Ribulose bisphosphate carboxylase large chain - Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)

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Q603Q7 (RBL_METCA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 61. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	MCA2743

Organism

Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath) [Complete proteome] [HAMAP]

Taxonomic identifier

243233 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Methylococcales › Methylococcaceae › Methylococcus ›

Protein attributes

Sequence length	473 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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. Both reactions occur simultaneously and in competition at the same active site. HAMAP-Rule MF_01338
Catalytic activity	2 3-phospho-D-glycerate + 2 H⁺ = D-ribulose 1,5-bisphosphate + CO₂ + H₂O. HAMAP-Rule MF_01338 3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O₂. HAMAP-Rule MF_01338
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Subunit structure	Heterohexadecamer of 8 large chains and 8 small chains By similarity.
Induction	Expressed under both copper-replete and copper-limited growth conditions. HAMAP-Rule MF_01338
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. HAMAP-Rule MF_01338
Sequence similarities	Belongs to the RuBisCO large chain family. Type I subfamily.

Ontologies

Keywords
Biological process	Calvin cycle Carbon dioxide fixation
Ligand	Magnesium Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	reductive pentose-phosphate cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP 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 HAMAP-Rule MF_01338

PRO_0000062628

Sites

Active site

168

Proton acceptor By similarity

Active site

287

Proton acceptor By similarity

Metal binding

194

Magnesium; via carbamate group By similarity

Metal binding

196

Magnesium By similarity

Metal binding

197

Magnesium By similarity

Binding site

116

Substrate; in homodimeric partner By similarity

Binding site

166

Substrate By similarity

Binding site

170

Substrate By similarity

Binding site

288

Substrate By similarity

Binding site

320

Substrate By similarity

Binding site

372

Substrate By similarity

Site

327

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

194

N6-carboxylysine By similarity

Experimental info

Sequence conflict

372

S → F in AAL40972. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q603Q7 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 5CE5048F754EA3DD
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FASTA

473

52,857

        10         20         30         40         50         60 
MAVKTYNAGV KEYRETYWDP NYTPADTDLL AVFKITPQPG VPREEAAAAV AAESSTGTWT 

        70         80         90        100        110        120 
TVWTDLLTDL DYYKGRAYRI EDVPGQDEQF YAFIAYPIDL FEEGSVVNVF TSLVGNVFGF 

       130        140        150        160        170        180 
KAVRGLRLED VRFPLAYVMT CGGPPHGIQV ERDIMNKYGR PLLGCTIKPK LGLSAKNYGR 

       190        200        210        220        230        240 
AVYECLRGGL DFTKDDENVN SQPFMRWRQR FDFVMEAIEK AEAETGERKG HYLNVTAPTP 

       250        260        270        280        290        300 
EEMYKRAEYA KEIGAPIIMH DFITGGFCAN TGLANWCRNN GMLLHIHRAM HAVMDRNPNH 

       310        320        330        340        350        360 
GIHFRVFTKM LRLSGGDHLH TGTVVGKLEG DRQATLGWID LLRERSIKED RSRGIFFDQE 

       370        380        390        400        410        420 
WGAMPGVFAV ASGGIHVWHM PALLSIFGDD AVFQFGGGTL GHPWGNAAGA AANRVALEAC 

       430        440        450        460        470 
VEARNEGRQL EKEGKEILTE AAKSSPELKA AMETWKEIKF EFDTVDKLDV AHR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The ribulose-1,5-bisphosphate carboxylase/oxygenase gene cluster of Methylococcus capsulatus (Bath)." Baxter N.J., Hirt R.P., Bodrossy L., Kovacs K.L., Embley T.M., Prosser J.I., Murrell J.C. Arch. Microbiol. 177:279-289(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], EXPRESSION. Strain: ATCC 33009 / NCIMB 11132 / Bath.
[2]	"Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath)." Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S., Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E., Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J. Eisen J.A. PLoS Biol. 2:1616-1628(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33009 / NCIMB 11132 / Bath.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF447860 Genomic DNA. Translation: AAL40972.1. AE017282 Genomic DNA. Translation: AAU91176.1.
RefSeq	YP_115143.1. NC_002977.6.
3D structure databases
ProteinModelPortal	Q603Q7.
SMR	Q603Q7. Positions 16-460.
ModBase	Search...
Protein-protein interaction databases
STRING	243233.MCA2743.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAU91176; AAU91176; MCA2743.
GeneID	3104087.
KEGG	mca:MCA2743.
PATRIC	22609356. VBIMetCap22254_2773.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1850.
HOGENOM	HOG000230831.
KO	K01601.
OMA	YKGRAYA.
ProtClustDB	PRK04208.
Family and domain databases
Gene3D	3.20.20.110. 1 hit. 3.30.70.150. 1 hit.
HAMAP	MF_01338. RuBisCO_L_type1.
InterPro	IPR020878. RuBisCo_large_chain_AS. IPR020888. RuBisCO_lsu. IPR000685. RuBisCO_lsu_C. IPR017443. RuBisCO_lsu_fd_N. IPR017444. RuBisCO_lsu_N. [Graphical view]
Pfam	PF00016. RuBisCO_large. 1 hit. PF02788. RuBisCO_large_N. 1 hit. [Graphical view]
SUPFAM	SSF51649. RuBisCO_large. 1 hit. SSF54966. RuBisCO_large. 1 hit.
PROSITE	PS00157. RUBISCO_LARGE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RBL_METCA

Accession

Primary (citable) accession number: Q603Q7
Secondary accession number(s): Q8VR29

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	November 23, 2004
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents