Reviewed, UniProtKB/Swiss-Prot O99000 (RBL_ADEOB)

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

Adenium obesum (Desert rose)

Taxonomic identifier

69375 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Gentianales › Apocynaceae › Apocynoideae › Wrightieae › Adenium

Protein attributes

Sequence length	466 AA.
Sequence status	Fragment.
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. 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; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity. HAMAP MF_01338
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. 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.

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 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
	Chain	‹1 – 466	›466	Ribulose bisphosphate carboxylase large chain HAMAP MF_01338		PRO_0000062340
Sites
	Active site	166	1	Proton acceptor By similarity
	Active site	285	1	Proton acceptor By similarity
	Metal binding	192	1	Magnesium; via carbamate group By similarity
	Metal binding	194	1	Magnesium By similarity
	Metal binding	195	1	Magnesium By similarity
	Binding site	114	1	Substrate; in homodimeric partner By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	286	1	Substrate By similarity
	Binding site	318	1	Substrate By similarity
	Binding site	370	1	Substrate By similarity
	Site	325	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	5	1	N6,N6,N6-trimethyllysine By similarity
	Modified residue	192	1	N6-carboxylysine By similarity
	Disulfide bond	238		Interchain; in linked form By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	O99000-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 17A0BA0A21D13F50	FASTA	466	51,650
	10 20 30 40 50 60 SVGFKAGVKE YKLTYYTPEY ETKDTDILAA FRVTPQPGVP PEEAGAAVAA ESSTGTWTTV 70 80 90 100 110 120 WTDGLTSLDR YKGRCYHIEP VPGEEDQYIA YVAYPLDLFE EGSVTNMLTS IVGNVFGFKA 130 140 150 160 170 180 LRALRLEDLR IPPAYIKTFQ GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV 190 200 210 220 230 240 YECLRGGLDF TKDDENVNSQ PFMRWRDRFL FCAEAIFKAQ AETGEIKGHY LNATAGTCEE 250 260 270 280 290 300 MYKRAVFARE LGAPIVMHDY LTGGFTANTS LAHYCRDNGL LLHIHRAMHA VIDRQKNHGM 310 320 330 340 350 360 HFRVLAKALR MSGGDHIHAG TVVGKLEGER DITLGFVDLL RDDFIEKDRS RGIYFTQDWV 370 380 390 400 410 420 SLPGVLAVAS GGIHVWHMPA LTEIFGDDSV LQFGGGTLGH PWGNAPGAVA NRVALEACVQ 430 440 450 460 ARNEGRDLAV EGNEIIREAS KWSPELAAAC EVWKEIRFNF KAVDTL

References

[1]	"Morphology and molecular data in phylogenetic fraternity: the tribe Wrightieae (Apocynaceae) revisited." Sennblad B., Endress M.E., Bremer B. Am. J. Bot. 85:1143-1158(1998) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ002880 Genomic DNA. Translation: CAB38851.1.
3D structure databases
SMR	O99000. Positions 1-463.
ModBase	Search...
Family and domain databases
HAMAP	MF_01338. RuBisCO_L_type1. [Tree]
InterPro	IPR020878. RuBisCo_large_chain_AS. IPR020888. RuBisCO_lsu. 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_ADEOB

Accession

Primary (citable) accession number: O99000

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	May 1, 1999
Last modified:	January 19, 2010
This is version 57 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)