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L0H228

- L0H228_9GAMM

UniProt

L0H228 - L0H228_9GAMM

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Protein

Ribulose bisphosphate carboxylase large chain

Gene
cbbL, Thimo_2947
Organism
Thioflavicoccus mobilis 8321
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 annotation, 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:cbbLUniRule annotation
ORF Names:Thimo_2947Imported
OrganismiThioflavicoccus mobilis 8321Imported
Taxonomic identifieri765912 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeThioflavicoccus
ProteomesiUP000010816: 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

Structurei

3D structure databases

ProteinModelPortaliL0H228.

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.

L0H228-1 [UniParc]FASTAAdd to Basket

« Hide

MAAKTYDAGV KEYRDMYWTP EYVPLDTDLL ACFKCTGQPG VPREEVAAAV    50
AAESSTGTWS TVWSELLTDL EYYKGRAYRI EDVPGDKESF YAFVAYPIDL 100
FEEGSVVNVL TSLVGNVFGF KALRHLRLED IRFPIAYIKT CNGPPAGIQV 150
ERDRLNKYAR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DLTKDDENVN 200
SQPFMRWRDR FEFVGEAIQK SQQETGERKG HYLNVTAPDP EQMYERAEFA 250
KEVGCPIIMH DFLTGGFTAN TGLAKWCRKN GMLLHIHRAM HAVIDRHPKH 300
GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRASTLGYVD QLRESFVPED 350
RSRGVFFDQD WGSMPGVFAV ASGGIHVWHM PALVTIFGDD SVLQFGGGTQ 400
GHPWGNAAGA AANRVALEAC IKARNQGRGL EKESRDILTE AARHSPELAM 450
AMETWKEIKF EFETVDKLDV A 471
Length:471
Mass (Da):52,517
Last modified:March 6, 2013 - v1
Checksum:i88447B6AE24F2CFC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003051 Genomic DNA. Translation: AGA91639.1.
RefSeqiYP_007245269.1. NC_019940.1.

Genome annotation databases

EnsemblBacteriaiAGA91639; AGA91639; Thimo_2947.
GeneIDi14305208.
KEGGitmb:Thimo_2947.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003051 Genomic DNA. Translation: AGA91639.1 .
RefSeqi YP_007245269.1. NC_019940.1.

3D structure databases

ProteinModelPortali L0H228.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AGA91639 ; AGA91639 ; Thimo_2947 .
GeneIDi 14305208.
KEGGi tmb:Thimo_2947.

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. "Complete sequence of chromosome of Thioflavicoccus mobilis 8321."
    US DOE Joint Genome Institute
    Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K.
    , Liu Z., Imhoff J., Thiel V., Frigaard N.-U., Bryant D., Woyke T.
    Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 8321Imported.

Entry informationi

Entry nameiL0H228_9GAMM
AccessioniPrimary (citable) accession number: L0H228
Entry historyi
Integrated into UniProtKB/TrEMBL: March 6, 2013
Last sequence update: March 6, 2013
Last modified: June 11, 2014
This is version 9 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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