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Q31738

- RBL_BREMA

UniProt

Q31738 - RBL_BREMA

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
rbcL
Organism
Brexia madagascariensis
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: 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
OrganismiBrexia madagascariensis
Taxonomic identifieri39394 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCelastralesCelastraceaeBrexia

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_0000031145
Chaini3 – ›469›467Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000031146Add
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

PRIDEiQ31738.

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

ProteinModelPortaliQ31738.
SMRiQ31738. Positions 9-469.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q31738-1 [UniParc]FASTAAdd to Basket

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MSPQTETKAS VGFKAGVKDY KLNYYTPDYE TKDTDILAAF RVTPQPGVPP    50
EEAGAAVAAE SSTGTWTTVW TDGLTSLDRY KGRCYHIEPV AGEENQYIPY 100
VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI PPAYSKTFQG 150
PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT 200
KDDENVNSQP FMRWRDRFLF CAEALYKAQA ETGEIKGHYL NATAGTCEEM 250
MKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV 300
IDRQKNHGMH FRVLAKALRM SGGDHVHAGT VVGKLEGERD ITLGFVDLLR 350
DDFIEKDRSR GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL 400
QFGGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREASK 450
WSPELAAACE VWKEIKFEF 469
Length:469
Mass (Da):52,056
Last modified:November 1, 1996 - v1
Checksum:iA56F292BA21F1F36
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei469 – 4691

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L11176 Genomic DNA. Translation: AAA84093.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L11176 Genomic DNA. Translation: AAA84093.1 .

3D structure databases

ProteinModelPortali Q31738.
SMRi Q31738. Positions 9-469.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q31738.

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. "Phylogenetic relationships among members of Saxifragaceae sensu lato based on rbcL sequence data."
    Morgan D.R., Soltis D.E.
    Ann. Mo. Bot. Gard. 80:631-660(1993)
    [AGRICOLA] [Europe PMC]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Leaf.

Entry informationi

Entry nameiRBL_BREMA
AccessioniPrimary (citable) accession number: Q31738
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 73 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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