Reviewed, UniProtKB/Swiss-Prot P36476 (RBL_ADICA)

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 capillus-veneris (Maidenhair fern)

Taxonomic identifier

13818 [NCBI]

Taxonomic lineage

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

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 transcript 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.
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	Acetylation Disulfide bond Methylation
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
	Propeptide	1 – 2	2	By similarity		PRO_0000031101
	Chain	3 – 475	473	Ribulose bisphosphate carboxylase large chain HAMAP MF_01338		PRO_0000031102
Sites
	Active site	175	1	Proton acceptor By similarity
	Active site	294	1	Proton acceptor By similarity
	Metal binding	201	1	Magnesium; via carbamate group By similarity
	Metal binding	203	1	Magnesium By similarity
	Metal binding	204	1	Magnesium By similarity
	Binding site	123	1	Substrate; in homodimeric partner By similarity
	Binding site	173	1	Substrate By similarity
	Binding site	177	1	Substrate By similarity
	Binding site	295	1	Substrate By similarity
	Binding site	327	1	Substrate By similarity
	Binding site	379	1	Substrate By similarity
	Site	334	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	3	1	N-acetylproline By similarity
	Modified residue	14	1	N6,N6,N6-trimethyllysine By similarity
	Modified residue	201	1	N6-carboxylysine By similarity
	Disulfide bond	247		Interchain; in linked form By similarity

Sequences

	Sequence		Length	Mass (Da)
	P36476-1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: DF0BFC53861EA998	FASTA	475	52,634
	10 20 30 40 50 60 MSPQTETKAG VGFKAGVKDY RLTYYTPEYK TKDTDILAAF RMTPQPGVPA EEAGAAVAAE 70 80 90 100 110 120 SSTGTWTTVW TDGLTSLDRY KGRCYDIEPV AGEENQYIAY VAYPLDLFEE GSVTNMLTSI 130 140 150 160 170 180 VGNVFGFKAL RALRLEDLRI PPAYSKTFLG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 190 200 210 220 230 240 SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFLF VAEALFKSQA ETGEIKGHYL 250 260 270 280 290 300 NATAGTCEEM MKRAVFAREL GAPIVMHDYL TGGFTANTSL AFYCRDNGLL LHIHRAMHAV 310 320 330 340 350 360 IDRQKNHGIH FRVLAKALRM SGGDHIHAGT VVGKLEGERE VTLGFVDLLR DDYIEKDRSR 370 380 390 400 410 420 GIYFTQDWVS MPGVFPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN 430 440 450 460 470 RVALEACVQA RNEGRDLARE GNEIIREASK WSPELAAACE IWKAIKFEFE TIDTL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Phylogenetic relationships of ferns deduced from rbcL gene sequence." Hasebe M., Ito M., Kofuji R., Ueda K., Iwatsuki K. J. Mol. Evol. 37:476-482(1993) [PubMed: 8283479] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Leaf.
[2]	"Complete nucleotide sequence of the chloroplast genome from a leptosporangiate fern, Adiantum capillus-veneris L." Wolf P.G., Rowe C.A., Sinclair R.B., Hasebe M. DNA Res. 10:59-65(2003) [PubMed: 12755170] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"High levels of RNA editing in a vascular plant chloroplast genome: analysis of transcripts from the fern Adiantum capillus-veneris." Wolf P.G., Rowe C.A., Hasebe M. Gene 339:89-97(2004) [PubMed: 15363849] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ABSENCE OF RNA EDITING. Tissue: Frond.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D14880 Genomic DNA. Translation: BAA03599.1. AY178864 Genomic DNA. Translation: AAP29399.1.
RefSeq	NP_848068.1.
3D structure databases
HSSP	HSSP built from PDB template 1RBL based on UniProtKB P00880.
SMR	P36476. Positions 11-475.
ModBase	Search...
Genome annotation databases
GeneID	807346.
Enzyme and pathway databases
BRENDA	4.1.1.39. 296414.
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_ADICA

Accession

Primary (citable) accession number: P36476

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 65 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)