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P48699

- RBL_DENCL

UniProt

P48699 - RBL_DENCL

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
rbcL
Organism
Dendrophthora clavata (Columbian mistletoe)
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 sitei122 – 1221Substrate; in homodimeric partner By similarity
Binding sitei172 – 1721Substrate By similarity
Active sitei174 – 1741Proton acceptor By similarity
Binding sitei176 – 1761Substrate By similarity
Metal bindingi200 – 2001Magnesium; via carbamate group By similarity
Metal bindingi202 – 2021Magnesium By similarity
Metal bindingi203 – 2031Magnesium By similarity
Active sitei293 – 2931Proton acceptor By similarity
Binding sitei294 – 2941Substrate By similarity
Binding sitei326 – 3261Substrate By similarity
Sitei333 – 3331Transition state stabilizer By similarity
Binding sitei378 – 3781Substrate 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
OrganismiDendrophthora clavata (Columbian mistletoe)
Taxonomic identifieri3965 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeSantalalesViscaceaeDendrophthora

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 – 474›474Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000062439Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131N6,N6,N6-trimethyllysine By similarity
Modified residuei200 – 2001N6-carboxylysine By similarity
Disulfide bondi246 – 246Interchain; 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

Proteomic databases

PRIDEiP48699.

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

ProteinModelPortaliP48699.
SMRiP48699. Positions 17-472.

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.

P48699-1 [UniParc]FASTAAdd to Basket

« Hide

SPQXETKASV GFKAGVKDYK LTYYTPDYKT KDTDILAAFR VTPQPGVPPE    50
EAGAAVAAES STGTWTTVWT DGLTSLDRYK GRCYHIEPVA GEENHFIAYV 100
AYPLDLFEEG SVTNMFTSIV GNVFGFKALR ALRLEDLRIP PAYSKTFQGP 150
PHGIQVERDK LNKYGRPLLG CTIKPKLGLS AKNYGRAVYE CLRGGLDFTK 200
DDENVNSQPF MRWRDRFVFC AEAIYKAQAE TGEIKGHYLN ATAGTCEEMI 250
KRAVFARELG VPIIMHDYLT GGFTANTSLA HYCRDNGLLL HIHRAMHAVI 300
DRQKNHGIHF RVLAKALRMS GGDHIHSGTV VGKLEGERDI TLGFVDLLRD 350
DFIAKDRSRG IYFTQDWVSL PGVLPVASGG IHVWHMPALT EIFGDDSVLQ 400
FGGGTLGHPW GNAPGAVANR VALEACVQAR NEGRDLAREG NEIIREASKW 450
SPELAAACEV WKEIKFEFQA VDTL 474
Length:474
Mass (Da):52,452
Last modified:February 1, 1996 - v1
Checksum:i6E9F94ED90BBDFF3
GO

Non-terminal residue

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L26069 Genomic DNA. Translation: AAB97296.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L26069 Genomic DNA. Translation: AAB97296.1 .

3D structure databases

ProteinModelPortali P48699.
SMRi P48699. Positions 17-472.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P48699.

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. "A comparision of angiosperm phylogenies from nuclear 18S rRNA and rbcL sequences."
    Nickrent D.L., Soltis D.E.
    Ann. Mo. Bot. Gard. 82:208-234(1995)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiRBL_DENCL
AccessioniPrimary (citable) accession number: P48699
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 68 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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