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F9ZKP6 (F9ZKP6_9PROT) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. 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
ORF Names:NAL212_2942 EMBL ADZ27727.1
OrganismNitrosomonas sp. AL212 [Complete proteome] EMBL ADZ27727.1
Taxonomic identifier153948 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

Protein attributes

Sequence length491 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 site1821Proton acceptor By similarity HAMAP-Rule MF_01338
Active site3001Proton acceptor By similarity HAMAP-Rule MF_01338
Metal binding2081Magnesium; via carbamate group By similarity HAMAP-Rule MF_01338
Metal binding2101Magnesium By similarity HAMAP-Rule MF_01338
Metal binding2111Magnesium By similarity HAMAP-Rule MF_01338
Binding site1301Substrate; in homodimeric partner By similarity HAMAP-Rule MF_01338
Binding site1801Substrate By similarity HAMAP-Rule MF_01338
Binding site1841Substrate By similarity HAMAP-Rule MF_01338
Binding site3011Substrate By similarity HAMAP-Rule MF_01338
Binding site3331Substrate By similarity HAMAP-Rule MF_01338
Binding site3851Substrate By similarity HAMAP-Rule MF_01338
Site3401Transition state stabilizer By similarity HAMAP-Rule MF_01338

Amino acid modifications

Modified residue2081N6-carboxylysine By similarity HAMAP-Rule MF_01338

Sequences

Sequence LengthMass (Da)Tools
F9ZKP6 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: B931FB461D8CAB98

FASTA49154,502
        10         20         30         40         50         60 
MASQTMKEGK ERYKSGVIPY KKMGYWEPAY VPKDTDVIAM FRITPQPGVD HEEAAAAVAG 

        70         80         90        100        110        120 
ESSTATWTVV WTDRLTACEL YRAKAYKSEL VPNTGPGTDN EAQYFAYIAY DIDLFEEGSI 

       130        140        150        160        170        180 
ANLTASIIGN VFGFKAVKAL RLEDMRIPVA YLKTFQGPAT GIVVERERLD KFGRPLLGAT 

       190        200        210        220        230        240 
TKPKLGLSGR NYGRVVYEGL KGGLDFMKDD ENINSQPFMH WRDRFLYCME AVNKASAATG 

       250        260        270        280        290        300 
EVKGHYLNVT AGTMEDMYER AEFAKSLGSV IVMIDLVIGY TAIQSMAKWA RRNDMILHLH 

       310        320        330        340        350        360 
RAGNSTYSRQ KNHGMNFRVI CKWMRMAGVD HIHAGTVVGK LEGDPLMIKG FYDTLRETRT 

       370        380        390        400        410        420 
EKSLEHGLFF DQDWASLNKC MPVASGGIHA GQMHQLIDYL GEDVILQFGG GTIGHPQGIQ 

       430        440        450        460        470        480 
AGAVANRVAL EAMIMARNEG RDYVKEGPQI LADAAKWCTP LKQALDTWKD ITFNYDSTDT 

       490 
ADFVPSTTAN A 

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References

[1]"Complete sequence of chromosome of Nitrosomonas sp. AL212."
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Suwa Y. expand/collapse author list , Klotz M.G., Bollmann A., Stein L.Y., Laanbroek H.J., Arp D.J., Norton J.M., Woyke T.
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: AL212 EMBL ADZ27727.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002552 Genomic DNA. Translation: ADZ27727.1.
RefSeqYP_004295889.1. NC_015222.1.

3D structure databases

ProteinModelPortalF9ZKP6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADZ27727; ADZ27727; NAL212_2942.
GeneID10299483.
KEGGnit:NAL212_2942.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01601.

Enzyme and pathway databases

BioCycNSP153948:GHZ8-2819-MONOMER.

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 nameF9ZKP6_9PROT
AccessionPrimary (citable) accession number: F9ZKP6
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: June 11, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)