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Q31HD9

- RBL1B_THICR

UniProt

Q31HD9 - RBL1B_THICR

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Protein
Ribulose bisphosphate carboxylase large chain 2
Gene
cbbL2, Tcr_0838
Organism
Thiomicrospira crunogena (strain XCL-2)
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 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 similarity
Binding sitei166 – 1661Substrate By similarity
Active sitei168 – 1681Proton acceptor By similarity
Binding sitei170 – 1701Substrate By similarity
Metal bindingi194 – 1941Magnesium; via carbamate group By similarity
Metal bindingi196 – 1961Magnesium By similarity
Metal bindingi197 – 1971Magnesium By similarity
Active sitei287 – 2871Proton acceptor By similarity
Binding sitei288 – 2881Substrate By similarity
Binding sitei320 – 3201Substrate By similarity
Sitei327 – 3271Transition state stabilizer By similarity
Binding sitei372 – 3721Substrate By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP
Complete GO annotation...

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

BioCyciTCRU317025:GHE8-857-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain 2 (EC:4.1.1.39)
Short name:
RuBisCO large subunit 2
Gene namesi
Name:cbbL2
Ordered Locus Names:Tcr_0838
OrganismiThiomicrospira crunogena (strain XCL-2)
Taxonomic identifieri317025 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesPiscirickettsiaceaeThiomicrospira
ProteomesiUP000002713: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471Ribulose bisphosphate carboxylase large chain 2UniRule annotation
PRO_0000251467Add
BLAST

Amino acid modifications

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

Proteomic databases

PRIDEiQ31HD9.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi317025.Tcr_0838.

Structurei

3D structure databases

ProteinModelPortaliQ31HD9.
SMRiQ31HD9. Positions 16-460.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiIGNDIST.
OrthoDBiEOG6ZKXMS.

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.

Q31HD9-1 [UniParc]FASTAAdd to Basket

« Hide

MASKTFDAGV QDYQLTYWTP DYTPLDTDLL ACFKVVPQDG VPREEAAAAV    50
AAESSTGTWT TVWTDLLTDM EFYKGRCYRI EDVPGDKNAF YAFIAYPLDL 100
FEEGSVVNVL TSLVGNVFGF KAVRSLRLED LRFPIAFIKT CGGPPAGIQV 150
ERDKLNKYGR PMLGCTIKPK LGLSAKNYGR AVYECLRGGL DLTKDDENIN 200
SQPFQRWQNR FEFVADAVDK ATAETGERKG HYLNVTAGTV EEMMKRAEFA 250
KELGQPIIMH DFLTAGFTAN TTLANWCRDN GMLLHIHRAM HAVIDRNPNH 300
GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRASTLGFVD QLREAFVPED 350
RSRGVFFDQD WGSMPGVMAV ASGGIHVWHM PALVNIFGDD SVLQFGGGTQ 400
GHPGGNAAGA AANRVALEAC VKARNEGRDL EREGGDILRD AARNSKELAV 450
ALDTWKEIKF EFDTVDKLDV G 471
Length:471
Mass (Da):51,865
Last modified:December 6, 2005 - v1
Checksum:i3568693BCFA7BBDD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000109 Genomic DNA. Translation: ABB41434.1.
RefSeqiYP_391108.1. NC_007520.2.

Genome annotation databases

EnsemblBacteriaiABB41434; ABB41434; Tcr_0838.
GeneIDi3760532.
KEGGitcx:Tcr_0838.
PATRICi23973632. VBIThiCru83387_0873.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000109 Genomic DNA. Translation: ABB41434.1 .
RefSeqi YP_391108.1. NC_007520.2.

3D structure databases

ProteinModelPortali Q31HD9.
SMRi Q31HD9. Positions 16-460.
ModBasei Search...

Protein-protein interaction databases

STRINGi 317025.Tcr_0838.

Proteomic databases

PRIDEi Q31HD9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB41434 ; ABB41434 ; Tcr_0838 .
GeneIDi 3760532.
KEGGi tcx:Tcr_0838.
PATRICi 23973632. VBIThiCru83387_0873.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi IGNDIST.
OrthoDBi EOG6ZKXMS.

Enzyme and pathway databases

BioCyci TCRU317025:GHE8-857-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 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: XCL-2.

Entry informationi

Entry nameiRBL1B_THICR
AccessioniPrimary (citable) accession number: Q31HD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: December 6, 2005
Last modified: May 14, 2014
This is version 59 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" By similarity.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi