Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

F9ZLP0

- F9ZLP0_ACICS

UniProt

F9ZLP0 - F9ZLP0_ACICS

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

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.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

Note: Binds 1 magnesium ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei115 – 1151Substrate; in homodimeric partnerUniRule annotation
Binding sitei165 – 1651SubstrateUniRule annotation
Active sitei167 – 1671Proton acceptorUniRule annotation
Binding sitei169 – 1691SubstrateUniRule annotation
Metal bindingi193 – 1931Magnesium; via carbamate groupUniRule annotation
Metal bindingi195 – 1951MagnesiumUniRule annotation
Metal bindingi196 – 1961MagnesiumUniRule annotation
Active sitei286 – 2861Proton acceptorUniRule annotation
Binding sitei287 – 2871SubstrateUniRule annotation
Binding sitei319 – 3191SubstrateUniRule annotation
Sitei326 – 3261Transition state stabilizerUniRule annotation
Binding sitei371 – 3711SubstrateUniRule 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-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliF9ZLP0.
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.

F9ZLP0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGKYEAGVK EYRHTYWAPD YVPLDSDILA CFKIVPQPGV DREEAAAAVA
60 70 80 90 100
AESSTGTWTT VWTDLLTDMD YYKGRAYRIE DVPGDDTAFY AFIAYPIDLF
110 120 130 140 150
EEGSVVNVFT SLVGNVFGFK AVRSLRLEDV RFPLHYVMTC NGPAHGIQVE
160 170 180 190 200
RDKMDKYGRP LLGCTIKPKL GLSAKNYGRA VYEALRGGLD FTKDDENVNS
210 220 230 240 250
QPFMRWRDRF LFVADAIRNA EAQTGERKGH YLNVTAPSPE EMYERAEFAK
260 270 280 290 300
ELGMPIIMHD FLTGGFCANT GLARWCRKNG VLLHIHRAMH AVIDRNPHHG
310 320 330 340 350
IHFRVLTKAL RLSGGDHLHT GTVVGKLEGD RASTLGWIDL LRESYIPEDR
360 370 380 390 400
SRGIFFDQDW GSMPGAFAVA SGGIHVWHMP ALVNIFGDDS VLQFGGGTLG
410 420 430 440 450
HPWGNAAGAA ANRVALEACV EARNRGVEIE KEGKEVLMNA ARHSPELKIA
460 470
LETWKEIKFE FDTVDKLDVQ NR
Length:472
Mass (Da):52,672
Last modified:October 19, 2011 - v1
Checksum:i6B35F9C6839946EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 19 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