Reviewed, UniProtKB/Swiss-Prot A4WZV1 (RBL2_RHOS5)

Names and origin

Protein names

Recommended name:
    Ribulose bisphosphate carboxylase large chain 2
      Short name=RuBisCO large subunit 2
    EC=4.1.1.39

Gene names

Name:	cbbL2
Ordered Locus Names:	Rsph17025_4063

Encoded on

Plasmid pRSPA02

Organism

Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) [Complete proteome] [HAMAP]

Taxonomic identifier

349102 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	473 AA.
Sequence status	Complete.
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. 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 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 Photosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
Technical term	Complete proteome Plasmid
Gene Ontology (GO)
Biological process	oxidation reduction 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 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 – 473	473	Ribulose bisphosphate carboxylase large chain 2 HAMAP MF_01338		PRO_0000355753
Sites
	Active site	168	1	Proton acceptor By similarity
	Active site	287	1	Proton acceptor By similarity
	Metal binding	194	1	Magnesium; via carbamate group By similarity
	Metal binding	196	1	Magnesium By similarity
	Metal binding	197	1	Magnesium By similarity
	Binding site	116	1	Substrate; in homodimeric partner By similarity
	Binding site	166	1	Substrate By similarity
	Binding site	170	1	Substrate By similarity
	Binding site	288	1	Substrate By similarity
	Binding site	320	1	Substrate By similarity
	Binding site	372	1	Substrate By similarity
	Site	327	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	194	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4WZV1-1 [UniParc]. Last modified May 29, 2007. Version 1. Checksum: C4D940B33CA93819	FASTA	473	53,109
	10 20 30 40 50 60 MAAKTYDAGV KDYRSIYWEP QYQVKDSDIL AVFKVVPQPG VSREEAAAAV AAESSTATWT 70 80 90 100 110 120 TVWTDLLTDL DYYKGRAYAI EDVPGSDEAF YAFIAYPMDL FEEGSVVNVF TSLVGNVFGF 130 140 150 160 170 180 KAVRALRLED VRFPLWFVMT CPGAPHGMKV ERDLLDKYGR PLLGCTIKPK LGLSAKNYGR 190 200 210 220 230 240 AVYECLRGGL DFTKDDENVN SQPFLRWRDR FLFCQEAIEK AEAETGERKG HYMNVTAGTM 250 260 270 280 290 300 EEIYERAEFA KEIGTPIIMS DYLTVGWSAH TSLSRWCRKN GMLLHVHRAM HAVMDRNPNH 310 320 330 340 350 360 GINFRVLAKI LRLMGGDHLH SGTVVGKLEG DREATIGWIN LLRDRFIKAD RSRGIFFDQD 370 380 390 400 410 420 WGPQPGLFPV ASGGIHVWHM PALVSIFGND SVLQFGGGTL GHPWGNAAGA CANRFALEAC 430 440 450 460 470 VQARNDGRNL EKEGKEILTK AAQTSPELRM AMETWKEVRF EFDTVDKLDV QHR

References

[1]

"Complete sequence of plasmid pRSPA02 of Rhodobacter sphaeroides ATCC 17025." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S. Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000663 Genomic DNA. Translation: ABP72915.1.
RefSeq	YP_001170220.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A4WZV1.
Genome annotation databases
GeneID	5086236.
GenomeReviews	Gene locus Rsph17025_4063 in contig CP000663_GR.
KEGG	rsq:Rsph17025_4063.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	KEDRSRG.
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

RBL2_RHOS5

Accession

Primary (citable) accession number: A4WZV1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	May 29, 2007
Last modified:	November 3, 2009
This is version 20 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)