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P92397

- RBL_LUPAL

UniProt

P92397 - RBL_LUPAL

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
rbcL
Organism
Lupinus albus (White lupin) (Lupinus termis)
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 sitei114 – 1141Substrate; in homodimeric partner By similarity
Binding sitei164 – 1641Substrate By similarity
Active sitei166 – 1661Proton acceptor By similarity
Binding sitei168 – 1681Substrate By similarity
Metal bindingi192 – 1921Magnesium; via carbamate group By similarity
Metal bindingi194 – 1941Magnesium By similarity
Metal bindingi195 – 1951Magnesium By similarity
Active sitei285 – 2851Proton acceptor By similarity
Binding sitei286 – 2861Substrate By similarity
Binding sitei318 – 3181Substrate By similarity
Sitei325 – 3251Transition state stabilizer By similarity
Binding sitei370 – 3701Substrate By similarity

GO - Molecular functioni

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

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
OrganismiLupinus albus (White lupin) (Lupinus termis)
Taxonomic identifieri3870 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeGenisteaeLupinus

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
Chaini‹1 – ›455›455Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000062508Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51N6,N6,N6-trimethyllysine By similarity
Modified residuei192 – 1921N6-carboxylysine By similarity
Disulfide bondi238 – 238Interchain; 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

Disulfide bond, Methylation

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

ProteinModelPortaliP92397.
SMRiP92397. Positions 9-455.

Family & Domainsi

Sequence similaritiesi

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: Fragment.

P92397-1 [UniParc]FASTAAdd to Basket

« Hide

SVGFKAGVKD YKLTYYTPDY ETKDTDILAA FRVTPQPGVP PEEAGAAVAA    50
ESSTGTWTTV WTDGLTSLDR YKGRCYHIEP VAGEENQFIA YVAYPLDLFE 100
EGSVTNMFTS IVGNVFGFKA LRALRLEDLR IPNAYVKTFQ GPPHGIQVER 150
DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF TKDDENVNSQ 200
PFMRWRDRFL FCAEALYKAQ AETGEIKGHY LNATAGTCEE MIKRAVFARE 250
LGVPIVMHDY LTGGFTANTS LAHYCRDNGL LLHIHRAMHA VIDRQKNHGM 300
HFRVLAKALR LSGGDHIHSG TVVGKLEGER EITLGFVDLL RDDFVEKDRS 350
RGIYFTQDWV SLPGVLPVAS GGIHVWHMPA LTEIFGDDSV LQFGGGTLGH 400
PWGNAPGAVA NRVALEACVQ ARNEGRDLAS EGNQIIREAS KWSPELAAAC 450
EVWKE 455
Length:455
Mass (Da):50,315
Last modified:May 1, 1997 - v1
Checksum:iFC9AD8CF670CE339
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei455 – 4551

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z70068 Genomic DNA. Translation: CAA93927.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z70068 Genomic DNA. Translation: CAA93927.1 .

3D structure databases

ProteinModelPortali P92397.
SMRi P92397. Positions 9-455.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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

  1. "Molecular phylogeny of the Papilionoideae (family Leguminosae): rbcL sequences versus chemical taxonomy."
    Kaess E., Wink M.
    Bot. Acta 108:149-162(1995)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Leaf.

Entry informationi

Entry nameiRBL_LUPAL
AccessioniPrimary (citable) accession number: P92397
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: February 19, 2014
This is version 71 of the entry and version 1 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.

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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