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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Nitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
Status
Reviewed-Annotation score: 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

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161Substrate; in homodimeric partnerUniRule annotation
Binding sitei166 – 1661SubstrateUniRule annotation
Active sitei168 – 1681Proton acceptorUniRule annotation
Binding sitei170 – 1701SubstrateUniRule annotation
Metal bindingi194 – 1941Magnesium; via carbamate groupUniRule annotation
Metal bindingi196 – 1961MagnesiumUniRule annotation
Metal bindingi197 – 1971MagnesiumUniRule annotation
Active sitei287 – 2871Proton acceptorUniRule annotation
Binding sitei288 – 2881SubstrateUniRule annotation
Binding sitei320 – 3201SubstrateUniRule annotation
Sitei327 – 3271Transition state stabilizerUniRule annotation
Binding sitei372 – 3721SubstrateUniRule 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

BioCyciNEUR228410:GJNO-1958-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
Synonyms:rbcLUniRule annotation
Ordered Locus Names:NE1921
OrganismiNitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
Taxonomic identifieri228410 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
ProteomesiUP000001416 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Ribulose bisphosphate carboxylase large chainPRO_0000062629Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941N6-carboxylysineUniRule annotation

Proteomic databases

PRIDEiQ82TG6.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi228410.NE1921.

Structurei

3D structure databases

ProteinModelPortaliQ82TG6.
SMRiQ82TG6. Positions 16-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiMVSINSI.
OrthoDBiEOG6ZKXMS.
PhylomeDBiQ82TG6.

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.

Q82TG6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAKTYNAGV KEYRHTYWEP HYNVQDTDIL ACFKIVPQPG VDREEAAAAV
60 70 80 90 100
AAESSTGTWT TVWTDLLTDL DYYKGRSYRI EDVPGDDSSF YAFIAYPIDL
110 120 130 140 150
FEEGSVVNVL TSLTGNVFGF KAVRSLRLED VRFPIAYVKT CGGPPNGIQV
160 170 180 190 200
ERDILNKYGR AYLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENVN
210 220 230 240 250
SQPFMRWRQR FDFVMEAIHK AERETGERKG HYLNVTAPTP EEMFKRAEYA
260 270 280 290 300
KELKAPIIMH DYIAGGFCAN TGLANWCRDN GILLHIHRAM HAVIDRNPHH
310 320 330 340 350
GIHFRVLAKM LRLSGGDHLH SGTVVGKLEG DREATLGWID IMRDSFIKED
360 370 380 390 400
RSRGIMFDQD WGSMPGVVPV ASGGIHVWHM PALVTIFGDD ACLQFGGGTL
410 420 430 440 450
GHPWGNAAGA AANRVALEAC VEARNRGVPI EKEGKAILTE AAKHSPELKI
460 470
AMETWKEIKF EFDTVDKLDV AHK
Length:473
Mass (Da):52,799
Last modified:June 1, 2003 - v1
Checksum:i911B9F731A66EE41
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL954747 Genomic DNA. Translation: CAD85832.1.
RefSeqiNP_841943.1. NC_004757.1.

Genome annotation databases

EnsemblBacteriaiCAD85832; CAD85832; NE1921.
KEGGineu:NE1921.
PATRICi22715143. VBINitEur56163_2157.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL954747 Genomic DNA. Translation: CAD85832.1.
RefSeqiNP_841943.1. NC_004757.1.

3D structure databases

ProteinModelPortaliQ82TG6.
SMRiQ82TG6. Positions 16-460.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi228410.NE1921.

Proteomic databases

PRIDEiQ82TG6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAD85832; CAD85832; NE1921.
KEGGineu:NE1921.
PATRICi22715143. VBINitEur56163_2157.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiMVSINSI.
OrthoDBiEOG6ZKXMS.
PhylomeDBiQ82TG6.

Enzyme and pathway databases

BioCyciNEUR228410:GJNO-1958-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea."
    Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.
    J. Bacteriol. 185:2759-2773(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 19718 / NBRC 14298.

Entry informationi

Entry nameiRBL_NITEU
AccessioniPrimary (citable) accession number: Q82TG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: June 1, 2003
Last modified: April 1, 2015
This is version 78 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".UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.