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A5FWR1

- RBL_ACICJ

UniProt

A5FWR1 - RBL_ACICJ

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, Acry_0824
Organism
Acidiphilium cryptum (strain JF-5)
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 sitei132 – 1321Substrate; in homodimeric partner By similarity
Binding sitei182 – 1821Substrate By similarity
Active sitei184 – 1841Proton acceptor By similarity
Binding sitei186 – 1861Substrate By similarity
Metal bindingi210 – 2101Magnesium; via carbamate group By similarity
Metal bindingi212 – 2121Magnesium By similarity
Metal bindingi213 – 2131Magnesium By similarity
Active sitei302 – 3021Proton acceptor By similarity
Binding sitei303 – 3031Substrate By similarity
Binding sitei335 – 3351Substrate By similarity
Sitei342 – 3421Transition state stabilizer By similarity
Binding sitei387 – 3871Substrate 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

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

BioCyciACRY349163:GHET-836-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:cbbL
Ordered Locus Names:Acry_0824
OrganismiAcidiphilium cryptum (strain JF-5)
Taxonomic identifieri349163 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium
ProteomesiUP000000245: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 493493Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000355747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei210 – 2101N6-carboxylysine By similarity

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi349163.Acry_0824.

Structurei

3D structure databases

ProteinModelPortaliA5FWR1.
SMRiA5FWR1. Positions 30-473.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
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.

A5FWR1-1 [UniParc]FASTAAdd to Basket

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MDTPTPNITN EALTVRGKER YRSGVLEYRK MGYWEPDYEP KITDVISLFR    50
ITPQDGVDPV EAAAAVAGES STATWTVVWT DRLTACEKYR AKAYRVDPVP 100
NAPGQYFAYI AYDLALFEPG SIANLTASII GNVFGFKPLK ALRLEDMRLP 150
VAYVKTFDGP ATGIVVERER LDKFGRPLLG ATVKPKLGLS GRNYGRVVYE 200
ALKGGLDFTK DDENINSQPF MHWRDRFLYC MEAVNKAQAA TGEVKGTYLN 250
VTAGTMEDMY ERASFAHELG SSIIMIDLVI GYTAIQSMSK WARKHDMILH 300
LHRAGHGTYT RHKTHGVSFR VISKWMRLAG VDHIHAGTVV GKLEGDPLTT 350
RGFYDILRED YNETRYEHGI FFDQDWAGTR KVMPVASGGI HAGQMHQLLH 400
HLGEDVVLQF GGGTIGHPQG IAAGAMANRV ALEAMILARN EGRDYLAEGP 450
QILNDAARHC LPLRQALDTW GEVTFNYAST DTPDFVPTAM PAY 493
Length:493
Mass (Da):54,797
Last modified:June 12, 2007 - v1
Checksum:i8794E5C4AC943AD6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000697 Genomic DNA. Translation: ABQ30043.1.
RefSeqiYP_001233962.1. NC_009484.1.

Genome annotation databases

EnsemblBacteriaiABQ30043; ABQ30043; Acry_0824.
GeneIDi5161365.
KEGGiacr:Acry_0824.
PATRICi20646630. VBIAciCry6074_1312.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000697 Genomic DNA. Translation: ABQ30043.1 .
RefSeqi YP_001233962.1. NC_009484.1.

3D structure databases

ProteinModelPortali A5FWR1.
SMRi A5FWR1. Positions 30-473.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349163.Acry_0824.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ30043 ; ABQ30043 ; Acry_0824 .
GeneIDi 5161365.
KEGGi acr:Acry_0824.
PATRICi 20646630. VBIAciCry6074_1312.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci ACRY349163:GHET-836-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: JF-5.

Entry informationi

Entry nameiRBL_ACICJ
AccessioniPrimary (citable) accession number: A5FWR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: June 12, 2007
Last modified: May 14, 2014
This is version 45 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

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