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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Sideroxydans lithotrophicus (strain ES-1)
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 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

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-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliD5CQ59.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.
OMAiMVSINSI.

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

« Hide

        10         20         30         40         50
MAVKTYNAGV KEYRQTYWTP EYTPLDTDIL ACFKITPQPG VDREEVAAAV
60 70 80 90 100
AAESSTGTWT TVWTDLLTDL DYYKGRAYRI EDVPGDDTCF YAFVAYPIDL
110 120 130 140 150
FEEGSVVNVL TSLVGNVFGF KALRALRLED VRFPIAYVKT CGGPPQGIQV
160 170 180 190 200
ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENVN
210 220 230 240 250
SQPFMRWRDR FEFVHEATLK AERETGERKG HYLNVTAPTP EEMYKRAEFA
260 270 280 290 300
KEIGAPIIMH DYLTGGLTAN TGLANWCRNN GMLLHIHRAM HAVLDRNPHH
310 320 330 340 350
GIHFRVLTKV LRLSGGDHLH SGTVVGKLEG DREATLGWID TMRDEFIKED
360 370 380 390 400
RSRGLFFDQD WGSMPGVLPV ASGGIHVWHM PALVTIFGDD SVLQFGGGTL
410 420 430 440 450
GHPWGNAAGA AANRVALEAC VAARNQGVAV EKEGKSILTE AAKSSPELKI
460 470
AMETWKEIKF EFDTVDKLDV AHK
Length:473
Mass (Da):52,606
Last modified:June 15, 2010 - v1
Checksum:i313B299AE15AF9C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
CP001965 Genomic DNA. Translation: ADE11223.1.
RefSeqiWP_013029121.1. NC_013959.1.
YP_003523610.1. NC_013959.1.

3D structure databases

ProteinModelPortaliD5CQ59.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.
OMAiMVSINSI.

Enzyme and pathway databases

BioCyciSLIT580332:GH9F-1002-MONOMER.

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]
ProtoNetiSearch...

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: February 4, 2015
This is version 29 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

External Data

Dasty 3

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 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.