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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Binding sitei116Substrate; in homodimeric partnerUniRule annotation1
Binding sitei166SubstrateUniRule annotation1
Active sitei168Proton acceptorUniRule annotation1
Binding sitei170SubstrateUniRule annotation1
Metal bindingi194Magnesium; via carbamate groupUniRule annotation1
Metal bindingi196MagnesiumUniRule annotation1
Metal bindingi197MagnesiumUniRule annotation1
Active sitei287Proton acceptorUniRule annotation1
Binding sitei288SubstrateUniRule annotation1
Binding sitei320SubstrateUniRule annotation1
Sitei327Transition state stabilizerUniRule annotation1
Binding sitei372SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

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

BioCyciHNEA555778:GIVV-951-MONOMER.
BRENDAi4.1.1.39. 6349.

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:Hneap_0922
OrganismiHalothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
Taxonomic identifieri555778 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesHalothiobacillaceaeHalothiobacillus
Proteomesi
  • UP000009102 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000626601 – 473Ribulose bisphosphate carboxylase large chainAdd BLAST473

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei194N6-carboxylysineUniRule annotation1

Expressioni

Inductioni

Produced when grown in air or in air supplemented with 5% CO2.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi555778.Hneap_0922.

Structurei

Secondary structure

1473
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 37Combined sources10
Helixi43 – 53Combined sources11
Turni54 – 56Combined sources3
Helixi63 – 67Combined sources5
Turni70 – 72Combined sources3
Beta strandi76 – 83Combined sources8
Beta strandi86 – 96Combined sources11
Helixi98 – 100Combined sources3
Helixi106 – 114Combined sources9
Helixi117 – 119Combined sources3
Beta strandi123 – 132Combined sources10
Helixi135 – 138Combined sources4
Helixi148 – 155Combined sources8
Beta strandi162 – 166Combined sources5
Beta strandi170 – 172Combined sources3
Helixi175 – 187Combined sources13
Beta strandi191 – 194Combined sources4
Beta strandi200 – 202Combined sources3
Helixi207 – 225Combined sources19
Beta strandi230 – 234Combined sources5
Helixi240 – 253Combined sources14
Beta strandi257 – 261Combined sources5
Turni262 – 265Combined sources4
Helixi267 – 280Combined sources14
Beta strandi283 – 287Combined sources5
Helixi291 – 295Combined sources5
Beta strandi300 – 302Combined sources3
Helixi304 – 314Combined sources11
Beta strandi317 – 320Combined sources4
Helixi329 – 331Combined sources3
Helixi333 – 343Combined sources11
Beta strandi345 – 347Combined sources3
Helixi351 – 353Combined sources3
Beta strandi368 – 374Combined sources7
Helixi377 – 379Combined sources3
Helixi380 – 387Combined sources8
Beta strandi389 – 394Combined sources6
Helixi397 – 400Combined sources4
Helixi406 – 425Combined sources20
Turni430 – 433Combined sources4
Helixi434 – 442Combined sources9
Helixi446 – 455Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SVDX-ray1.80A1-473[»]
ProteinModelPortaliO85040.
SMRiO85040.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO85040.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
OrthoDBiPOG091H14UZ.

Family and domain databases

CDDicd08212. RuBisCO_large_I. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[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.

O85040-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVKKYSAGV KEYRQTYWMP EYTPLDSDIL ACFKITPQPG VDREEAAAAV
60 70 80 90 100
AAESSTGTWT TVWTDLLTDM DYYKGRAYRI EDVPGDDAAF YAFIAYPIDL
110 120 130 140 150
FEEGSVVNVF TSLVGNVFGF KAVRGLRLED VRFPLAYVKT CGGPPHGIQV
160 170 180 190 200
ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENIN
210 220 230 240 250
SQPFMRWRDR FLFVQDATET AEAQTGERKG HYLNVTAPTP EEMYKRAEFA
260 270 280 290 300
KEIGAPIIMH DYITGGFTAN TGLAKWCQDN GVLLHIHRAM HAVIDRNPNH
310 320 330 340 350
GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESFIPED
360 370 380 390 400
RSRGIFFDQD WGSMPGVFAV ASGGIHVWHM PALVNIFGDD SVLQFGGGTL
410 420 430 440 450
GHPWGNAAGA AANRVALEAC VEARNQGRDI EKEGKEILTA AAQHSPELKI
460 470
AMETWKEIKF EFDTVDKLDT QNR
Length:473
Mass (Da):52,636
Last modified:November 1, 1998 - v1
Checksum:iB84D2EDE46CAF7D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038430 Genomic DNA. Translation: AAC32549.1.
CP001801 Genomic DNA. Translation: ACX95765.1.
RefSeqiWP_012823801.1. NC_013422.1.

Genome annotation databases

EnsemblBacteriaiACX95765; ACX95765; Hneap_0922.
KEGGihna:Hneap_0922.
PATRICi32205718. VBIHalNea120669_0941.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038430 Genomic DNA. Translation: AAC32549.1.
CP001801 Genomic DNA. Translation: ACX95765.1.
RefSeqiWP_012823801.1. NC_013422.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SVDX-ray1.80A1-473[»]
ProteinModelPortaliO85040.
SMRiO85040.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi555778.Hneap_0922.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACX95765; ACX95765; Hneap_0922.
KEGGihna:Hneap_0922.
PATRICi32205718. VBIHalNea120669_0941.

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
OrthoDBiPOG091H14UZ.

Enzyme and pathway databases

BioCyciHNEA555778:GIVV-951-MONOMER.
BRENDAi4.1.1.39. 6349.

Miscellaneous databases

EvolutionaryTraceiO85040.

Family and domain databases

CDDicd08212. RuBisCO_large_I. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[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...

Entry informationi

Entry nameiRBL1_HALNC
AccessioniPrimary (citable) accession number: O85040
Secondary accession number(s): D0KZ92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 1, 1998
Last modified: November 30, 2016
This is version 89 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.