Reviewed, UniProtKB/Swiss-Prot A2SJJ7 (RBL1B_METPP)

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:	Mpe_A2782

Organism

Methylibium petroleiphilum (strain PM1) [Complete proteome] [HAMAP]

Taxonomic identifier

420662 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Methylibium

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 2 HAMAP MF_01338		PRO_0000299965
Sites
	Active site	177	1	Proton acceptor By similarity
	Active site	295	1	Proton acceptor By similarity
	Metal binding	203	1	Magnesium; via carbamate group By similarity
	Metal binding	205	1	Magnesium By similarity
	Metal binding	206	1	Magnesium By similarity
	Binding site	125	1	Substrate; in homodimeric partner By similarity
	Binding site	175	1	Substrate By similarity
	Binding site	179	1	Substrate By similarity
	Binding site	296	1	Substrate By similarity
	Binding site	328	1	Substrate By similarity
	Binding site	380	1	Substrate By similarity
	Site	335	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	203	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2SJJ7-1 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: 3B36C71F79F2FCAD	FASTA	485	53,310
	10 20 30 40 50 60 MNEPTQITDT KKRYAAGVLK YAQMGYWNGD YVPKDTDILA LFRITPQDGV DPIEAAAAVA 70 80 90 100 110 120 GESSTATWTV VWTDRLTACD MYRAKAYKVE PVPNNPGQYF CYVAYDLSLF EEGSIANVTA 130 140 150 160 170 180 SIIGNVFSFK PLKAARLEDM KFPVSYVKTF AGPPTGIVVE RERLDKFGRP LLGATTKPKL 190 200 210 220 230 240 GLSGRNYGRV VYEGLKGGLD FMKDDENINS QPFMHWRDRF LFVMDAVNKA SAATGEVKGS 250 260 270 280 290 300 YLNVTAGTME EMYRRAEFAK ELGSVIIMID LVVGYTAIQS MSNWARQNDM VLHMHRAGHG 310 320 330 340 350 360 TYTRQKNHGV SFRVIAKWLR MAGVDHLHTG TAVGKLEGDP LTVQGYYNVC RDTHTKVDLP 370 380 390 400 410 420 RGIFFDQDWG ALKKVMPVAS GGIHAGQMHQ LIDLFGDDVV LQFGGGTIGH PQGIQAGATA 430 440 450 460 470 480 NRVALEAMVL ARNEGRDIKN EGPQILRDAA KSCTPLAAAL DTWGDITFNY TSTDTSDYVP TPSVA

References

[1]

"Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1." Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R. J. Bacteriol. 189:1931-1945(2007) [PubMed: 17158667] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000555 Genomic DNA. Translation: ABM95736.1. Different initiation.
RefSeq	YP_001021971.1.
3D structure databases
SMR	A2SJJ7. Positions 49-515.
ModBase	Search...
Genome annotation databases
GeneID	4785032.
GenomeReviews	Gene locus Mpe_A2782 in contig CP000555_GR.
KEGG	mpt:Mpe_A2782.
NMPDR	fig|279263.3.peg.3495.
Organism-specific databases
CMR	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]
ProtoNet	Search...

Entry information

Entry name

RBL1B_METPP

Accession

Primary (citable) accession number: A2SJJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	March 24, 2009
This is version 20 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)