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O85040

- RBL1_HALNC

UniProt

O85040 - RBL1_HALNC

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, Hneap_0922
Organism
Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
Status
Reviewed - 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 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 sitei116 – 1161Substrate; in homodimeric partner By similarity
Binding sitei166 – 1661Substrate By similarity
Active sitei168 – 1681Proton acceptor By similarity
Binding sitei170 – 1701Substrate By similarity
Metal bindingi194 – 1941Magnesium; via carbamate group By similarity
Metal bindingi196 – 1961Magnesium By similarity
Metal bindingi197 – 1971Magnesium By similarity
Active sitei287 – 2871Proton acceptor By similarity
Binding sitei288 – 2881Substrate By similarity
Binding sitei320 – 3201Substrate By similarity
Sitei327 – 3271Transition state stabilizer By similarity
Binding sitei372 – 3721Substrate By similarity

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

BioCyciHNEA555778:GIVV-951-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:cbbL
Ordered Locus Names:Hneap_0922
OrganismiHalothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus neapolitanus)
Taxonomic identifieri555778 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesHalothiobacillaceaeHalothiobacillus
ProteomesiUP000009102: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000062660Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941N6-carboxylysine By similarity

Expressioni

Inductioni

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

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi555778.Hneap_0922.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 3710
Helixi43 – 5311
Turni54 – 563
Helixi63 – 675
Turni70 – 723
Beta strandi76 – 838
Beta strandi86 – 9611
Helixi98 – 1003
Helixi106 – 1149
Helixi117 – 1193
Beta strandi123 – 13210
Helixi135 – 1384
Helixi148 – 1558
Beta strandi162 – 1665
Beta strandi170 – 1723
Helixi175 – 18713
Beta strandi191 – 1944
Beta strandi200 – 2023
Helixi207 – 22519
Beta strandi230 – 2345
Helixi240 – 25314
Beta strandi257 – 2615
Turni262 – 2654
Helixi267 – 28014
Beta strandi283 – 2875
Helixi291 – 2955
Beta strandi300 – 3023
Helixi304 – 31411
Beta strandi317 – 3204
Helixi329 – 3313
Helixi333 – 34311
Beta strandi345 – 3473
Helixi351 – 3533
Beta strandi368 – 3747
Helixi377 – 3793
Helixi380 – 3878
Beta strandi389 – 3946
Helixi397 – 4004
Helixi406 – 42520
Turni430 – 4334
Helixi434 – 4429
Helixi446 – 45510

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SVDX-ray1.80A1-473[»]
ProteinModelPortaliO85040.
SMRiO85040. Positions 16-460.

Miscellaneous databases

EvolutionaryTraceiO85040.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiMETWKEV.
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.

O85040-1 [UniParc]FASTAAdd to Basket

« Hide

MAVKKYSAGV KEYRQTYWMP EYTPLDSDIL ACFKITPQPG VDREEAAAAV    50
AAESSTGTWT TVWTDLLTDM DYYKGRAYRI EDVPGDDAAF YAFIAYPIDL 100
FEEGSVVNVF TSLVGNVFGF KAVRGLRLED VRFPLAYVKT CGGPPHGIQV 150
ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENIN 200
SQPFMRWRDR FLFVQDATET AEAQTGERKG HYLNVTAPTP EEMYKRAEFA 250
KEIGAPIIMH DYITGGFTAN TGLAKWCQDN GVLLHIHRAM HAVIDRNPNH 300
GIHFRVLTKI LRLSGGDHLH TGTVVGKLEG DRASTLGWID LLRESFIPED 350
RSRGIFFDQD WGSMPGVFAV ASGGIHVWHM PALVNIFGDD SVLQFGGGTL 400
GHPWGNAAGA AANRVALEAC VEARNQGRDI EKEGKEILTA AAQHSPELKI 450
AMETWKEIKF EFDTVDKLDT QNR 473
Length:473
Mass (Da):52,636
Last modified:November 1, 1998 - v1
Checksum:iB84D2EDE46CAF7D8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF038430 Genomic DNA. Translation: AAC32549.1.
CP001801 Genomic DNA. Translation: ACX95765.1.
RefSeqiWP_012823801.1. NC_013422.1.
YP_003262812.1. NC_013422.1.

Genome annotation databases

EnsemblBacteriaiACX95765; ACX95765; Hneap_0922.
GeneIDi8534063.
KEGGihna:Hneap_0922.
PATRICi32205718. VBIHalNea120669_0941.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF038430 Genomic DNA. Translation: AAC32549.1 .
CP001801 Genomic DNA. Translation: ACX95765.1 .
RefSeqi WP_012823801.1. NC_013422.1.
YP_003262812.1. NC_013422.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SVD X-ray 1.80 A 1-473 [» ]
ProteinModelPortali O85040.
SMRi O85040. Positions 16-460.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 555778.Hneap_0922.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACX95765 ; ACX95765 ; Hneap_0922 .
GeneIDi 8534063.
KEGGi hna:Hneap_0922.
PATRICi 32205718. VBIHalNea120669_0941.

Phylogenomic databases

eggNOGi COG1850.
HOGENOMi HOG000230831.
KOi K01601.
OMAi METWKEV.
OrthoDBi EOG6ZKXMS.

Enzyme and pathway databases

BioCyci HNEA555778:GIVV-951-MONOMER.

Miscellaneous databases

EvolutionaryTracei O85040.

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

« Hide 'large scale' publications
  1. "Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in expression of form II RuBisCO, loss of carboxysomes, and an increased CO2 requirement for growth."
    Baker S.H., Jin S., Aldrich H.C., Howard G.T., Shively J.M.
    J. Bacteriol. 180:4133-4139(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], EXPRESSION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 23641 / c2.
  3. "The structure of Halothiobacillus neapolitanus Rubisco."
    Kerfeld C.A., Sawaya M.R., Pashkov I., Cannon G., Williams E., Tran K., Yeates T.O.
    Submitted (APR-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

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: September 3, 2014
This is version 76 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" By similarity.

Keywords - Technical termi

3D-structure, Complete proteome

Documents

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

External Data

Dasty 3

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