Reviewed, UniProtKB/Swiss-Prot P54205 (RBL_SYNY3)

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:	cbbL
Synonyms:	rbcL
Ordered Locus Names:	slr0009

Organism

Synechocystis sp. (strain PCC 6803) [Complete proteome] [HAMAP]

Taxonomic identifier

1148 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

Protein attributes

Sequence length	470 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein 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.
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
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
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
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW monooxygenase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct ribulose-bisphosphate carboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
trxA	P52231	1	EBI-862277,EBI-862916

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 470	470	Ribulose bisphosphate carboxylase large chain HAMAP MF_01338		PRO_0000062655
Sites
	Active site	170	1	Proton acceptor By similarity
	Active site	289	1	Proton acceptor By similarity
	Metal binding	196	1	Magnesium; via carbamate group By similarity
	Metal binding	198	1	Magnesium By similarity
	Metal binding	199	1	Magnesium By similarity
	Binding site	118	1	Substrate; in homodimeric partner By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	172	1	Substrate By similarity
	Binding site	290	1	Substrate By similarity
	Binding site	322	1	Substrate By similarity
	Binding site	374	1	Substrate By similarity
	Site	329	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	196	1	N6-carboxylysine By similarity
	Disulfide bond	242		Interchain; in linked form By similarity

Sequences

	Sequence		Length	Mass (Da)
	P54205-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 45B9322482745B2B	FASTA	470	52,491
	10 20 30 40 50 60 MVQAKAGFKA GVQDYRLTYY TPDYTPKDTD LLACFRMTPQ PGVPAEEAAA AVAAESSTGT 70 80 90 100 110 120 WTTVWTDNLT DLDRYKGRCY DLEAVPNEDN QYFAFIAYPL DLFEEGSVTN VLTSLVGNVF 130 140 150 160 170 180 GFKALRALRL EDIRFPVALI KTFQGPPHGI TVERDKLNKY GRPLLGCTIK PKLGLSAKNY 190 200 210 220 230 240 GRAVYECLRG GLDFTKDDEN INSQPFMRWR DRFLFVQEAI EKAQAETNEM KGHYLNVTAG 250 260 270 280 290 300 TCEEMMKRAE FAKEIGTPII MHDFFTGGFT ANTTLARWCR DNGILLHIHR AMHAVVDRQK 310 320 330 340 350 360 NHGIHFRVLA KCLRLSGGDH LHSGTVVGKL EGERGITMGF VDLMREDYVE EDRSRGIFFT 370 380 390 400 410 420 QDYASMPGTM PVASGGIHVW HMPALVEIFG DDSCLQFGGG TLGHPWGNAP GATANRVALE 430 440 450 460 470 ACVQARNEGR NLAREGNDVI REACRWSPEL AAACELWKEI KFEFEAMDTL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Construction of a Synechocystis PCC6803 mutant suitable for the study of variant hexadecameric ribulose bisphosphate carboxylase/oxygenase enzymes." Amichay D., Levitz R., Gurevitz M. Plant Mol. Biol. 23:465-476(1993) [PubMed: 8219082] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome." Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S. DNA Res. 2:153-166(1995) [PubMed: 8590279] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	X65960 Genomic DNA. Translation: CAA46773.1. BA000022 Genomic DNA. Translation: BAA10190.1.
PIR	S39561.
RefSeq	NP_442120.1.
3D structure databases
HSSP	HSSP built from PDB template 1RBL based on UniProtKB P00880.
SMR	P54205. Positions 3-470.
ModBase	Search...
Protein-protein interaction databases
IntAct	P54205. 2 interactions.
Genome annotation databases
GeneID	952593.
GenomeReviews	Gene locus slr0009 in contig BA000022_GR.
KEGG	syn:slr0009.
NMPDR	fig|1148.1.peg.2221.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P54205.
OMA	P54205. YTPDYTP.
Enzyme and pathway databases
BioCyc	MetaCyc:MON-750. SSP1148:SLR0009-MON.
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_SYNY3

Accession

Primary (citable) accession number: P54205

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 66 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)