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UniProtKB - I3Y991 (I3Y991_THIV6)

UniProt

I3Y991 - I3Y991_THIV6

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Thiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium violascens)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei115 – 1151Substrate; in homodimeric partnerUniRule annotation
Binding sitei165 – 1651SubstrateUniRule annotation
Active sitei167 – 1671Proton acceptorUniRule annotation
Binding sitei169 – 1691SubstrateUniRule annotation
Metal bindingi193 – 1931Magnesium; via carbamate groupUniRule annotation
Metal bindingi195 – 1951MagnesiumUniRule annotation
Metal bindingi196 – 1961MagnesiumUniRule annotation
Active sitei286 – 2861Proton acceptorUniRule annotation
Binding sitei287 – 2871SubstrateUniRule annotation
Binding sitei319 – 3191SubstrateUniRule annotation
Sitei326 – 3261Transition state stabilizerUniRule annotation
Binding sitei371 – 3711SubstrateUniRule annotation

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, PhotosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciTVIO765911:GLMH-1563-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
Ordered Locus Names:Thivi_1570Imported
OrganismiThiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium violascens)Imported
Taxonomic identifieri765911 [NCBI]
Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Chromatiaceae › Thiocystis ›
Proteomesi
  • UP000006062 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei193 – 1931N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliI3Y991.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 136121RuBisCO_large_NInterPro annotationAdd
BLAST
Domaini146 – 454309RuBisCO_largeInterPro annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

KOiK01601.
OMAiFTQDWAS.
OrthoDBiPOG091H14UZ.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_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.

I3Y991-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKTYSAGVK EYRETYWMPD YKPKETDLLA CFKITPQAGV PREEAAAAVA 
        60         70         80         90        100
AESSTGTWTT VWTDLLTDLD HYKGRAYAIE DVPGDDTCYY AFIAYPIDLF 
       110        120        130        140        150
EEGSVVNVFT SLVGNVFGFK AVRALRLEDV RFPIAYVMTC NGPPHGIQVE 
       160        170        180        190        200
RDMMNKYGRP LLGCTIKPKL GLSAKNYGRA VYECLRGGLD FTKDDENVNS 
       210        220        230        240        250
QPFMRWRQRF DFVIDAIDKA ERETGERKGH YLNVTAPTPE EMYKRAEHAK 
       260        270        280        290        300
EIGAPIIMHD YITGGFCANT GLAQWCRDNG MLLHIHRAMH AVLDRNPHHG 
       310        320        330        340        350
IHFRVLAKIL RLSGGDHLHS GTVVGKLEGD REATLGWIDI MRDSFIKEDR 
       360        370        380        390        400
SRGIFFDQDW GSMPGVFPVA SGGIHVWHMP ALVTIFGDDS VLQFGGGTLG 
       410        420        430        440        450
HPWGNAAGAA ANRVALEACV QARNEGVAIE KEGKEVLTNA AKNSPELKVA 
       460        470 
METWKEIKFE FDTVDKLDVA HK
Length:472
Mass (Da):52,594
Last modified:September 5, 2012 - v1
Checksum:i14C66F85CA42A001
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003154 Genomic DNA. Translation: AFL73559.1.
RefSeqiWP_014778025.1. NC_018012.1.

Genome annotation databases

EnsemblBacteriaiAFL73559; AFL73559; Thivi_1570.
KEGGitvi:Thivi_1570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003154 Genomic DNA. Translation: AFL73559.1.
RefSeqiWP_014778025.1. NC_018012.1.

3D structure databases

ProteinModelPortaliI3Y991.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFL73559; AFL73559; Thivi_1570.
KEGGitvi:Thivi_1570.

Phylogenomic databases

KOiK01601.
OMAiFTQDWAS.
OrthoDBiPOG091H14UZ.

Enzyme and pathway databases

BioCyciTVIO765911:GLMH-1563-MONOMER.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_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...

Entry informationi

Entry nameiI3Y991_THIV6
AccessioniPrimary (citable) accession number: I3Y991
Entry historyi
Integrated into UniProtKB/TrEMBL: September 5, 2012
Last sequence update: September 5, 2012
Last modified: September 7, 2016
This is version 28 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 proteome, Reference 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.