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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.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.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

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

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 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: Chloroplast

Organism-specific databases

GrameneiP00874.
MaizeGDBi69185.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-HAMAP
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

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. 1 PublicationCurated
Sequence conflicti153 – 1531H → R1 PublicationCurated
Sequence conflicti155 – 1551I → M1 PublicationCurated
Sequence conflicti228 – 2281A → S in CAA23474. 1 PublicationCurated
Sequence conflicti248 – 2481E → D in CAA23474. 1 PublicationCurated
Sequence conflicti253 – 2531R → G in CAA23474. 1 PublicationCurated
Sequence conflicti259 – 2591E → Q in CAA23474. 1 PublicationCurated
Sequence conflicti291 – 2911Missing in CAA23474. 1 PublicationCurated
Sequence conflicti394 – 3941F → L in CAA23474. 1 PublicationCurated
Sequence conflicti415 – 4151P → H in CAA23474. 1 PublicationCurated
Sequence conflicti441 – 4433GNE → VQ in CAA23474. 1 PublicationCurated

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...
MobiDBi 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: October 29, 2014
This is version 103 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