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P43222 (RBL_ACRAU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain
Short name=RuBisCO large subunit
EC=4.1.1.39
Gene names
Name:rbcL
Encoded onPlastid; Chloroplast
OrganismAcrostichum aureum (Golden leather fern)
Taxonomic identifier29594 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Moniliformopses › Polypodiopsida › Polypodiales › Pteridaceae › Acrostichum

Protein attributes

Sequence length417 AA.
Sequence statusFragment.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP MF_01338

Catalytic activity

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP MF_01338

3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP MF_01338

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01338

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains By similarity.

Subcellular location

Plastid › chloroplast HAMAP MF_01338.

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. HAMAP MF_01338

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›417›417Ribulose bisphosphate carboxylase large chain HAMAP MF_01338
PRO_0000062338

Sites

Active site1551Proton acceptor By similarity
Active site2741Proton acceptor By similarity
Metal binding1811Magnesium; via carbamate group By similarity
Metal binding1831Magnesium By similarity
Metal binding1841Magnesium By similarity
Binding site1031Substrate; in homodimeric partner By similarity
Binding site1531Substrate By similarity
Binding site1571Substrate By similarity
Binding site2751Substrate By similarity
Binding site3071Substrate By similarity
Binding site3591Substrate By similarity
Site3141Transition state stabilizer By similarity

Amino acid modifications

Modified residue1811N6-carboxylysine By similarity

Experimental info

Non-terminal residue11
Non-terminal residue4171

Sequences

Sequence LengthMass (Da)Tools
P43222 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 97EF24CB0F6B39AA

FASTA41746,284
        10         20         30         40         50         60 
DLTYYTPEYQ TKDTDILAAF RMTPQPGVPA EEAGAAVAAE SSTGTWTTVW TDGLTTLDRY 

        70         80         90        100        110        120 
KGRCYDIEPV PGEENQYIAY VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL RALRLEDLRI 

       130        140        150        160        170        180 
PPAYPKTFIG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT 

       190        200        210        220        230        240 
KDDENVNSQP FMRWRDRFLF VAEALFKALA ETGEIKGHYL NATAGTSEEM MKRARFAREL 

       250        260        270        280        290        300 
GAPIVMHDYL TGGFTANTSL AFYCRDNGLL LHIHRAMHAV IDRQRNHGMH FRVLAKALRM 

       310        320        330        340        350        360 
SGGDHIHAGT VVGKLEGERE VTLGFVDLLR DDYIEKDRSR GIYFTQDWVS MPGVIPVASG 

       370        380        390        400        410 
GIHVWHMPAL TEIFGDDAVL QFCGGTLGHP WGNAPGAVAN RVALEACVQA RNEGRDL

« Hide

References

[1]"rbcL gene sequences provide evidence for the evolutionary lineages of leptosporangiate ferns."
Hasebe M., Omori T., Nakazawa M., Sano T., Kato M., Iwatsuki K.
Proc. Natl. Acad. Sci. U.S.A. 91:5730-5734(1994) [PubMed: 8202555] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U05601 Genomic DNA. Translation: AAA19885.1.

3D structure databases

ProteinModelPortalP43222.
SMRP43222. Positions 2-417.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_01338. RuBisCO_L_type1.
[Tree]
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
Gene3DG3DSA:3.20.20.110. RuBisCO_large. 1 hit.
G3DSA:3.30.70.150. RuBisCO_large. 1 hit.
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRBL_ACRAU
AccessionPrimary (citable) accession number: P43222
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 28, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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