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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Thioalkalimicrobium cyclicum (strain DSM 14477 / JCM 11371 / ALM1)
Status
Unreviewed-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)DescriptionActionsGraphical viewLength
Binding sitei116Substrate; in homodimeric partnerUniRule annotation1
Binding sitei166SubstrateUniRule annotation1
Active sitei168Proton acceptorUniRule annotation1
Binding sitei170SubstrateUniRule annotation1
Metal bindingi194Magnesium; via carbamate groupUniRule annotation1
Metal bindingi196MagnesiumUniRule annotation1
Metal bindingi197MagnesiumUniRule annotation1
Active sitei287Proton acceptorUniRule annotation1
Binding sitei288SubstrateUniRule annotation1
Binding sitei320SubstrateUniRule annotation1
Sitei327Transition state stabilizerUniRule annotation1
Binding sitei372SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

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:cbbLUniRule annotation
Ordered Locus Names:Thicy_1565Imported
OrganismiThioalkalimicrobium cyclicum (strain DSM 14477 / JCM 11371 / ALM1)Imported
Taxonomic identifieri717773 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesPiscirickettsiaceaeThioalkalimicrobium
Proteomesi
  • UP000009232 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei194N6-carboxylysineUniRule annotation1
Disulfide bondi240Interchain; in linked formUniRule annotation

Post-translational modificationi

The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.UniRule annotation

Keywords - PTMi

Disulfide bondUniRule annotation

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.UniRule annotation

Protein-protein interaction databases

STRINGi717773.Thicy_1565.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 137RuBisCO_large_NInterPro annotationAdd BLAST122
Domaini147 – 455RuBisCO_largeInterPro annotationAdd BLAST309

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
KOiK01601.
OMAiIAGQELR.
OrthoDBiPOG091H14UZ.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR033966. RuBisCO.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[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.

F6DAZ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANQTFNAGV QDYKLTYWTP DYTPLDTDLL ACFKVIPQAG VPREEAAAAV
60 70 80 90 100
AAESSTGTWT TVWTDLLTDM EFYKGRCYRI EDVPGNKDAF YAFIAYPLDL
110 120 130 140 150
FEEGSVVNVL TSLVGNVFGF KAVRSLRLED IRFPVAFIKT CGGPPSGIQV
160 170 180 190 200
ERDKLNKYGR PMLGCTIKPK LGLSAKNYGR AVYECLRGGL DLTKDDENIN
210 220 230 240 250
SQPFQRWRDR FSFVADAINK AEAETGEVKG HYLNVTAATC EDMMERAEYA
260 270 280 290 300
KELGVRIVMH DFLTGGFTAN TSLANWCRKN GMLLHIHRAM HAVIDRNPNH
310 320 330 340 350
GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRASTLGFVD QLREAFVPED
360 370 380 390 400
RSRGVFFDQD WGSMPGVMAV ASGGIHVWHM PALVTIFGDD SVLQFGGGTQ
410 420 430 440 450
GHPGGNAAGA AANRVALEAC VKARNEGRDL EREGGDILRD AARHSPELAV
460 470
ALETWKEIKF EFDTVDKLDA
Length:470
Mass (Da):51,764
Last modified:July 27, 2011 - v1
Checksum:i9CE28847060ECC49
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002776 Genomic DNA. Translation: AEG32323.1.
RefSeqiWP_013836097.1. NC_015581.1.

Genome annotation databases

EnsemblBacteriaiAEG32323; AEG32323; Thicy_1565.
KEGGitcy:Thicy_1565.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002776 Genomic DNA. Translation: AEG32323.1.
RefSeqiWP_013836097.1. NC_015581.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi717773.Thicy_1565.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAEG32323; AEG32323; Thicy_1565.
KEGGitcy:Thicy_1565.

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
KOiK01601.
OMAiIAGQELR.
OrthoDBiPOG091H14UZ.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR033966. RuBisCO.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiF6DAZ0_THICA
AccessioniPrimary (citable) accession number: F6DAZ0
Entry historyi
Integrated into UniProtKB/TrEMBL: July 27, 2011
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 42 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".UniRule annotation

Keywords - Technical termi

Complete proteomeImported

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 one 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.