Reviewed, UniProtKB/Swiss-Prot Q6N9J0 (RBL1_RHOPA)

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
Ordered Locus Names:	RPA1559

Organism

Rhodopseudomonas palustris [Complete proteome] [HAMAP]

Taxonomic identifier

1076 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Rhodopseudomonas

Protein attributes

Sequence length	485 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
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 – 485	485	Ribulose bisphosphate carboxylase large chain HAMAP MF_01338		PRO_0000062646
Sites
	Active site	176	1	Proton acceptor By similarity
	Active site	294	1	Proton acceptor By similarity
	Metal binding	202	1	Magnesium; via carbamate group By similarity
	Metal binding	204	1	Magnesium By similarity
	Metal binding	205	1	Magnesium By similarity
	Binding site	124	1	Substrate; in homodimeric partner By similarity
	Binding site	174	1	Substrate By similarity
	Binding site	178	1	Substrate By similarity
	Binding site	295	1	Substrate By similarity
	Binding site	327	1	Substrate By similarity
	Binding site	379	1	Substrate By similarity
	Site	334	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	202	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6N9J0-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: F16FDCB22E8061B7	FASTA	485	53,914
	10 20 30 40 50 60 MNEAVTIRGK ERYKSGVMEY KKMGYWEPDY EPKDTDVIAL FRVTPQDGVD PIEAAAAVAG 70 80 90 100 110 120 ESSTATWTVV WTDRLTAAEK YRAKCYRVDP VPNSLGQYFA YIAYDLDLFE PGSISNLTAS 130 140 150 160 170 180 IIGNVFGFKP LKALRLEDMR LPIAYVKTFQ GPATGIVVER ERMDKFGRPL LGATVKPKLG 190 200 210 220 230 240 LSGRNYGRVV YEALKGGLDF TKDDENINSQ PFMHWRERFQ YCMEAVNKAQ AQTGEIKGTY 250 260 270 280 290 300 LNVTAATMED MYERAEYAKE LGSIIVMIDL VIGYTAIQSM AKWARKNDMI LHLHRAGHST 310 320 330 340 350 360 YTRQRNHGVS FRVIAKWMRL AGVDHIHAGT VVGKLEGDPA TTKGYYDICR EDFNPMTLEN 370 380 390 400 410 420 GLFFDQHWAS LNKLMPVASG GIHAGQMHQL LHLLGEDVVL QFGGGTIGHP MGIAAGATAN 430 440 450 460 470 480 RVALEAMILA RNEGRDYLHE GPEILAKAAQ TCTPLKAALD TWKNVTFNYE STDTPDYAPT PSVSV

References

[1]

"Complete genome sequence of the metabolically versatile photosynthetic bacterium Rhodopseudomonas palustris." Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., Harrison F.H., Gibson J., Harwood C.S. Nat. Biotechnol. 22:55-61(2004) [PubMed: 14704707] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-98 / CGA009.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX572597 Genomic DNA. Translation: CAE27000.1.
RefSeq	NP_946905.1.
3D structure databases
SMR	Q6N9J0. Positions 12-477.
ModBase	Search...
Genome annotation databases
GeneID	2691334.
GenomeReviews	Gene locus RPA1559 in contig BX571963_GR.
KEGG	rpa:RPA1559.
NMPDR	fig|258594.1.peg.1549.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6N9J0.
OMA	QYFAYIA.
Enzyme and pathway databases
BioCyc	RPAL258594:RPA1559-MON.
BRENDA	4.1.1.39. 373.
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

RBL1_RHOPA

Accession

Primary (citable) accession number: Q6N9J0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	July 5, 2004
Last modified:	November 3, 2009
This is version 39 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)