE

UniProt

P00874 - RBL_MAIZE

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
rbcL
Organism
Zea mays (Maize)
Status
Reviewed - 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 By similarity.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

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei123 – 1231Substrate; in homodimeric partner By similarity
Binding sitei173 – 1731Substrate By similarity
Active sitei175 – 1751Proton acceptor By similarity
Binding sitei177 – 1771Substrate By similarity
Metal bindingi201 – 2011Magnesium; via carbamate group By similarity
Metal bindingi203 – 2031Magnesium By similarity
Metal bindingi204 – 2041Magnesium By similarity
Active sitei294 – 2941Proton acceptor By similarity
Binding sitei295 – 2951Substrate By similarity
Binding sitei327 – 3271Substrate By similarity
Sitei334 – 3341Transition state stabilizer By similarity
Binding sitei379 – 3791Substrate By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. photorespiration Source: UniProtKB-KW
  2. reductive pentose-phosphate cycle Source: UniProtKB-KW
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 chain (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:rbcL
Encoded oniPlastid; Chloroplast
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea
ProteomesiUP000007305: Chloroplast

Organism-specific databases

GrameneiP00874.
MaizeGDBi69185.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22 By similarity
PRO_0000031295
Chaini3 – 476474Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000031296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylproline By similarity
Modified residuei14 – 141N6,N6,N6-trimethyllysine By similarity
Modified residuei201 – 2011N6-carboxylysine By similarity
Disulfide bondi247 – 247Interchain; in linked form By similarity

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 By similarity.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 By similarity.

Structurei

3D structure databases

ProteinModelPortaliP00874.
SMRiP00874. Positions 11-476.

Family & Domainsi

Sequence similaritiesi

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

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MSPQTETKAS VGFKAGVKDY KLTYYTPEYE TKDTDILAAF RVTPQLGVPP    50
EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV PGDPDQYICY 100
VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PPAYSKTFQG 150
PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRACY ECLRGGLDFT 200
KDDENVNSQP FMRWRDRFVF CAEAIYKAQA ETGEIKGHYL NATAGTCEEM 250
IKRAVFAREL GVPIVMHDYL TGGFTANTTL SHYCRDNGLL LHIHRAMHAV 300
IDRQKNHGMH FRVLAKALRM SGGDHIHSGT VVGKLEGERE ITLGFVDLLR 350
DDFIEKDRSR GIFFTQDWVS MPGVIPVASG GIHVWHMPAL TEIFGDDSVL 400
QFGGGTLGHP WGNAPGAAAN RVALEACVQA RNEGRDLARE GNEIIKAACK 450
WSAELAAACE IWKEIKFDGF KAMDTI 476
Length:476
Mass (Da):52,701
Last modified:November 1, 1995 - v2
Checksum:i07ECB650E0C8F6E3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631T → AA in CAA23474. 1 Publication
Sequence conflicti153 – 1531H → R1 Publication
Sequence conflicti155 – 1551I → M1 Publication
Sequence conflicti228 – 2281A → S in CAA23474. 1 Publication
Sequence conflicti248 – 2481E → D in CAA23474. 1 Publication
Sequence conflicti253 – 2531R → G in CAA23474. 1 Publication
Sequence conflicti259 – 2591E → Q in CAA23474. 1 Publication
Sequence conflicti291 – 2911Missing in CAA23474. 1 Publication
Sequence conflicti394 – 3941F → L in CAA23474. 1 Publication
Sequence conflicti415 – 4151P → H in CAA23474. 1 Publication
Sequence conflicti441 – 4433GNE → VQ in CAA23474. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
V00171 Genomic DNA. Translation: CAA23474.1 .
Z11973 Genomic DNA. Translation: CAA78027.1 .
X86563 Genomic DNA. Translation: CAA60294.1 .
PIRi A01093. RKZML.
S58560.
RefSeqi NP_043033.1. NC_001666.2.

3D structure databases

ProteinModelPortali P00874.
SMRi P00874. Positions 11-476.
ModBasei Search...

Proteomic databases

PRIDEi P00874.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 845212.
KEGGi zma:845212.

Organism-specific databases

Gramenei P00874.
MaizeGDBi 69185.

Phylogenomic databases

HOGENOMi HOG000230831.
KOi K01601.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01338. RuBisCO_L_type1.
InterProi IPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 101 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" By similarity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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