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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.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

Mg2+UniRule annotationNote: Binds 1 Mg(2+) ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei122 – 1221Substrate; in homodimeric partnerUniRule annotation
Binding sitei172 – 1721SubstrateUniRule annotation
Active sitei174 – 1741Proton acceptorUniRule annotation
Binding sitei176 – 1761SubstrateUniRule annotation
Metal bindingi200 – 2001Magnesium; via carbamate groupUniRule annotation
Metal bindingi202 – 2021MagnesiumUniRule annotation
Metal bindingi203 – 2031MagnesiumUniRule annotation
Active sitei293 – 2931Proton acceptorUniRule annotation
Binding sitei294 – 2941SubstrateUniRule annotation
Binding sitei326 – 3261SubstrateUniRule annotation
Sitei333 – 3331Transition state stabilizerUniRule annotation
Binding sitei378 – 3781SubstrateUniRule 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
OrganismiDendrophthora clavata (Columbian mistletoe)
Taxonomic identifieri3965 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeSantalalesViscaceaeDendrophthora

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 – 474›474Ribulose bisphosphate carboxylase large chainPRO_0000062439Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131N6,N6,N6-trimethyllysineUniRule annotation
Modified residuei200 – 2001N6-carboxylysineUniRule annotation
Disulfide bondi246 – 246Interchain; 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

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.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP48699.
SMRiP48699. Positions 17-472.
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.

P48699-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
SPQXETKASV GFKAGVKDYK LTYYTPDYKT KDTDILAAFR VTPQPGVPPE
60 70 80 90 100
EAGAAVAAES STGTWTTVWT DGLTSLDRYK GRCYHIEPVA GEENHFIAYV
110 120 130 140 150
AYPLDLFEEG SVTNMFTSIV GNVFGFKALR ALRLEDLRIP PAYSKTFQGP
160 170 180 190 200
PHGIQVERDK LNKYGRPLLG CTIKPKLGLS AKNYGRAVYE CLRGGLDFTK
210 220 230 240 250
DDENVNSQPF MRWRDRFVFC AEAIYKAQAE TGEIKGHYLN ATAGTCEEMI
260 270 280 290 300
KRAVFARELG VPIIMHDYLT GGFTANTSLA HYCRDNGLLL HIHRAMHAVI
310 320 330 340 350
DRQKNHGIHF RVLAKALRMS GGDHIHSGTV VGKLEGERDI TLGFVDLLRD
360 370 380 390 400
DFIAKDRSRG IYFTQDWVSL PGVLPVASGG IHVWHMPALT EIFGDDSVLQ
410 420 430 440 450
FGGGTLGHPW GNAPGAVANR VALEACVQAR NEGRDLAREG NEIIREASKW
460 470
SPELAAACEV WKEIKFEFQA VDTL
Length:474
Mass (Da):52,452
Last modified:February 1, 1996 - v1
Checksum:i6E9F94ED90BBDFF3
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26069 Genomic DNA. Translation: AAB97296.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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: November 26, 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".UniRule annotation

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3