Reviewed, UniProtKB/Swiss-Prot Q07209 (RBL_AILAL)

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

Ailanthus altissima (Tree of heaven)

Taxonomic identifier

23810 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Sapindales › Simaroubaceae › Ailanthus

Protein attributes

Sequence length	465 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 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 – 465	›465	Ribulose bisphosphate carboxylase large chain HAMAP MF_01338		PRO_0000062346
Sites
	Active site	165	1	Proton acceptor By similarity
	Active site	284	1	Proton acceptor By similarity
	Metal binding	191	1	Magnesium; via carbamate group By similarity
	Metal binding	193	1	Magnesium By similarity
	Metal binding	194	1	Magnesium By similarity
	Binding site	113	1	Substrate; in homodimeric partner By similarity
	Binding site	163	1	Substrate By similarity
	Binding site	167	1	Substrate By similarity
	Binding site	285	1	Substrate By similarity
	Binding site	317	1	Substrate By similarity
	Binding site	369	1	Substrate By similarity
	Site	324	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	4	1	N6,N6,N6-trimethyllysine By similarity
	Modified residue	191	1	N6-carboxylysine By similarity
	Disulfide bond	237		Interchain; in linked form By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q07209-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: D993D8710B727599	FASTA	465	51,646
	10 20 30 40 50 60 VGFKAGVKDY KLTYYTPEYV TKDTDILAAF RVTPQPGVPP EEAGAAVAAE SSTGTWTTVW 70 80 90 100 110 120 TDGLTSLDRY KGRCYNIEPV AGEENQYICY VAYPLDLFEE GSVTNMFTSI VGNVFGFKAL 130 140 150 160 170 180 RALRLEDLRI PPEYSKTFQG PLHGIQVERD KLNKYGRPLL GCTIKPKLGL SAKNYGRAVY 190 200 210 220 230 240 ECLRGGLDFT KDDENVNSQP FMRWRDRFLF CAEAIYKSQA ETGEIKGHYL NATAGTCEEM 250 260 270 280 290 300 IKRAVFAREL GVPIVMHDYL TGGFTANTSL AHYCRDNGLL LHIHRAMHAV IDRQKNHGMH 310 320 330 340 350 360 FRVLAKALRL SGGDHIHAGT VVGKLEGERD ITLGFVDLLR DDFIEKDRSR GIYFTQDWVS 370 380 390 400 410 420 LPGVLPVASG GIHVWHMPAL TEIFGDDSVL QFGGGTLGHP WGNAPGAVAN RVALEACVQA 430 440 450 460 RNEGRDLARE GNEIIREASK WSPELAAACE VWKEIKFEFP AMDTL

References

[1]	"Affinities of the Australian endemic Akaniaceae: new evidence from rbcL sequences." Gadek P.A., Quinn C.J., Rodman J.E., Karol K.G., Conti E., Price R.A., Fernando E.S. Aust. Syst. Bot. 5:717-724(1992) [Agricola: IND93029186] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	L12566 Genomic DNA. Translation: AAA32637.2.
3D structure databases
HSSP	HSSP built from PDB template 8RUC based on UniProtKB P00875.
SMR	Q07209. Positions 1-465.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.1.1.39. 20469.
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_AILAL

Accession

Primary (citable) accession number: Q07209
Secondary accession number(s): Q38682

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 59 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)