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P22859

- RBL1B_ALLVD

UniProt

P22859 - RBL1B_ALLVD

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Protein

Ribulose bisphosphate carboxylase large chain 2

Gene

cbbL2

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.

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 Mg(2+) ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei116 – 1161Substrate; in homodimeric partnerUniRule annotation
Binding sitei166 – 1661SubstrateUniRule annotation
Active sitei168 – 1681Proton acceptorUniRule annotation
Binding sitei170 – 1701SubstrateUniRule annotation
Metal bindingi194 – 1941Magnesium; via carbamate groupUniRule annotation
Metal bindingi196 – 1961MagnesiumUniRule annotation
Metal bindingi197 – 1971MagnesiumUniRule annotation
Active sitei287 – 2871Proton acceptorUniRule annotation
Binding sitei288 – 2881SubstrateUniRule annotation
Binding sitei320 – 3201SubstrateUniRule annotation
Sitei327 – 3271Transition state stabilizerUniRule annotation
Binding sitei372 – 3721SubstrateUniRule 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

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 2UniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunit 2UniRule annotation
Gene namesi
Name:cbbL2UniRule annotation
Synonyms:rbcLUniRule annotation
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 2PRO_0000062622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941N6-carboxylysineUniRule annotation
Disulfide bondi240 – 240Interchain; in linked formUniRule annotation

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.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.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP22859.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

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

        10         20         30         40         50
MSTKTYDAGV KDYALTYWTP DYVPLDSDLL ACFKVTPQAK VSREEAAAAV
60 70 80 90 100
AAESSTGTWT TVWSDLLTDL DYYKGRAYRI EDVPGDKESF YAFIAYPLDL
110 120 130 140 150
FEEGSIVNVL TSLVGNVFGF KAVRALRLED IRFPLHYVKT CGGPPNGIQV
160 170 180 190 200
ERDRMDKYGR PFLGATVKPK LGLSAKNYGR AVYEMLRGGL DFTKDDENVN
210 220 230 240 250
SQPFMRWQNR FEFVSEAVRK AQEETGERKG HYLNVTAPTC EEMFKRAEFA
260 270 280 290 300
KECGAPIIMH DFLTGGFTAN TSLANWCRDN GMLLHIHRAM HAVIDRNPKH
310 320 330 340 350
GIHFRVLAKC LRLSGGDHLH TGTVVGKLEG DRQSTLGFVD QLRESFIPED
360 370 380 390 400
RSRGLFFDQD WGGMPGVMAV ASGGIHVWHI PALVTIFGDD SVLQFGGGTQ
410 420 430 440 450
GHPWGNAAGA AANRVATEAC VKARNEGVEI EKHAREVLSD AARHSPELAV
460 470
AMETWKEIKF EFDVVDKLDA A
Length:471
Mass (Da):52,284
Last modified:June 15, 2010 - v4
Checksum:i08A26940B6458D97
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451P → R in BAA14229. (PubMed:1899846)Curated
Sequence conflicti222 – 2221Q → R in BAA14229. (PubMed:1899846)Curated
Sequence conflicti297 – 2971N → H in BAA14229. (PubMed:1899846)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90204 Genomic DNA. Translation: BAA14229.1.
CP001896 Genomic DNA. Translation: ADC63659.1.
PIRiJQ0586. RKKRL2.
RefSeqiWP_012971927.1. NC_013851.1.
YP_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:
EMBLi
GenBanki
DDBJi
Links Updated
D90204 Genomic DNA. Translation: BAA14229.1 .
CP001896 Genomic DNA. Translation: ADC63659.1 .
PIRi JQ0586. RKKRL2.
RefSeqi WP_012971927.1. NC_013851.1.
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: November 26, 2014
This is version 94 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".UniRule annotation

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.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3