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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / AIU301)
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 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

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

BioCyciAMUL926570:GI8V-1104-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 annotationImported
Ordered Locus Names:ACMV_10890Imported
OrganismiAcidiphilium multivorum (strain DSM 11245 / JCM 8867 / AIU301)Imported
Taxonomic identifieri926570 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium
ProteomesiUP000007100: Chromosome

PTM / Processingi

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

Structurei

3D structure databases

ProteinModelPortaliF0IX26.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

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.

F0IX26-1 [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 STIIMIDLVI 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 DTPDFAPTAM PAY
Length:493
Mass (Da):54,783
Last modified:May 3, 2011 - v1
Checksum:iF3AEA66096D65998
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP012035 Genomic DNA. Translation: BAJ80436.1.
RefSeqiWP_013639783.1. NC_015186.1.
YP_004283318.1. NC_015186.1.

Genome annotation databases

EnsemblBacteriaiBAJ80436; BAJ80436; ACMV_10890.
GeneIDi10320528.
KEGGiamv:ACMV_10890.
PATRICi46810953. VBIAciMul178205_1458.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP012035 Genomic DNA. Translation: BAJ80436.1.
RefSeqiWP_013639783.1. NC_015186.1.
YP_004283318.1. NC_015186.1.

3D structure databases

ProteinModelPortaliF0IX26.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAJ80436; BAJ80436; ACMV_10890.
GeneIDi10320528.
KEGGiamv:ACMV_10890.
PATRICi46810953. VBIAciMul178205_1458.

Phylogenomic databases

KOiK01601.

Enzyme and pathway databases

BioCyciAMUL926570:GI8V-1104-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. "Whole genome sequence of Acidiphilium multivorum AIU301."
    Narita-Yamada S., Nakamura S., Ito N., Takarada H., Katano Y., Nakazawa H., Hosoyama A., Yamada R., Fujita N.
    Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 11245 / JCM 8867 / AIU301Imported.

Entry informationi

Entry nameiF0IX26_ACIMA
AccessioniPrimary (citable) accession number: F0IX26
Entry historyi
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: February 4, 2015
This is version 26 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 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.