Reviewed, UniProtKB/Swiss-Prot Q8RTI2 (RBL2_MAGMG)

Names and origin

Protein names

Recommended name:
    Ribulose bisphosphate carboxylase
      Short name=RuBisCO
    EC=4.1.1.39

Gene names

Name:

cbbM

Organism

Magnetospirillum magnetotacticum (Aquaspirillum magnetotacticum)

Taxonomic identifier

188 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Magnetospirillum

Protein attributes

Sequence length	459 AA.
Sequence status	Complete.
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. HAMAP MF_01339
Catalytic activity	2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O. HAMAP MF_01339 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2. HAMAP MF_01339
Cofactor	Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01339
Subunit structure	Homodimer By similarity. HAMAP MF_01339
Miscellaneous	The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits By similarity. HAMAP MF_01339
Sequence similarities	Belongs to the RuBisCO large chain family. Type II subfamily.

Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
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
Cellular component	plastid Inferred from electronic annotation. Source: InterPro
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 – 459	459	Ribulose bisphosphate carboxylase HAMAP MF_01339		PRO_0000062663
Sites
	Active site	166	1	Proton acceptor By similarity
	Active site	287	1	Proton acceptor By similarity
	Metal binding	191	1	Magnesium; via carbamate group By similarity
	Metal binding	193	1	Magnesium By similarity
	Metal binding	194	1	Magnesium By similarity
	Binding site	111	1	Substrate; in homodimeric partner By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	288	1	Substrate By similarity
	Binding site	321	1	Substrate By similarity
	Binding site	368	1	Substrate By similarity
	Site	329	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	191	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8RTI2-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 7BAF901EE932774F	FASTA	459	50,217
	10 20 30 40 50 60 MDQSKRYVNL ALSEADLIKG GRHVLCAYRM RPRPGHGYVE TAAHFAAESS TGTNVEVCTT 70 80 90 100 110 120 DDFTRGVDAL VYEVDEAEGL MKIAYPVDLF DRNIIDGKAM IASFLTLTVG NNQGMSDVEN 130 140 150 160 170 180 AKMEDFYVPP EFLKLFDGPA CNISHMWKVL GRPEVNGGMV VGTIIKPKLG LRPKPFADAC 190 200 210 220 230 240 HQFWLGGDFI KNDEPQGNQV FAPLKETMRL VADAMRRAQD ETGVPKLLSA NITADDPAEM 250 260 270 280 290 300 IARGNFILET FGENASHVAF LVDGFVAGPT AVTTCRRNFP DTFLHYHRAG HGAITSRQSK 310 320 330 340 350 360 RGYTVLVHMK MARLLGASGI HTGTMGYGKM EGAPDEKMVA YMLERQIAEG PYYRQDWGGM 370 380 390 400 410 420 ASCTPIISGG MSALRLPGFF DNLGHSNVIQ TSGGGAFGHK DGAIAGALSL RQAHEAWLKK 430 440 450 IDLVDYAQTH AELRGAFESF ASDADRLYPG WRDRLRIAA

References

[1]	"Chemolithoautotrophy in the marine, magnetotactic bacterial strains MV-1 and MV-2." Bazylinski D.A., Dean A.J., Williams T.J., Long L.K., Middleton S.L., Dubbels B.L. Arch. Microbiol. 182:373-387(2004) [PubMed: 15338111] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MS-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF442517 Genomic DNA. Translation: AAL76920.1.
3D structure databases
SMR	Q8RTI2. Positions 2-457.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.1.1.39. 258821.
Family and domain databases
HAMAP	MF_01339. RuBisCO_L_type2. [Tree]
InterPro	IPR020871. RuBisCO. IPR020878. RuBisCo_large_chain_AS. 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_MAGMG

Accession

Primary (citable) accession number: Q8RTI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	June 1, 2002
Last modified:	January 19, 2010
This is version 38 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)