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P22859

- RBL1B_ALLVD

UniProt

P22859 - RBL1B_ALLVD

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Protein
Ribulose bisphosphate carboxylase large chain 2
Gene
cbbL2, rbcL, Alvin_2750
Organism
Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D) (Chromatium vinosum)
Status
Reviewed - Annotation score: 4 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

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

BioCyciAVIN572477:GCJK-2812-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain 2 (EC:4.1.1.39)
Short name:
RuBisCO large subunit 2
Gene namesi
Name:cbbL2
Synonyms:rbcL
Ordered Locus Names:Alvin_2750
OrganismiAllochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / D) (Chromatium vinosum)
Taxonomic identifieri572477 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeAllochromatium
ProteomesiUP000001441: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 471470Ribulose bisphosphate carboxylase large chain 2UniRule annotation
PRO_0000062622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941N6-carboxylysine By similarity
Disulfide bondi240 – 240Interchain; in linked form By similarity

Post-translational modificationi

The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover By similarity.UniRule annotation

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity.

Structurei

3D structure databases

ProteinModelPortaliP22859.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000230831.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22859-1 [UniParc]FASTAAdd to Basket

« Hide

MSTKTYDAGV KDYALTYWTP DYVPLDSDLL ACFKVTPQAK VSREEAAAAV    50
AAESSTGTWT TVWSDLLTDL DYYKGRAYRI EDVPGDKESF YAFIAYPLDL 100
FEEGSIVNVL TSLVGNVFGF KAVRALRLED IRFPLHYVKT CGGPPNGIQV 150
ERDRMDKYGR PFLGATVKPK LGLSAKNYGR AVYEMLRGGL DFTKDDENVN 200
SQPFMRWQNR FEFVSEAVRK AQEETGERKG HYLNVTAPTC EEMFKRAEFA 250
KECGAPIIMH DFLTGGFTAN TSLANWCRDN GMLLHIHRAM HAVIDRNPKH 300
GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRQSTLGFVD QLRESFIPED 350
RSRGLFFDQD WGGMPGVMAV ASGGIHVWHI PALVTIFGDD SVLQFGGGTQ 400
GHPWGNAAGA AANRVATEAC VKARNEGVEI EKHAREVLSD AARHSPELAV 450
AMETWKEIKF EFDVVDKLDA A 471
Length:471
Mass (Da):52,284
Last modified:June 15, 2010 - v4
Checksum:i08A26940B6458D97
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451P → R in BAA14229. 1 Publication
Sequence conflicti222 – 2221Q → R in BAA14229. 1 Publication
Sequence conflicti297 – 2971N → H in BAA14229. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D90204 Genomic DNA. Translation: BAA14229.1.
CP001896 Genomic DNA. Translation: ADC63659.1.
PIRiJQ0586. RKKRL2.
RefSeqiYP_003444691.1. NC_013851.1.

Genome annotation databases

EnsemblBacteriaiADC63659; ADC63659; Alvin_2750.
GeneIDi8788139.
KEGGialv:Alvin_2750.
PATRICi31925280. VBIAllVin64954_2712.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D90204 Genomic DNA. Translation: BAA14229.1 .
CP001896 Genomic DNA. Translation: ADC63659.1 .
PIRi JQ0586. RKKRL2.
RefSeqi YP_003444691.1. NC_013851.1.

3D structure databases

ProteinModelPortali P22859.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADC63659 ; ADC63659 ; Alvin_2750 .
GeneIDi 8788139.
KEGGi alv:Alvin_2750.
PATRICi 31925280. VBIAllVin64954_2712.

Phylogenomic databases

HOGENOMi HOG000230831.
KOi K01601.

Enzyme and pathway databases

BioCyci AVIN572477:GCJK-2812-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. "Sequence and expression of genes encoding the large and small subunits of ribulose 1,5-bisphosphate carboxylase/oxygenase from Chromatium vinosum."
    Kobayashi H., Viale A.M., Takabe T., Akazawa T., Wada K., Shinozaki K., Kobayashi K., Sugiura M.
    Gene 97:55-62(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequence of chromosome of Allochromatium vinosum DSM 180."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Zigann R., Dahl C., Woyke T.
    Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 17899 / DSM 180 / NBRC 103801 / D.
  3. "Distinct properties of Escherichia coli products of plant-type ribulose-1,5-bisphosphate carboxylase/oxygenase directed by two sets of genes from the photosynthetic bacterium Chromatium vinosum."
    Viale A.M., Kobayashi H., Akazawa T.
    J. Biol. Chem. 265:18386-18392(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-26.

Entry informationi

Entry nameiRBL1B_ALLVD
AccessioniPrimary (citable) accession number: P22859
Secondary accession number(s): D3RQ48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 15, 2010
Last modified: May 14, 2014
This is version 92 of the entry and version 4 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.

Caution

In C.vinosum two similar set of genes code for RuBisCO large and small chains: the RbcL-RbcS and the RbcA-RbcB sets. Under standard photoautotrophic culture conditions only the latter set seems active, the former probably being cryptic.

Keywords - Technical termi

Complete proteome, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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