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B8EPF9

- B8EPF9_METSB

UniProt

B8EPF9 - B8EPF9_METSB

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Methylocella silvestris (strain BL2 / DSM 15510 / NCIMB 13906)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei124 – 1241Substrate; in homodimeric partnerUniRule annotation
Binding sitei174 – 1741SubstrateUniRule annotation
Active sitei176 – 1761Proton acceptorUniRule annotation
Binding sitei178 – 1781SubstrateUniRule annotation
Metal bindingi202 – 2021Magnesium; via carbamate groupUniRule annotation
Metal bindingi204 – 2041MagnesiumUniRule annotation
Metal bindingi205 – 2051MagnesiumUniRule annotation
Active sitei294 – 2941Proton acceptorUniRule annotation
Binding sitei295 – 2951SubstrateUniRule annotation
Binding sitei327 – 3271SubstrateUniRule annotation
Sitei334 – 3341Transition state stabilizerUniRule annotation
Binding sitei379 – 3791SubstrateUniRule annotation

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

LyaseUniRule annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciMSIL395965:GCND-1219-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunitUniRule annotation
Gene namesi
Name:cbbLUniRule annotation
Ordered Locus Names:Msil_1195Imported
OrganismiMethylocella silvestris (strain BL2 / DSM 15510 / NCIMB 13906)Imported
Taxonomic identifieri395965 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBeijerinckiaceaeMethylocella
ProteomesiUP000002257: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

Protein-protein interaction databases

STRINGi395965.Msil_1195.

Structurei

3D structure databases

ProteinModelPortaliB8EPF9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO large chain family. Type I subfamily.UniRule annotation

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.

B8EPF9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTASPPAQPR SRYSAGVMEY REMGYWQPDY VPGETDIIAC FRVTPQEGVD
60 70 80 90 100
PIEASAAVAG ESSTATWTVV WTDRLTASEK YRAKCYRVDP VPNAPGSWFA
110 120 130 140 150
FIAYDLDLFE PGSISNLAAS IIGNVFGFKP LRALRLEDMR FPVAYVKTFQ
160 170 180 190 200
GPATGIVVER ERLDKFGRPL LGATVKPKLG LSGRNYGRVV YEALKGGLDF
210 220 230 240 250
TKDDENINSQ PFMHWRDRFL YCMEAVNRAE AATGEIKGTY LNVTAATMED
260 270 280 290 300
MYERAEFAKE LGSVIIMIDL VIGYTAIQSM AKWARRNDMI LHLHRAGHST
310 320 330 340 350
YTRQKIHGVS FRVIAKWMRL AGVDHIHAGT VVGKLEGDPN TTRGYYDICR
360 370 380 390 400
EDYNPQQLEH GIFFDQHWAS LNKLMPVASG GIHAGQMHQL LALLGEDVVL
410 420 430 440 450
QFGGGTIGHP MGIAAGATAN RVALEAMIFA RNCGRDTLAE GQTILEDAAR
460 470 480
GCTPLRQALD VWKDVSFDYT STDSPDFIPT ATPA
Length:484
Mass (Da):53,508
Last modified:March 3, 2009 - v1
Checksum:i07A90129067ABB20
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001280 Genomic DNA. Translation: ACK50164.1.
RefSeqiYP_002361526.1. NC_011666.1.

Genome annotation databases

EnsemblBacteriaiACK50164; ACK50164; Msil_1195.
GeneIDi7092268.
KEGGimsl:Msil_1195.
PATRICi22597875. VBIMetSil55537_1316.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001280 Genomic DNA. Translation: ACK50164.1 .
RefSeqi YP_002361526.1. NC_011666.1.

3D structure databases

ProteinModelPortali B8EPF9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 395965.Msil_1195.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACK50164 ; ACK50164 ; Msil_1195 .
GeneIDi 7092268.
KEGGi msl:Msil_1195.
PATRICi 22597875. VBIMetSil55537_1316.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci MSIL395965:GCND-1219-MONOMER.

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

  1. "Complete genome sequence of the aerobic facultative methanotroph Methylocella silvestris BL2."
    Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B., Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.
    J. Bacteriol. 192:3840-3841(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BL2 / DSM 15510 / NCIMB 13906Imported.

Entry informationi

Entry nameiB8EPF9_METSB
AccessioniPrimary (citable) accession number: B8EPF9
Entry historyi
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: October 29, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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".UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3