Reviewed, UniProtKB/Swiss-Prot P30828 (RBL_MAGLA)

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

Magnolia latahensis

Taxonomic identifier

3409 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › magnoliids › Magnoliales › Magnoliaceae › Magnolia

Protein attributes

Sequence length	253 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 + 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.
Caution	This sequence originates from a miocene fossil leaf sample.

Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation Photorespiration Photosynthesis
Cellular component	Chloroplast Plastid
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
Technical term	Extinct organism protein
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
	Chain	‹1 – ›253	›253	Ribulose bisphosphate carboxylase large chain
Sites
	Active site	87	1	Proton acceptor By similarity
	Active site	206	1	Proton acceptor By similarity
	Metal binding	113	1	Magnesium; via carbamate group By similarity
	Metal binding	115	1	Magnesium By similarity
	Metal binding	116	1	Magnesium By similarity
	Binding site	35	1	Substrate; in homodimeric partner By similarity
	Binding site	85	1	Substrate By similarity
	Binding site	89	1	Substrate By similarity
	Binding site	207	1	Substrate By similarity
	Binding site	239	1	Substrate By similarity
	Site	246	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	113	1	N6-carboxylysine By similarity
	Disulfide bond	159		Interchain; in linked form By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	253	1

Sequences

	Sequence		Length	Mass (Da)
	P30828-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: F182B07840842950	FASTA	253	28,360
	10 20 30 40 50 60 PVAGEENQYI AYVAYPLDLF EEGSVTNMFT SIVGNVFGFK ALRALRLEDL RIPTAYVKTF 70 80 90 100 110 120 QGPPHGIQVE RDKLNKYGRP LLGCTIKPKL GLSAKNYGRA VYECLRGGLD FTKDDENVNS 130 140 150 160 170 180 QPFMRWRDRF LFCAEALYKA QAETGEIKGH YLNATAGTCE EMMKRAIFAR ELGVPIVMHD 190 200 210 220 230 240 YLTGGFTANT SLAHYCRDNG LLLHIHRAMH AVIDRQKNHG IHFRVLAKAL RMSGGDHIHS 250 GTVVGKLEGE RDI

References

[1]	"Chloroplast DNA sequence from a miocene Magnolia species." Golenberg E.M., Giannasi D.E., Clegg M.T., Smiley C.J., Durbin M., Henderson D., Zurawski G. Nature 344:656-658(1990) [PubMed: 2325772] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	X54344 Genomic DNA. Translation: CAA38232.1.
3D structure databases
SMR	P30828. Positions 1-253.
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]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

RBL_MAGLA

Accession

Primary (citable) accession number: P30828

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	September 2, 2008
This is version 53 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)