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B8GQP8

- RBL_THISH

UniProt

B8GQP8 - RBL_THISH

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Thioalkalivibrio sulfidiphilus (strain HL-EbGR7)
Status
Reviewed - 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

Binds 1 magnesium 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

BioCyciTSUL396588:GH5B-3252-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:Tgr7_3203
OrganismiThioalkalivibrio sulfidiphilus (strain HL-EbGR7)
Taxonomic identifieri396588 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeThioalkalivibrio
ProteomesiUP000002383: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Ribulose bisphosphate carboxylase large chainPRO_1000166263Add
BLAST

Amino acid modifications

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

Proteomic databases

PRIDEiB8GQP8.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi396588.Tgr7_3203.

Structurei

3D structure databases

ProteinModelPortaliB8GQP8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
KOiK01601.
OMAiFTQDWAS.
OrthoDBiEOG6ZKXMS.

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.

B8GQP8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAKKYSAGV KEYRQTYWTP EYVPLDTDLL ACFKITPQPG VDREEAAAAV
60 70 80 90 100
AAESSTGTWT TVWTDLLTDM DYYKGRAYRI EDVPGDDECF YAFIAYPIDL
110 120 130 140 150
FEEGSVVNVF TSLVGNVFGF KAVRALRLED VRFPIAYVKT CGGPPHGIQV
160 170 180 190 200
ERDMMNKYGR PMLGCTIKPK LGLSGKNYGR AVYECLRGGL DFTKDDENIN
210 220 230 240 250
SQPFMRWRQR FDFVMEAIHK AEAETGERKG HYLNVTAPTP EEMYKRAEYA
260 270 280 290 300
KEIGAPIIMH DYITGGFTAN TGLANWCRDN GVLLHIHRAM HAVLDRHPKH
310 320 330 340 350
GIHFRVLAKI LRLSGGDHLH TGTVVGKLEG DRAATLGWID LLREQFVPED
360 370 380 390 400
RSRGIMFDQD WGSMPGVFAV ASGGIHVWHM PALVTIFGDD SVLQFGGGTL
410 420 430 440 450
GHPWGNAAGA HANRVALEAC VQARNEGRDV EREGKEILTA AAAHSPELKI
460 470
AMETWKEIKF EFDTVDKLDV AHK
Length:473
Mass (Da):52,759
Last modified:March 3, 2009 - v1
Checksum:i3B9757752D1DFF12
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001339 Genomic DNA. Translation: ACL74272.1.
RefSeqiYP_002515259.1. NC_011901.1.

Genome annotation databases

EnsemblBacteriaiACL74272; ACL74272; Tgr7_3203.
GeneIDi7315575.
KEGGitgr:Tgr7_3203.
PATRICi23965902. VBIThiSp19295_3168.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001339 Genomic DNA. Translation: ACL74272.1 .
RefSeqi YP_002515259.1. NC_011901.1.

3D structure databases

ProteinModelPortali B8GQP8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 396588.Tgr7_3203.

Proteomic databases

PRIDEi B8GQP8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACL74272 ; ACL74272 ; Tgr7_3203 .
GeneIDi 7315575.
KEGGi tgr:Tgr7_3203.
PATRICi 23965902. VBIThiSp19295_3168.

Phylogenomic databases

eggNOGi COG1850.
KOi K01601.
OMAi FTQDWAS.
OrthoDBi EOG6ZKXMS.

Enzyme and pathway databases

BioCyci TSUL396588:GH5B-3252-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01338. RuBisCO_L_type1.
InterProi IPR020878. RuBisCo_large_chain_AS.
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.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HL-EbGR7.

Entry informationi

Entry nameiRBL_THISH
AccessioniPrimary (citable) accession number: B8GQP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: October 1, 2014
This is version 35 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