SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q2YB78

- RBL_NITMU

UniProt

Q2YB78 - RBL_NITMU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, Nmul_A0686
Organism
Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849)
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 By similarity.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 By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei128 – 1281Substrate; in homodimeric partner By similarity
Binding sitei178 – 1781Substrate By similarity
Active sitei180 – 1801Proton acceptor By similarity
Binding sitei182 – 1821Substrate By similarity
Metal bindingi206 – 2061Magnesium; via carbamate group By similarity
Metal bindingi208 – 2081Magnesium By similarity
Metal bindingi209 – 2091Magnesium By similarity
Active sitei298 – 2981Proton acceptor By similarity
Binding sitei299 – 2991Substrate By similarity
Binding sitei331 – 3311Substrate By similarity
Sitei338 – 3381Transition state stabilizer By similarity
Binding sitei383 – 3831Substrate By similarity

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

BioCyciNMUL323848:GKEC-703-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:cbbL
Ordered Locus Names:Nmul_A0686
OrganismiNitrosospira multiformis (strain ATCC 25196 / NCIMB 11849)
Taxonomic identifieri323848 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosospira
ProteomesiUP000002718: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 489489Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000251449Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei206 – 2061N6-carboxylysine By similarity

Proteomic databases

PRIDEiQ2YB78.

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains By similarity.

Protein-protein interaction databases

STRINGi323848.Nmul_A0686.

Structurei

3D structure databases

ProteinModelPortaliQ2YB78.
SMRiQ2YB78. Positions 10-482.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
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.

Q2YB78-1 [UniParc]FASTAAdd to Basket

« Hide

MSEAITGAER YKSGVIPYKK MGYWEPDYVP KDTDIIAMFR ITPQAGVEPE    50
EAAAAVAGES STATWTVVWT DRLTACELYR AKAFRTDPVP NTGEGTKTEQ 100
QYFAYIAYDL DLFEPGSIAN LTASIIGNVF GFKAVKALRL EDMRIPVAYL 150
KTFQGPATGI IVERERLDKF GRPLLGATTK PKLGLSGRNY GRVVYEGLKG 200
GLDFMKDDEN INSQPFMHWR DRFLYCMEAV NKASAATGEV KGHYLNVTAG 250
TMEEMYERAE FAKSLGSVII MIDLVIGYTA IQSMAKWARK NDMILHLHRA 300
GNSTYSRQKN HGMNFRVICK WMRMAGVDHI HAGTVVGKLE GDPLMIKGFY 350
DTLRDRHTPV SLEHGLFFEQ DWASLNKVMP VASGGIHAGQ MHQLLDYLGE 400
DVILQFGGGT IGHPQGIQAG AVANRVALEA MIMARNEGRD YVKEGPQILE 450
EAAKWCTPLK LALDTWKDIT FNYESTDTAD FVPSETASV 489
Length:489
Mass (Da):54,315
Last modified:December 20, 2005 - v1
Checksum:i02CFEB7C9D0C2523
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000103 Genomic DNA. Translation: ABB73993.1.
RefSeqiYP_411385.1. NC_007614.1.

Genome annotation databases

EnsemblBacteriaiABB73993; ABB73993; Nmul_A0686.
GeneIDi3784063.
KEGGinmu:Nmul_A0686.
PATRICi22724432. VBINitMul110821_0791.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000103 Genomic DNA. Translation: ABB73993.1 .
RefSeqi YP_411385.1. NC_007614.1.

3D structure databases

ProteinModelPortali Q2YB78.
SMRi Q2YB78. Positions 10-482.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 323848.Nmul_A0686.

Proteomic databases

PRIDEi Q2YB78.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB73993 ; ABB73993 ; Nmul_A0686 .
GeneIDi 3784063.
KEGGi nmu:Nmul_A0686.
PATRICi 22724432. VBINitMul110821_0791.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci NMUL323848:GKEC-703-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 1 of Nitrosospira multiformis ATCC 25196."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25196 / NCIMB 11849.

Entry informationi

Entry nameiRBL_NITMU
AccessioniPrimary (citable) accession number: Q2YB78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: December 20, 2005
Last modified: May 14, 2014
This is version 55 of the entry and version 1 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" By similarity.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi