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L0DYE9

- L0DYE9_THIND

UniProt

L0DYE9 - L0DYE9_THIND

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL [H], cbbL, TVNIR_2992
Organism
Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2)
Status
Unreviewed - 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 sitei116 – 1161Substrate; in homodimeric partner By similarityUniRule annotation
Binding sitei166 – 1661Substrate By similarityUniRule annotation
Active sitei168 – 1681Proton acceptor By similarityUniRule annotation
Binding sitei170 – 1701Substrate By similarityUniRule annotation
Metal bindingi194 – 1941Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi196 – 1961Magnesium By similarityUniRule annotation
Metal bindingi197 – 1971Magnesium By similarityUniRule annotation
Active sitei287 – 2871Proton acceptor By similarityUniRule annotation
Binding sitei288 – 2881Substrate By similarityUniRule annotation
Binding sitei320 – 3201Substrate By similarityUniRule annotation
Sitei327 – 3271Transition state stabilizer By similarityUniRule annotation
Binding sitei372 – 3721Substrate By similarityUniRule 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

LyaseUniRule annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

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:cbbL [H]Imported
Synonyms:cbbLUniRule annotation
Ordered Locus Names:TVNIR_2992Imported
OrganismiThioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2)Imported
Taxonomic identifieri1255043 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeThioalkalivibrio
ProteomesiUP000010809: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941N6-carboxylysine By similarityUniRule annotation

Interactioni

Subunit structurei

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

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK01601.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020888. 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.

Sequencei

Sequence statusi: Complete.

L0DYE9-1 [UniParc]FASTAAdd to Basket

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MAVKTYEAGV KEYREKYWTP DYVPLDTDLL ACFKVTGQPG VPREEVAAAV    50
AAESSTGTWS TVWSELLTDL EYYKGRAYRI EDVPGDKESF YAFVAYPLDL 100
FEEGSIVNVL TSLVGNVFGF KALKHLRLED IRFPIAYIKT CMGPPSGIQV 150
ERDKLNKYGR PMLGATIKPK LGLSAKNYGR AVYECLRGGL DLTKDDENVN 200
SQPFMRWQNR FEFVAEAVMK AQAETGERKG HYLNVTAPDP EQMYERAEFA 250
KELGMPIVMH DFLTGGFTAN TGLAKWCRKN GILLHIHRAM HAVIDRHPKH 300
GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRNSTLGFVD QLREAFVPED 350
RARGVFFDQD WGSMPGVFAV ASGGIHVWHM PALVAIFGDD SVLQFGGGTQ 400
GHPWGNAAGA AANRVALEAC VKARNEGREL EREAREILTD AARHSPELAI 450
AMETWKEIKF EFETVDKLDV G 471
Length:471
Mass (Da):52,430
Last modified:March 6, 2013 - v1
Checksum:iDACF7DFA1BBF5683
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003989 Genomic DNA. Translation: AGA34629.1.
RefSeqiWP_015259737.1. NC_019902.1.
YP_007218110.1. NC_019902.1.

Genome annotation databases

EnsemblBacteriaiAGA34629; AGA34629; TVNIR_2992.
GeneIDi14277757.
KEGGitni:TVNIR_2992.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003989 Genomic DNA. Translation: AGA34629.1 .
RefSeqi WP_015259737.1. NC_019902.1.
YP_007218110.1. NC_019902.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AGA34629 ; AGA34629 ; TVNIR_2992 .
GeneIDi 14277757.
KEGGi tni:TVNIR_2992.

Phylogenomic databases

KOi K01601.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01338. RuBisCO_L_type1.
InterProi 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.
ProtoNeti Search...

Publicationsi

  1. "omplete sequence of Thioalkalivibrio nitratireducens."
    Tikhonova T.V., Pavlov A.R., Beletsky A.V., Mardanov A.V., Sorokin D.Y., Ravin N.V., Popov V.O.
    Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 14787 / UNIQEM 213 / ALEN2.

Entry informationi

Entry nameiL0DYE9_THIND
AccessioniPrimary (citable) accession number: L0DYE9
Entry historyi
Integrated into UniProtKB/TrEMBL: March 6, 2013
Last sequence update: March 6, 2013
Last modified: September 3, 2014
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.UniRule annotation

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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