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M4IPR8 (M4IPR8_RHIML) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 8. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Ribulose bisphosphate carboxylase large chain HAMAP-Rule MF_01338

Short name=RuBisCO large subunit HAMAP-Rule MF_01338
EC=4.1.1.39 HAMAP-Rule MF_01338
Gene names
Name:cbbL HAMAP-Rule MF_01338
ORF Names:C770_GR4pD1397 EMBL AGA11500.1
Encoded onPlasmid pRmeGR4d Ref.1 EMBL AGA11500.1
OrganismSinorhizobium meliloti GR4 [Complete proteome] EMBL AGA11500.1
Taxonomic identifier1235461 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. 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. HAMAP-Rule MF_01338

Subunit structure

Heterohexadecamer of 8 large chains and 8 small chains By similarity. 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. HAMAP-Rule MF_01338

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1781Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2961Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2041Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2061Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2071Magnesium By similarity HAMAP-Rule MF_01338
Binding site1261Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1761Substrate By similarity HAMAP-Rule MF_01338
Binding site1801Substrate By similarity HAMAP-Rule MF_01338
Binding site2971Substrate By similarity HAMAP-Rule MF_01338
Binding site3291Substrate By similarity HAMAP-Rule MF_01338
Binding site3811Substrate By similarity HAMAP-Rule MF_01338
Site3361Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2041N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
M4IPR8 [UniParc].

Last modified May 29, 2013. Version 1.
Checksum: 4386CA656929EC5F

FASTA48653,791
        10         20         30         40         50         60 
MNADAKTEIK GRERYKAGVL KYAQMGYWNG DYEPKDTDLI ALFRITPQDG VDPIEAAAAV 

        70         80         90        100        110        120 
AGESSTATWT VVWTDRLTAC DQYRAKAYRV DPVPGTPGQY FCYVAYDLIL FEEGSIANLT 

       130        140        150        160        170        180 
ASIIGNVFSF KPLKAARLED MRLPVAYVKT FRGPPTGIVV ERERLDKFGK PLLGATTKPK 

       190        200        210        220        230        240 
LGLSGKNYGR VVYEGLKGGL DFMKDDENIN SQPFMHWRDR YLYCMEAVNH ASAVTGEVKG 

       250        260        270        280        290        300 
HYLNITAGTM EEMYRRAEFA KELGSVIVMV DLIVGWTAIQ SISEWCRQND MILHMHRAGH 

       310        320        330        340        350        360 
GTYTRQKNHG ISFRVIAKWL RLAGVDHLHA GTAVGKLEGD PPTVQGYYNV CREMKNEVDL 

       370        380        390        400        410        420 
PRGLFFEQDW ADLKKVMPVA SGGIHAGQMH QLLDLFGDDV VLQFGGGTIG HPMGIQAGAT 

       430        440        450        460        470        480 
ANRVALEAMV LARNEGRDIA HEGPEILRAA AKWCKPLEAA LDIWGNISFN YTPTDTSDFV 


PSVTAA 

« Hide

References

[1]"Complete genome sequence of the alfalfa symbiont Sinorhizobium/Ensifer meliloti strain GR4."
Martinez-Abarca F., Martinez-Rodriguez L., Lopez-Contreras J.A., Jimenez-Zurdo J.I., Toro N.
Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: GR4 EMBL AGA11500.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003937 Genomic DNA. Translation: AGA11500.1.
RefSeqYP_007195099.1. NC_019849.1.

3D structure databases

ProteinModelPortalM4IPR8.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAGA11500; AGA11500; C770_GR4pD1397.
GeneID14257949.
KEGGsmeg:C770_GR4pD1397.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Family and domain databases

Gene3D3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPMF_01338. RuBisCO_L_type1.
InterProIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameM4IPR8_RHIML
AccessionPrimary (citable) accession number: M4IPR8
Entry history
Integrated into UniProtKB/TrEMBL: May 29, 2013
Last sequence update: May 29, 2013
Last modified: February 19, 2014
This is version 8 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)