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Q603Q7

- RBL_METCA

UniProt

Q603Q7 - RBL_METCA

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, MCA2743
Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

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.UniRule annotation

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotation
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.UniRule annotation

Cofactori

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161Substrate; in homodimeric partner By similarity
Binding sitei166 – 1661Substrate By similarity
Active sitei168 – 1681Proton acceptor By similarity
Binding sitei170 – 1701Substrate By similarity
Metal bindingi194 – 1941Magnesium; via carbamate group By similarity
Metal bindingi196 – 1961Magnesium By similarity
Metal bindingi197 – 1971Magnesium By similarity
Active sitei287 – 2871Proton acceptor By similarity
Binding sitei288 – 2881Substrate By similarity
Binding sitei320 – 3201Substrate By similarity
Sitei327 – 3271Transition state stabilizer By similarity
Binding sitei372 – 3721Substrate By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:cbbL
Ordered Locus Names:MCA2743
OrganismiMethylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Taxonomic identifieri243233 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaMethylococcalesMethylococcaceaeMethylococcus
ProteomesiUP000006821: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000062628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941N6-carboxylysine By similarity

Proteomic databases

PRIDEiQ603Q7.

Expressioni

Inductioni

Expressed under both copper-replete and copper-limited growth conditions.UniRule annotation

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains By similarity.

Protein-protein interaction databases

STRINGi243233.MCA2743.

Structurei

3D structure databases

ProteinModelPortaliQ603Q7.
SMRiQ603Q7. Positions 16-460.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
OrthoDBiEOG6ZKXMS.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q603Q7-1 [UniParc]FASTAAdd to Basket

« Hide

MAVKTYNAGV KEYRETYWDP NYTPADTDLL AVFKITPQPG VPREEAAAAV    50
AAESSTGTWT TVWTDLLTDL DYYKGRAYRI EDVPGQDEQF YAFIAYPIDL 100
FEEGSVVNVF TSLVGNVFGF KAVRGLRLED VRFPLAYVMT CGGPPHGIQV 150
ERDIMNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENVN 200
SQPFMRWRQR FDFVMEAIEK AEAETGERKG HYLNVTAPTP EEMYKRAEYA 250
KEIGAPIIMH DFITGGFCAN TGLANWCRNN GMLLHIHRAM HAVMDRNPNH 300
GIHFRVFTKM LRLSGGDHLH TGTVVGKLEG DRQATLGWID LLRERSIKED 350
RSRGIFFDQE WGAMPGVFAV ASGGIHVWHM PALLSIFGDD AVFQFGGGTL 400
GHPWGNAAGA AANRVALEAC VEARNEGRQL EKEGKEILTE AAKSSPELKA 450
AMETWKEIKF EFDTVDKLDV AHR 473
Length:473
Mass (Da):52,857
Last modified:November 23, 2004 - v1
Checksum:i5CE5048F754EA3DD
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti372 – 3721S → F in AAL40972. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF447860 Genomic DNA. Translation: AAL40972.1.
AE017282 Genomic DNA. Translation: AAU91176.1.
RefSeqiWP_010961949.1. NC_002977.6.
YP_115143.1. NC_002977.6.

Genome annotation databases

EnsemblBacteriaiAAU91176; AAU91176; MCA2743.
GeneIDi3104087.
KEGGimca:MCA2743.
PATRICi22609356. VBIMetCap22254_2773.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF447860 Genomic DNA. Translation: AAL40972.1 .
AE017282 Genomic DNA. Translation: AAU91176.1 .
RefSeqi WP_010961949.1. NC_002977.6.
YP_115143.1. NC_002977.6.

3D structure databases

ProteinModelPortali Q603Q7.
SMRi Q603Q7. Positions 16-460.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243233.MCA2743.

Proteomic databases

PRIDEi Q603Q7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAU91176 ; AAU91176 ; MCA2743 .
GeneIDi 3104087.
KEGGi mca:MCA2743.
PATRICi 22609356. VBIMetCap22254_2773.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi FTQDWAS.
OrthoDBi EOG6ZKXMS.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01338. RuBisCO_L_type1.
InterProi IPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33009 / NCIMB 11132 / Bath.

Entry informationi

Entry nameiRBL_METCA
AccessioniPrimary (citable) accession number: Q603Q7
Secondary accession number(s): Q8VR29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 23, 2004
Last modified: September 3, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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