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E8TEA0

- E8TEA0_MESCW

UniProt

E8TEA0 - E8TEA0_MESCW

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Mesorhizobium ciceri bv. biserrulae (strain HAMBI 2942 / LMG 23838 / WSM1271)
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

Note: Binds 1 magnesium ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei136 – 1361Substrate; in homodimeric partnerUniRule annotation
Binding sitei186 – 1861SubstrateUniRule annotation
Active sitei188 – 1881Proton acceptorUniRule annotation
Binding sitei190 – 1901SubstrateUniRule annotation
Metal bindingi214 – 2141Magnesium; via carbamate groupUniRule annotation
Metal bindingi216 – 2161MagnesiumUniRule annotation
Metal bindingi217 – 2171MagnesiumUniRule annotation
Active sitei306 – 3061Proton acceptorUniRule annotation
Binding sitei307 – 3071SubstrateUniRule annotation
Binding sitei339 – 3391SubstrateUniRule annotation
Sitei346 – 3461Transition state stabilizerUniRule annotation
Binding sitei391 – 3911SubstrateUniRule 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

BioCyciMCIC765698:GHQ5-4336-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:Mesci_4283Imported
OrganismiMesorhizobium ciceri bv. biserrulae (strain HAMBI 2942 / LMG 23838 / WSM1271)Imported
Taxonomic identifieri765698 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium
ProteomesiUP000007471: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei214 – 2141N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliE8TEA0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.
OMAiCTPLKQA.

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.

E8TEA0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNKIDILPAG TLKEGKERYK SGVIPYKKMG YWEPDYRPKE TDLIAMFRIT
60 70 80 90 100
PQPGVDHEEA AAAIAGESST ATWTVVWTDR LTACELYRAK AFRSEPVPNT
110 120 130 140 150
GPGTKTEQQY FAYIAYDLDL FEPGSIANLT ASIIGNVFGF KAVKALRLED
160 170 180 190 200
MRIPVAYLKT FQGPATGIVV ERERLDKFGR PLLGATTKPK LGLSGRNYGR
210 220 230 240 250
VVYEALKGGL DFVKDDENIN SQPFMHWRDR FLYCMEAVNK ASAATGEVKG
260 270 280 290 300
HYLNVTAGTM EEMYERAEFA KQLGSCIVMI DLVIGYTAIQ SMAKWARRND
310 320 330 340 350
MILHLHRAGN STYSRQKNHG MNFRVICKWM RMAGVDHIHA GTVVGKLEGD
360 370 380 390 400
PLMIKGFYDT LREERTPQNL ETGLFFDQEW ASLNKVMPVA SGGIHAGQMH
410 420 430 440 450
QLIHYLGEDV ILQFGGGTIG HPDGIQAGAT ANRVALEAMI LARNEGRDYL
460 470 480 490
REGTKILEQA ARWCTPLKAA LETWKDVTFN YESTDTADFV PTATPSF
Length:497
Mass (Da):55,476
Last modified:April 5, 2011 - v1
Checksum:i95D543D064004907
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002447 Genomic DNA. Translation: ADV13393.1.
RefSeqiWP_013532056.1. NC_014923.1.
YP_004143443.1. NC_014923.1.

Genome annotation databases

EnsemblBacteriaiADV13393; ADV13393; Mesci_4283.
GeneIDi10119774.
KEGGimci:Mesci_4283.
PATRICi45258702. VBIMesCic160642_4780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002447 Genomic DNA. Translation: ADV13393.1 .
RefSeqi WP_013532056.1. NC_014923.1.
YP_004143443.1. NC_014923.1.

3D structure databases

ProteinModelPortali E8TEA0.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADV13393 ; ADV13393 ; Mesci_4283 .
GeneIDi 10119774.
KEGGi mci:Mesci_4283.
PATRICi 45258702. VBIMesCic160642_4780.

Phylogenomic databases

HOGENOMi HOG000230831.
KOi K01601.
OMAi CTPLKQA.

Enzyme and pathway databases

BioCyci MCIC765698:GHQ5-4336-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 sequence of chromosome of Mesorhizobium ciceri bv. biserrulae WSM1271."
    Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Nandasena K., Reeve W.G., Howieson J.G., O'Hara G., Tiwari R.P., Woyke T.
    Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HAMBI 2942 / LMG 23838 / WSM1271Imported.

Entry informationi

Entry nameiE8TEA0_MESCW
AccessioniPrimary (citable) accession number: E8TEA0
Entry historyi
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: November 26, 2014
This is version 29 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 proteomeImported

External Data

Dasty 3