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P28425

- RBL_HYDVI

UniProt

P28425 - RBL_HYDVI

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

rbcL

Organism
Hydrophyllum virginianum (Eastern waterleaf)
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 sitei114 – 1141Substrate; in homodimeric partnerUniRule annotation
Binding sitei164 – 1641SubstrateUniRule annotation
Active sitei166 – 1661Proton acceptorUniRule annotation
Binding sitei168 – 1681SubstrateUniRule annotation
Metal bindingi192 – 1921Magnesium; via carbamate groupUniRule annotation
Metal bindingi194 – 1941MagnesiumUniRule annotation
Metal bindingi195 – 1951MagnesiumUniRule annotation
Active sitei285 – 2851Proton acceptorUniRule annotation
Binding sitei286 – 2861SubstrateUniRule annotation
Binding sitei318 – 3181SubstrateUniRule annotation
Sitei325 – 3251Transition state stabilizerUniRule annotation
Binding sitei370 – 3701SubstrateUniRule 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
OrganismiHydrophyllum virginianum (Eastern waterleaf)
Taxonomic identifieri4134 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesHydrophyllaceaeHydrophyllum

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 – 467›467Ribulose bisphosphate carboxylase large chainPRO_0000062494Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51N6,N6,N6-trimethyllysineUniRule annotation
Modified residuei192 – 1921N6-carboxylysineUniRule annotation
Disulfide bondi238 – 238Interchain; 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

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

ProteinModelPortaliP28425.
SMRiP28425. Positions 1-454.
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.

P28425-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
SVGFKAGVKE YKLTYYTPEY ETKDTDILAA FRVSPQPGVP PEEAGAAVAA
60 70 80 90 100
ESSTGTWTTV WTDGLTNLDR YKGRCYHIDP VLGEEDQYIA YVAYPLDLFE
110 120 130 140 150
EGSVTNMFTS IVGNVFGFKA LRALRLEDLR IPTAYVKTFQ GPPHGIQVER
160 170 180 190 200
DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF TKDDENVNSQ
210 220 230 240 250
PFMRWRDRLL FCAEAIFKSQ AETGEIKGHY LNATAGNCEE MMKRAVFARE
260 270 280 290 300
LGVPIVMHDY LTGGFTANTT LASYCRDNGL LLHIHRAMHA VIDRQKNHGI
310 320 330 340 350
HFRVLAKALR MSGGDHIHSG TVVGKLEGER NITLSFVVLL RDDYIEKDRS
360 370 380 390 400
RGIFFTQDWV SLPGVLPVAS GGIHVWHMPA LVEIFGDDSV LQFGGGTLGH
410 420 430 440 450
PWGNAPGAVA NRVSLEACVQ ARNEGRDLAR EGNDIIREAC KWSPELAAAC
460
EVWKEIKFEF TDMDTLD
Length:467
Mass (Da):51,905
Last modified:December 1, 1992 - v1
Checksum:iAFD680117497BD9B
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L01927 Genomic DNA. Translation: AAA84324.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L01927 Genomic DNA. Translation: AAA84324.2 .

3D structure databases

ProteinModelPortali P28425.
SMRi P28425. Positions 1-454.
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. "Carnivorous plants: phylogeny and structural evolution."
    Albert V.A., Williams S.E., Chase M.W.
    Science 257:1491-1495(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiRBL_HYDVI
AccessioniPrimary (citable) accession number: P28425
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: October 29, 2014
This is version 78 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