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D5MHI3 (D5MHI3_9BACT) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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 EMBL CBE69215.1
ORF Names:DAMO_2165 EMBL CBE69215.1
OrganismCandidatus Methylomirabilis oxyfera EMBL CBE69215.1
Taxonomic identifier671143 [NCBI]
Taxonomic lineageBacteria › candidate division NC10 › Candidatus Methylomirabilis

Protein attributes

Sequence length487 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 site1791Proton acceptor By similarity HAMAP-Rule MF_01338
Active site2971Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2051Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2071Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2081Magnesium By similarity HAMAP-Rule MF_01338
Binding site1271Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1771Substrate By similarity HAMAP-Rule MF_01338
Binding site1811Substrate By similarity HAMAP-Rule MF_01338
Binding site2981Substrate By similarity HAMAP-Rule MF_01338
Binding site3301Substrate By similarity HAMAP-Rule MF_01338
Binding site3821Substrate By similarity HAMAP-Rule MF_01338
Site3371Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2051N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
D5MHI3 [UniParc].

Last modified June 15, 2010. Version 1.
Checksum: 0573994987187B54

FASTA48753,978
        10         20         30         40         50         60 
MAGAAGTSKD PKDRYKAGGV VPYKQMGYWR PEYEPKDTDV IAVFRITPQE GVDPDEAAAA 

        70         80         90        100        110        120 
VAGESSTATW TVVWTDRLTD HDAYRGKAYR VDPVPGSPGQ YFAYIAYDLD LFEDGSIVNV 

       130        140        150        160        170        180 
SASIIGNVFG FKPLKALRLE DMRFPVAYLK TFQGPPTGIV VERERLDKFG RPLLGATIKP 

       190        200        210        220        230        240 
KLGLSGKNYG RVVYEALKGG LDFTKDDENI NSQAFMHWRD RFLFAMEGVN RASAATGEVK 

       250        260        270        280        290        300 
GHYLNISAGT MEDMYERAEF AKELGSVIIM IDLVIGYTAI QSISKWARKN DMMLHLHRAG 

       310        320        330        340        350        360 
HSTYTRQKTH GVNFRVICKW MRMAGVDHIH AGTVIGKLEG DPYMVKGFYD TLRETHTPMN 

       370        380        390        400        410        420 
LQNGLFFDQD WASLRKVMPV ASGGIHAGQM HQLLHYFGED VVMQFGGGTI GHPTGIAAGA 

       430        440        450        460        470        480 
TANRVALEAM VQARNEGRDY FNEGPEILAN AARWCQPLRT ALEVWKDITF NYASTDTADF 


VPTTTAV

« Hide

References

[1]Genoscope - CEA
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Nitrite-driven anaerobic methane oxidation by oxygenic bacteria."
Ettwig K.F., Butler M.K., Le Paslier D., Pelletier E., Mangenot S., Kuypers M.M.M., Schreiber F., Dutilh B.E., Zedelius J., de Beer D., Gloerich J., Wessels H.J.C.T., van Allen T., Luesken F., Wu M., van de Pas-Schoonen K.T., Op den Camp H.J.M., Janssen-Megens E.M. expand/collapse author list , Francoijs K-J., Stunnenberg H., Weissenbach J., Jetten M.S.M., Strous M.
Nature 464:543-548(2010)
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FP565575 Genomic DNA. Translation: CBE69215.1.
RefSeqYP_003207046.1. NC_013260.1.

3D structure databases

ProteinModelPortalD5MHI3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID13097391.
KEGGmox:DAMO_2165.

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. RuBisCO_large. 1 hit.
SSF54966. RuBisCO_large. 1 hit.
PROSITEPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD5MHI3_9BACT
AccessionPrimary (citable) accession number: D5MHI3
Entry history
Integrated into UniProtKB/TrEMBL: June 15, 2010
Last sequence update: June 15, 2010
Last modified: May 1, 2013
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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