Ribulose bisphosphate carboxylase large chain precursor - Physcomitrella patens subsp. patens (Moss)

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P34915 (RBL_PHYPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ribulose bisphosphate carboxylase large chain
Short name=RuBisCO large subunit
EC=4.1.1.39

Gene names

Name:

rbcL

Encoded on

Plastid; Chloroplast

Organism

Physcomitrella patens subsp. patens (Moss) [Reference proteome]

Taxonomic identifier

145481 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Bryophyta › Bryophytina › Bryopsida › Funariidae › Funariales › Funariaceae › Physcomitrella ›

Protein attributes

Sequence length	475 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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-Rule MF_01338
Catalytic activity	2 3-phospho-D-glycerate + 2 H⁺ = D-ribulose 1,5-bisphosphate + CO₂ + H₂O. HAMAP-Rule MF_01338 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O₂. HAMAP-Rule MF_01338
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Subunit structure	Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity.
Subcellular location	Plastid › chloroplast HAMAP-Rule MF_01338.
Post-translational modification	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. HAMAP-Rule 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-Rule MF_01338
Sequence similarities	Belongs to the RuBisCO large chain family. Type I subfamily.

Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation Photorespiration Photosynthesis
Cellular component	Chloroplast Plastid
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
PTM	Acetylation Disulfide bond Methylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	photorespiration Inferred from electronic annotation. Source: UniProtKB-KW reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW ribulose-bisphosphate carboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 2

By similarity

PRO_0000031347

Chain

3 – 475

473

Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338

PRO_0000031348

Sites

Active site

175

Proton acceptor By similarity

Active site

294

Proton acceptor By similarity

Metal binding

201

Magnesium; via carbamate group By similarity

Metal binding

203

Magnesium By similarity

Metal binding

204

Magnesium By similarity

Binding site

123

Substrate; in homodimeric partner By similarity

Binding site

173

Substrate By similarity

Binding site

177

Substrate By similarity

Binding site

295

Substrate By similarity

Binding site

327

Substrate By similarity

Binding site

379

Substrate By similarity

Site

334

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

N-acetylproline By similarity

Modified residue

N6,N6,N6-trimethyllysine By similarity

Modified residue

201

N6-carboxylysine By similarity

Disulfide bond

247

Interchain; in linked form By similarity

Experimental info

Sequence conflict

A → T in CAA52269. Ref.1

Sequence conflict

Q → H in CAA52269. Ref.1

Sequence conflict

A → L in CAA52269. Ref.1

Sequence conflict

190

Y → N in CAA52269. Ref.1

Sequence conflict

251

I → L in CAA52269. Ref.1

Sequence conflict

255 – 256

QF → PC in CAA52269. Ref.1

Sequence conflict

301

L → V in CAA52269. Ref.1

Sequence conflict

339

R → L in CAA52269. Ref.1

Sequence conflict

372 – 374

PGV → QVF in CAA52269. Ref.1

Sequence conflict

385

W → G in CAA52269. Ref.1

Sequence conflict

414

A → T in CAA52269. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P34915 [UniParc].

Last modified November 7, 2003. Version 2.
Checksum: 30A91B8A714507AF
Show »

FASTA

475

52,705

        10         20         30         40         50         60 
MSPRPEIKAG VGFKAGVKDY RLTYYTPDYQ TKDTDILAAF RMTPQPGVPA EECGAAVAAE 

        70         80         90        100        110        120 
SSTGTWTTVW TDGLTSLDRY KGRCYAIEPV AGEENQYIAY VAYPLDLFEE GSVTNLFTSI 

       130        140        150        160        170        180 
VGNVFGFKAL RALRLEDLRI PPAYSKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 

       190        200        210        220        230        240 
SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKSQG ETGEIKGHYL 

       250        260        270        280        290        300 
NATAGTCEEM IKRAQFAREL GMPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV 

       310        320        330        340        350        360 
LDRQKNHGMH FRVLAKALRL SGGDHIHSGT VVGKLEGERQ VTLGFVDLLR DDYIEKDRSR 

       370        380        390        400        410        420 
GIYFTQDWVS LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN 

       430        440        450        460        470 
RVALEACVQA RNEGRDLARE GNEIIREAAK WSPELAAACE VWKEIKFEFD TVDTL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An open reading frame (ycf11) is evolutionary conserved from Cyanobacteria to the plastid DNAs of Archegoniates and Gymnosperms is modified in the plastid DNAs of Dicots and is not plastome encoded in Monocots." Kruse S., Martin W., Wehe M., Reski R. J. Plant Physiol. 146:258-262(1995) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Physcomitrella patens chloroplast genes." Sugita M., Sugiura C. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Protonema.
[3]	"Complete chloroplast DNA sequence of the moss Physcomitrella patens: evidence for the loss and relocation of rpoA from the chloroplast to the nucleus." Sugiura C., Kobayashi Y., Setsuyuki A., Sugita C., Sugita M. Nucleic Acids Res. 31:5324-5331(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Gransden 2004.
[4]	"Cytokinin affects nuclear- and plastome-encoded energy-converting plastid enzymes." Kasten B., Buck F., Nuske J., Reski R. Planta 201:261-272(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 184-195. Tissue: Protonema.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X74156 Genomic DNA. Translation: CAA52269.1. AB066207 Genomic DNA. Translation: BAB62086.1. AP005672 Genomic DNA. Translation: BAC85044.1.
PIR	S34663.
RefSeq	NP_904194.1. NC_005087.1.
3D structure databases
ProteinModelPortal	P34915.
SMR	P34915. Positions 18-473.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2546763.
KEGG	ppp:PhpapaCp031.
Phylogenomic databases
KO	K01601.
ProtClustDB	CHL00040.
Family and domain databases
Gene3D	3.20.20.110. 1 hit. 3.30.70.150. 1 hit.
HAMAP	MF_01338. RuBisCO_L_type1.
InterPro	IPR020878. RuBisCo_large_chain_AS. IPR020888. RuBisCO_lsu. IPR000685. RuBisCO_lsu_C. IPR017443. RuBisCO_lsu_fd_N. IPR017444. RuBisCO_lsu_N. [Graphical view]
Pfam	PF00016. RuBisCO_large. 1 hit. PF02788. RuBisCO_large_N. 1 hit. [Graphical view]
SUPFAM	SSF51649. RuBisCO_large. 1 hit. SSF54966. RuBisCO_large. 1 hit.
PROSITE	PS00157. RUBISCO_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RBL_PHYPA

Accession

Primary (citable) accession number: P34915
Secondary accession number(s): Q95FY7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	November 7, 2003
Last modified:	May 1, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents