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A5FWR1

- RBL_ACICJ

UniProt

A5FWR1 - RBL_ACICJ

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

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.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 sitei132 – 1321Substrate; in homodimeric partnerUniRule annotation
Binding sitei182 – 1821SubstrateUniRule annotation
Active sitei184 – 1841Proton acceptorUniRule annotation
Binding sitei186 – 1861SubstrateUniRule annotation
Metal bindingi210 – 2101Magnesium; via carbamate groupUniRule annotation
Metal bindingi212 – 2121MagnesiumUniRule annotation
Metal bindingi213 – 2131MagnesiumUniRule annotation
Active sitei302 – 3021Proton acceptorUniRule annotation
Binding sitei303 – 3031SubstrateUniRule annotation
Binding sitei335 – 3351SubstrateUniRule annotation
Sitei342 – 3421Transition state stabilizerUniRule annotation
Binding sitei387 – 3871SubstrateUniRule 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

BioCyciACRY349163:GHET-836-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: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 chainPRO_0000355747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei210 – 2101N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi349163.Acry_0824.

Structurei

3D structure databases

ProteinModelPortaliA5FWR1.
SMRiA5FWR1. Positions 30-473.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

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

« Hide

        10         20         30         40         50
MDTPTPNITN EALTVRGKER YRSGVLEYRK MGYWEPDYEP KITDVISLFR
60 70 80 90 100
ITPQDGVDPV EAAAAVAGES STATWTVVWT DRLTACEKYR AKAYRVDPVP
110 120 130 140 150
NAPGQYFAYI AYDLALFEPG SIANLTASII GNVFGFKPLK ALRLEDMRLP
160 170 180 190 200
VAYVKTFDGP ATGIVVERER LDKFGRPLLG ATVKPKLGLS GRNYGRVVYE
210 220 230 240 250
ALKGGLDFTK DDENINSQPF MHWRDRFLYC MEAVNKAQAA TGEVKGTYLN
260 270 280 290 300
VTAGTMEDMY ERASFAHELG SSIIMIDLVI GYTAIQSMSK WARKHDMILH
310 320 330 340 350
LHRAGHGTYT RHKTHGVSFR VISKWMRLAG VDHIHAGTVV GKLEGDPLTT
360 370 380 390 400
RGFYDILRED YNETRYEHGI FFDQDWAGTR KVMPVASGGI HAGQMHQLLH
410 420 430 440 450
HLGEDVVLQF GGGTIGHPQG IAAGAMANRV ALEAMILARN EGRDYLAEGP
460 470 480 490
QILNDAARHC LPLRQALDTW GEVTFNYAST DTPDFVPTAM PAY
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: October 1, 2014
This is version 46 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