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O32740

- RBL1_RHOCB

UniProt

O32740 - RBL1_RHOCB

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, cbbL1, RCAP_rcc00579
Organism
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Status
Reviewed - 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 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, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciRCAP272942:GJIY-590-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
Synonyms:cbbL1
Ordered Locus Names:RCAP_rcc00579
OrganismiRhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Taxonomic identifieri272942 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
ProteomesiUP000002361: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000062645Add
BLAST

Amino acid modifications

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

Proteomic databases

PRIDEiO32740.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliO32740.
SMRiO32740. Positions 17-460.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.
OMAiMFKRAEY.

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.

O32740-1 [UniParc]FASTAAdd to Basket

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MAAKTYDAGV KDYRSIYWEP QYQVKDSDIL AVFKVVPQPG VSREEAAAAV    50
AAESSTATWT TVWTDLLTDL DYYKGRAYAI EDVPGSDEAF YAFIAYPMDL 100
FEEGSVVNVF TSLVGNVFGF KAVRALRLED VRFPLWFVMT CPGAPHGMKV 150
ERDLLDKYGR PLLGCTIKPK LGLAAKNYGR AVYECLRGGL DFTKDDENVN 200
SQPFLRWRDR FLFCQEAIQK AEAETGERKG HYMNVTAGTM EEIYERAEFA 250
KEIGTPIIMS DYLTVGWAAH TSLSRWCRKN GMLLHVHRAM HAVMDRNPNH 300
GINFRVLAKI LRLMGGDHLH SGTVVGKLEG DREATIGWIN LLRDRFIKAD 350
RSRGIFFDQD WGPQPGLFPV ASGGIHVWHM PALVSIFGND SVLQFGGGTL 400
GHPWGNAAGA CANRVALEAC VQARNEGRHL EKEGKEILTK AAQSSPELRM 450
AMETWKEIKF EFDTVDKLDV QHR 473
Length:473
Mass (Da):53,037
Last modified:January 1, 1998 - v1
Checksum:i9F2C3173618B9958
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L82000 Genomic DNA. Translation: AAC37141.1.
CP001312 Genomic DNA. Translation: ADE84344.1.
RefSeqiWP_013066323.1. NC_014034.1.
YP_003576751.1. NC_014034.1.

Genome annotation databases

EnsemblBacteriaiADE84344; ADE84344; RCAP_rcc00579.
GeneIDi9003408.
KEGGircp:RCAP_rcc00579.
PATRICi35501218. VBIRhoCap134200_0588.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L82000 Genomic DNA. Translation: AAC37141.1 .
CP001312 Genomic DNA. Translation: ADE84344.1 .
RefSeqi WP_013066323.1. NC_014034.1.
YP_003576751.1. NC_014034.1.

3D structure databases

ProteinModelPortali O32740.
SMRi O32740. Positions 17-460.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi O32740.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADE84344 ; ADE84344 ; RCAP_rcc00579 .
GeneIDi 9003408.
KEGGi rcp:RCAP_rcc00579.
PATRICi 35501218. VBIRhoCap134200_0588.

Phylogenomic databases

HOGENOMi HOG000230831.
KOi K01601.
OMAi MFKRAEY.

Enzyme and pathway databases

BioCyci RCAP272942:GJIY-590-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

« Hide 'large scale' publications
  1. "Rhodobacter capsulatus genes encoding form I ribulose-1,5-bisphosphate carboxylase/oxygenase (cbbLS) and neighbouring genes were acquired by a horizontal gene transfer."
    Paoli G.C., Soyer F., Shively J., Tabita F.R.
    Microbiology 144:219-227(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
  2. "Complete genome sequence of the photosynthetic purple nonsulfur bacterium Rhodobacter capsulatus SB 1003."
    Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., Haselkorn R.
    J. Bacteriol. 192:3545-3546(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-309 / NBRC 16581 / SB1003.
  3. "Expression of the cbbLcbbS and cbbM genes and distinct organization of the cbb Calvin cycle structural genes of Rhodobacter capsulatus."
    Paoli G.C., Morgan N.S., Tabita F.R., Shively J.M.
    Arch. Microbiol. 164:396-405(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: OPERON ORGANIZATION.
    Strain: ATCC BAA-309 / NBRC 16581 / SB1003.

Entry informationi

Entry nameiRBL1_RHOCB
AccessioniPrimary (citable) accession number: O32740
Secondary accession number(s): D5ANJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 78 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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