Reviewed, UniProtKB/Swiss-Prot P48694 (RBL_COFAR)

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

Coffea arabica (Coffee)

Taxonomic identifier

13443 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Gentianales › Rubiaceae › Ixoroideae › Coffeeae › Coffea

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 + CO(2) + H(2)O. 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O(2).
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.
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 Methylation
Gene Ontology (GO)
Molecular function	ribulose-bisphosphate carboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Propeptide	1 – 2	2	By similarity
	Chain	3 – 481	479	Ribulose bisphosphate carboxylase large chain
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
Experimental info
	Sequence conflict	89	1	P → H in CAA58609 and CAA57001. Ref.2 Ref.3
	Sequence conflict	387	1	M → I in CAA58609 and CAA57001. Ref.2 Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P48694-1 [UniParc]. Last modified November 28, 2006. Version 2. Checksum: 3A6DBC8F05C1EE72	FASTA	481	53,354
	10 20 30 40 50 60 MSPQTETKAS VGFKAGVKEY KLTYYTPEYE TKDTDILAAF RVTPQPGVPP EEAGAAVAAE 70 80 90 100 110 120 SSTGTWTAVW TDGLTSLDRY KGRCYHIEPV PGEENQYIAY VAYPLDLFEE GSVTNMFTSI 130 140 150 160 170 180 VGNVFGFKAL RALRLEDLRV PPAYIKTFQG PPHGIQVERD KLNKYGRPLL GCTIKPKLGL 190 200 210 220 230 240 SAKNYGRAVY ECLRGGLDFT KDDENVNSQP FMRWRDRFCF CAEALFKAQA ETGEIKGHYL 250 260 270 280 290 300 NATAGTCEEM IKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV 310 320 330 340 350 360 IDRQKNHGMH FRVLAKGLRM SGGDHIHAGT VVGKLEGERD ITLGFVDLLR DDFIEKDRSR 370 380 390 400 410 420 GIYFTQDWVS LPGVIPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN 430 440 450 460 470 480 RVALEACVKA RNEGRDLAAE GNEIIREASK WSPELAAACE VWKEIRFNFE AMDKLDKEKD L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete nucleotide sequence of the coffee (Coffea arabica L.) chloroplast genome: organization and implications for biotechnology and phylogenetic relationships amongst angiosperms." Samson N., Bausher M.G., Lee S.-B., Jansen R.K., Daniell H. Plant Biotechnol. J. 5:339-353(2007) [PubMed: 17309688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"Comparison of the evolution of ribulose-1, 5-biphosphate carboxylase (rbcL) and atpB-rbcL noncoding spacer sequences in a recent plant group, the tribe Rubieae (Rubiaceae)." Manen J.F., Natali A. J. Mol. Evol. 41:920-927(1995) [PubMed: 8587137] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-453.
[3]	"Subfamilial and tribal relationships in the Rubiaceae based on rbcL sequence data." Bremer B., Andreasen K., Olsson D. Ann. Mo. Bot. Gard. 82:383-397(1995) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-481.

Cross-references

Sequence databases
EMBLGenBankDDBJ	EF044213 Genomic DNA. Translation: ABJ89687.1. X81095 Genomic DNA. Translation: CAA57001.1. X83631 Genomic DNA. Translation: CAA58609.1.
PIR	S47224.
RefSeq	YP_817490.1.
3D structure databases
HSSP	HSSP built from PDB template 3RUB based on UniProtKB P00876.
SMR	P48694. Positions 11-475.
ModBase	Search...
Genome annotation databases
GeneID	4421771.
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:3.30.70.150. 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]
ProDom	P48694. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

RBL_COFAR

Accession

Primary (citable) accession number: P48694
Secondary accession number(s): A0A343

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	November 28, 2006
Last modified:	September 2, 2008
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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