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F9ZLP0

- F9ZLP0_ACICS

UniProt

F9ZLP0 - F9ZLP0_ACICS

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Protein

Ribulose bisphosphate carboxylase large chain

Gene
cbbL, Atc_0926
Organism
Acidithiobacillus caldus (strain SM-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 sitei115 – 1151Substrate; in homodimeric partner By similarityUniRule annotation
Binding sitei165 – 1651Substrate By similarityUniRule annotation
Active sitei167 – 1671Proton acceptor By similarityUniRule annotation
Binding sitei169 – 1691Substrate By similarityUniRule annotation
Metal bindingi193 – 1931Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi195 – 1951Magnesium By similarityUniRule annotation
Metal bindingi196 – 1961Magnesium By similarityUniRule annotation
Active sitei286 – 2861Proton acceptor By similarityUniRule annotation
Binding sitei287 – 2871Substrate By similarityUniRule annotation
Binding sitei319 – 3191Substrate By similarityUniRule annotation
Sitei326 – 3261Transition state stabilizer By similarityUniRule annotation
Binding sitei371 – 3711Substrate 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 annotation, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciACAL990288:GJBS-941-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:Atc_0926Imported
OrganismiAcidithiobacillus caldus (strain SM-1)Imported
Taxonomic identifieri990288 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus
ProteomesiUP000006135: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei193 – 1931N6-carboxylysine By similarityUniRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliF9ZLP0.

Family & Domainsi

Sequence similaritiesi

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.

F9ZLP0-1 [UniParc]FASTAAdd to Basket

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MAGKYEAGVK EYRHTYWAPD YVPLDSDILA CFKIVPQPGV DREEAAAAVA    50
AESSTGTWTT VWTDLLTDMD YYKGRAYRIE DVPGDDTAFY AFIAYPIDLF 100
EEGSVVNVFT SLVGNVFGFK AVRSLRLEDV RFPLHYVMTC NGPAHGIQVE 150
RDKMDKYGRP LLGCTIKPKL GLSAKNYGRA VYEALRGGLD FTKDDENVNS 200
QPFMRWRDRF LFVADAIRNA EAQTGERKGH YLNVTAPSPE EMYERAEFAK 250
ELGMPIIMHD FLTGGFCANT GLARWCRKNG VLLHIHRAMH AVIDRNPHHG 300
IHFRVLTKAL RLSGGDHLHT GTVVGKLEGD RASTLGWIDL LRESYIPEDR 350
SRGIFFDQDW GSMPGAFAVA SGGIHVWHMP ALVNIFGDDS VLQFGGGTLG 400
HPWGNAAGAA ANRVALEACV EARNRGVEIE KEGKEVLMNA ARHSPELKIA 450
LETWKEIKFE FDTVDKLDVQ NR 472
Length:472
Mass (Da):52,672
Last modified:October 19, 2011 - v1
Checksum:i6B35F9C6839946EE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002573 Genomic DNA. Translation: AEK57575.1.
RefSeqiYP_004748275.1. NC_015850.1.

Genome annotation databases

EnsemblBacteriaiAEK57575; AEK57575; Atc_0926.
GeneIDi10988712.
KEGGiacu:Atc_0926.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002573 Genomic DNA. Translation: AEK57575.1 .
RefSeqi YP_004748275.1. NC_015850.1.

3D structure databases

ProteinModelPortali F9ZLP0.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEK57575 ; AEK57575 ; Atc_0926 .
GeneIDi 10988712.
KEGGi acu:Atc_0926.

Phylogenomic databases

KOi K01601.

Enzyme and pathway databases

BioCyci ACAL990288:GJBS-941-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. "Unraveling the Acidithiobacillus caldus complete genome and its central metabolisms for carbon assimilation."
    You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B., Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.
    J. Genet. Genomics 38:243-252(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SM-1Imported.

Entry informationi

Entry nameiF9ZLP0_ACICS
AccessioniPrimary (citable) accession number: F9ZLP0
Entry historyi
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: June 11, 2014
This is version 16 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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