Reviewed, UniProtKB/Swiss-Prot P43223 (RBL_ADIPE)

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

Adiantum pedatum (Capillaire)

Taxonomic identifier

29590 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Moniliformopses › Filicophyta › Filicopsida › Filicales › Pteridaceae › Adiantum

Protein attributes

Sequence length	413 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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.
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.
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 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.
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.
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	Disulfide bond
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW 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: UniProtKB-KW 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
	Chain	‹1 – ›413	›413	Ribulose bisphosphate carboxylase large chain HAMAP MF_01338		PRO_0000062341
Sites
	Active site	152	1	Proton acceptor By similarity
	Active site	271	1	Proton acceptor By similarity
	Metal binding	178	1	Magnesium; via carbamate group By similarity
	Metal binding	180	1	Magnesium By similarity
	Metal binding	181	1	Magnesium By similarity
	Binding site	100	1	Substrate; in homodimeric partner By similarity
	Binding site	150	1	Substrate By similarity
	Binding site	154	1	Substrate By similarity
	Binding site	272	1	Substrate By similarity
	Binding site	304	1	Substrate By similarity
	Binding site	356	1	Substrate By similarity
	Site	311	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	178	1	N6-carboxylysine By similarity
	Disulfide bond	224		Interchain; in linked form By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	413	1

Sequences

	Sequence		Length	Mass (Da)
	P43223-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: C3DE2ED825DFFC04	FASTA	413	45,751
	10 20 30 40 50 60 YYTPEYKTKD TDILAAFRMT PQPGVPAEEA GAAVAAESST GTWTTVWTDG LTSLDRYKGR 70 80 90 100 110 120 CYDIEPVAGE ENQYIAYVAY PLDLFEEGSV TNMLTSIVGN VFGFKALRAL RLEDLRIPPA 130 140 150 160 170 180 YSKTFMGPPH GIQVERDKLN KYGRPLLGCT IKPKLGLSAK NYGRAVYECL RGGLDFTKDD 190 200 210 220 230 240 ENVNSQPFMR WRDRFLFVAE ALFKSQAETG EIKGHYLNAT AGTCEEMMKR AVFARELGAP 250 260 270 280 290 300 IVMHDYLTGG FTANTSLAFY CRDNGLLLHI HRAMHAVIDR QRNHGIHFRV LAKALRMSGG 310 320 330 340 350 360 DHIHAGTVVG KLEGEREVTL GFVDLLRDDY IEKDRSRGIY FTQDWVSMPG VFPVASGGIH 370 380 390 400 410 VWHMPALTEI FGDDSVLQFG GGTLGHPWGN APGAVANRVA LEACVQARNE GRD

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
EMBLGenBankDDBJ	U05602 Genomic DNA. Translation: AAA19886.1.
3D structure databases
SMR	P43223. Positions 1-413.
ModBase	Search...
Family and domain databases
HAMAP	MF_01338. [Tree]
InterPro	IPR000685. RuBisCO_lsu_C. IPR017443. RuBisCO_lsu_fd_N. IPR017444. RuBisCO_lsu_N. [Graphical view]
Gene3D	G3DSA:3.20.20.110. RuBisCO_large. 1 hit. G3DSA:3.30.70.150. RuBisCO_large. 1 hit.
Pfam	PF00016. RuBisCO_large. 1 hit. PF02788. RuBisCO_large_N. 1 hit. [Graphical view]
PROSITE	PS00157. RUBISCO_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RBL_ADIPE

Accession

Primary (citable) accession number: P43223

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)