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D5CQ59

- D5CQ59_SIDLE

UniProt

D5CQ59 - D5CQ59_SIDLE

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, Slit_0985
Organism
Sideroxydans lithotrophicus (strain ES-1)
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 annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciSLIT580332:GH9F-1002-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:Slit_0985Imported
OrganismiSideroxydans lithotrophicus (strain ES-1)Imported
Taxonomic identifieri580332 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaGallionellalesGallionellaceaeSideroxydans
ProteomesiUP000001625: 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

ProteinModelPortaliD5CQ59.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.

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.

D5CQ59-1 [UniParc]FASTAAdd to Basket

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MAVKTYNAGV KEYRQTYWTP EYTPLDTDIL ACFKITPQPG VDREEVAAAV    50
AAESSTGTWT TVWTDLLTDL DYYKGRAYRI EDVPGDDTCF YAFVAYPIDL 100
FEEGSVVNVL TSLVGNVFGF KALRALRLED VRFPIAYVKT CGGPPQGIQV 150
ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENVN 200
SQPFMRWRDR FEFVHEATLK AERETGERKG HYLNVTAPTP EEMYKRAEFA 250
KEIGAPIIMH DYLTGGLTAN TGLANWCRNN GMLLHIHRAM HAVLDRNPHH 300
GIHFRVLTKV LRLSGGDHLH SGTVVGKLEG DREATLGWID TMRDEFIKED 350
RSRGLFFDQD WGSMPGVLPV ASGGIHVWHM PALVTIFGDD SVLQFGGGTL 400
GHPWGNAAGA AANRVALEAC VAARNQGVAV EKEGKSILTE AAKSSPELKI 450
AMETWKEIKF EFDTVDKLDV AHK 473
Length:473
Mass (Da):52,606
Last modified:June 15, 2010 - v1
Checksum:i313B299AE15AF9C3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001965 Genomic DNA. Translation: ADE11223.1.
RefSeqiWP_013029121.1. NC_013959.1.
YP_003523610.1. NC_013959.1.

Genome annotation databases

EnsemblBacteriaiADE11223; ADE11223; Slit_0985.
GeneIDi8891657.
KEGGislt:Slit_0985.
PATRICi35400070. VBISidLit69165_0978.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001965 Genomic DNA. Translation: ADE11223.1 .
RefSeqi WP_013029121.1. NC_013959.1.
YP_003523610.1. NC_013959.1.

3D structure databases

ProteinModelPortali D5CQ59.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADE11223 ; ADE11223 ; Slit_0985 .
GeneIDi 8891657.
KEGGi slt:Slit_0985.
PATRICi 35400070. VBISidLit69165_0978.

Phylogenomic databases

HOGENOMi HOG000230831.
KOi K01601.

Enzyme and pathway databases

BioCyci SLIT580332:GH9F-1002-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. "Complete sequence of Sideroxydans lithotrophicus ES-1."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.
    Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ES-1Imported.

Entry informationi

Entry nameiD5CQ59_SIDLE
AccessioniPrimary (citable) accession number: D5CQ59
Entry historyi
Integrated into UniProtKB/TrEMBL: June 15, 2010
Last sequence update: June 15, 2010
Last modified: September 3, 2014
This is version 24 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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