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P56889

- RBL1_SINMW

UniProt

P56889 - RBL1_SINMW

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Sinorhizobium medicae (strain WSM419) (Ensifer medicae)
Status
Reviewed - 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 sitei126 – 1261Substrate; in homodimeric partnerUniRule annotation
Binding sitei176 – 1761SubstrateUniRule annotation
Active sitei178 – 1781Proton acceptorUniRule annotation
Binding sitei180 – 1801SubstrateUniRule annotation
Metal bindingi204 – 2041Magnesium; via carbamate groupUniRule annotation
Metal bindingi206 – 2061MagnesiumUniRule annotation
Metal bindingi207 – 2071MagnesiumUniRule annotation
Active sitei296 – 2961Proton acceptorUniRule annotation
Binding sitei297 – 2971SubstrateUniRule annotation
Binding sitei329 – 3291SubstrateUniRule annotation
Sitei336 – 3361Transition state stabilizerUniRule annotation
Binding sitei381 – 3811SubstrateUniRule 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

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciSMED366394:GJAL-3985-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:Smed_3924
Encoded oniPlasmid pSMED010 Publication
OrganismiSinorhizobium medicae (strain WSM419) (Ensifer medicae)
Taxonomic identifieri366394 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
ProteomesiUP000001108: Plasmid pSMED01

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 486486Ribulose bisphosphate carboxylase large chainPRO_0000062644Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei204 – 2041N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi366394.Smed_3924.

Structurei

3D structure databases

ProteinModelPortaliP56889.
SMRiP56889. Positions 7-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiCTPLKQA.
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.

P56889-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNADAKTEIK GRERYKAGVL KYAQMGYWNG DYEPKDTDLI ALFRITPQDG
60 70 80 90 100
VDPIEAAAAV AGESSTATWT VVWTDRLTAC DQYRAKAYRV DPVPGTPGQY
110 120 130 140 150
FCYVAYDLIL FEEGSIANLT ASIIGNVFSF KPLKAARLED MRLPVAYVKT
160 170 180 190 200
FKGPPTGIVV ERERLDKFGK PLLGATTKPK LGLSGKNYGR VVYEGLKGGL
210 220 230 240 250
DFMKDDENIN SQPFMHWRDR YLYCMEAVNH ASAVTGEVKG HYLNVTAGTM
260 270 280 290 300
EEMYRRAEFA KELGSVIVMV DLIIGWTAIQ SMSEWCRQND MILHMHRAGH
310 320 330 340 350
GTYTRQKNHG ISFRVIAKWL RLAGVDHLHA GTAVGKLEGD PLTVQGYYNV
360 370 380 390 400
CREMKNAVDL PRGLFFEQDW ADLKKVLPVA SGGIHAGQMH QLLDLFGDDV
410 420 430 440 450
VLQFGGGTIG HPMGIQAGAT ANRVALEAMV LARNEGRDIA HEGPEILRAA
460 470 480
AKWCKPLEAA LDTWGNISFN YTPTDTSDFV PSVTAA
Length:486
Mass (Da):53,709
Last modified:November 13, 2007 - v2
Checksum:iCF54E04F5FD76336
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61K → N in AAF25379. 1 PublicationCurated
Sequence conflicti35 – 351K → N in AAF25379. 1 PublicationCurated
Sequence conflicti52 – 521D → H in AAF25379. 1 PublicationCurated
Sequence conflicti56 – 561A → P in AAF25379. 1 PublicationCurated
Sequence conflicti76 – 761R → P in AAF25379. 1 PublicationCurated
Sequence conflicti128 – 1281F → L in AAF25379. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF211846 Genomic DNA. Translation: AAF25379.1.
CP000739 Genomic DNA. Translation: ABR62734.1.
RefSeqiYP_001312667.1. NC_009620.1.

Genome annotation databases

EnsemblBacteriaiABR62734; ABR62734; Smed_3924.
GeneIDi5318709.
KEGGismd:Smed_3924.
PATRICi23613394. VBISinMed134228_0370.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF211846 Genomic DNA. Translation: AAF25379.1 .
CP000739 Genomic DNA. Translation: ABR62734.1 .
RefSeqi YP_001312667.1. NC_009620.1.

3D structure databases

ProteinModelPortali P56889.
SMRi P56889. Positions 7-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 366394.Smed_3924.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABR62734 ; ABR62734 ; Smed_3924 .
GeneIDi 5318709.
KEGGi smd:Smed_3924.
PATRICi 23613394. VBISinMed134228_0370.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SMED366394:GJAL-3985-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

« Hide 'large scale' publications
  1. "Genetic regulation of C1 metabolism in Sinorhizobium meliloti."
    Fenner B.J., Tiwari R.P., Dilworth M.J.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., Richardson P.
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: WSM419.

Entry informationi

Entry nameiRBL1_SINMW
AccessioniPrimary (citable) accession number: P56889
Secondary accession number(s): A6UGF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 13, 2007
Last modified: October 1, 2014
This is version 84 of the entry and version 2 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".UniRule annotation

Keywords - Technical termi

Complete proteome, Plasmid

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3