Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q33015

- RBL_PTEVI

UniProt

Q33015 - RBL_PTEVI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Pteris vittata (Chinese ladder brake)
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 sitei113 – 1131Substrate; in homodimeric partnerUniRule annotation
Binding sitei163 – 1631SubstrateUniRule annotation
Active sitei165 – 1651Proton acceptorUniRule annotation
Binding sitei167 – 1671SubstrateUniRule annotation
Metal bindingi191 – 1911Magnesium; via carbamate groupUniRule annotation
Metal bindingi193 – 1931MagnesiumUniRule annotation
Metal bindingi194 – 1941MagnesiumUniRule annotation
Active sitei284 – 2841Proton acceptorUniRule annotation
Binding sitei285 – 2851SubstrateUniRule annotation
Binding sitei317 – 3171SubstrateUniRule annotation
Sitei324 – 3241Transition state stabilizerUniRule annotation
Binding sitei369 – 3691SubstrateUniRule annotation

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 chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunitUniRule annotation
Gene namesi
Name:rbcLUniRule annotation
Encoded oniPlastid; Chloroplast
OrganismiPteris vittata (Chinese ladder brake)
Taxonomic identifieri13821 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaMoniliformopsesPolypodiidaePolypodialesPteridaceaePteris

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›440›440Ribulose bisphosphate carboxylase large chainPRO_0000062577Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41N6,N6,N6-trimethyllysineUniRule annotation
Modified residuei191 – 1911N6-carboxylysineUniRule annotation
Disulfide bondi237 – 237Interchain; 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

Disulfide bond, Methylation

Proteomic databases

PRIDEiQ33015.

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

ProteinModelPortaliQ33015.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

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.

Q33015 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
VGFKAGVKDY RLTYYTPEYK TKDTDILAAF RMTPQPGVPA EEAGAAVAAE
60 70 80 90 100
SSTGTWTTVW TDGLTSLDRY KGRCYDIEPV AGEENQYIAY VAYPLDLFEE
110 120 130 140 150
GSVTNMLTSI VGNVFGXKAX RALRLEDLRI LPAYSKTFIG PPHGIQVERD
160 170 180 190 200
KLNKYGRPLL GCTIKPKLGL CAKNYGRAVY ECLRGGLDFT KDDENVNSQP
210 220 230 240 250
SMRWRDRFLF VAEALFKAQA ETGEVKGHYL NATAGTCEEM IKRATFAREL
260 270 280 290 300
GAPIVMHDYL TGGFTANTSL AFYCRDNGLL LHIHRAMHAV IDRQRNHGMH
310 320 330 340 350
LRVLAKALRM SGGDHIHAGT VVGKLEGERE VTLGFVDLLR DDYIEKDRSR
360 370 380 390 400
GIYFTQDWVS MPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP
410 420 430 440
WGNAPGAVAN RVALEACVQA RNEGRDLARE GNEIIREASK
Length:440
Mass (Da):48,575
Last modified:November 1, 1997 - v1
Checksum:i904A064E8BB40578
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei440 – 4401

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05941 Genomic DNA. Translation: AAC48966.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05941 Genomic DNA. Translation: AAC48966.1 .

3D structure databases

ProteinModelPortali Q33015.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q33015.

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 of dennstaedtioid ferns: evidence from rbcL sequences."
    Wolf P.G., Soltis P.S., Soltis D.E.
    Mol. Phylogenet. Evol. 3:383-392(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Leaf.

Entry informationi

Entry nameiRBL_PTEVI
AccessioniPrimary (citable) accession number: Q33015
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 74 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".UniRule annotation

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3