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Q0I8Q2

- RBL_SYNS3

UniProt

Q0I8Q2 - RBL_SYNS3

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Synechococcus sp. (strain CC9311)
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 in the photorespiration process. 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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei115 – 1151Substrate; in homodimeric partnerUniRule annotation
Binding sitei165 – 1651SubstrateUniRule annotation
Active sitei167 – 1671Proton acceptorUniRule annotation
Binding sitei169 – 1691SubstrateUniRule annotation
Metal bindingi193 – 1931Magnesium; via carbamate groupUniRule annotation
Metal bindingi195 – 1951MagnesiumUniRule annotation
Metal bindingi196 – 1961MagnesiumUniRule annotation
Active sitei286 – 2861Proton acceptorUniRule annotation
Binding sitei287 – 2871SubstrateUniRule annotation
Binding sitei319 – 3191SubstrateUniRule annotation
Sitei326 – 3261Transition state stabilizerUniRule annotation
Binding sitei371 – 3711SubstrateUniRule 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. photorespiration Source: UniProtKB-KW
  2. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciSSP64471:GIVP-1967-MONOMER.

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
Synonyms:rbcLUniRule annotation
Ordered Locus Names:sync_1967
OrganismiSynechococcus sp. (strain CC9311)
Taxonomic identifieri64471 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001961: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Ribulose bisphosphate carboxylase large chainPRO_0000299975Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei193 – 1931N6-carboxylysineUniRule annotation

Proteomic databases

PRIDEiQ0I8Q2.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi64471.sync_1967.

Structurei

3D structure databases

ProteinModelPortaliQ0I8Q2.
SMRiQ0I8Q2. Positions 15-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
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.

Q0I8Q2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKKYDAGVK EYRDTYWTPD YVPLDTDLLA CFKCTGQEGV PKEEVAAAVA
60 70 80 90 100
AESSTGTWST VWSELLTDLD FYKGRCYRIE DVPGDKESFY AFIAYPLDLF
110 120 130 140 150
EEGSITNVLT SLVGNVFGFK ALRHLRLEDI RFPIAFIKCC AGPPNGIAVE
160 170 180 190 200
RDRMNKYGRP LLGCTIKPKL GLSGKNYGRV VYECLRGGLD FTKDDENINS
210 220 230 240 250
QPFQRWQNRF EFVAEAIKLA EQETGERKGH YLNVTANTPE EMYERAEFAK
260 270 280 290 300
ELNQPIIMHD FITGGFTANT GLSKWCRKNG MLLHIHRAMH AVIDRHPKHG
310 320 330 340 350
IHFRVLAKCL RLSGGDQLHT GTVVGKLEGD RQTTLGYIDQ LRESFVPEDR
360 370 380 390 400
SRGNFFDQDW GSMPGVFAVA SGGIHVWHMP ALVAIFGDDS VLQFGGGTHG
410 420 430 440 450
HPWGSAAGAA ANRVALEACV KARNAGREIE KESRDILMEA GKHSPELAIA
460 470
LETWKEIKFE FDTVDKLDVQ
Length:470
Mass (Da):52,583
Last modified:October 3, 2006 - v1
Checksum:iED75385F35DAC046
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000435 Genomic DNA. Translation: ABI45662.1.
RefSeqiWP_011619883.1. NC_008319.1.
YP_731170.1. NC_008319.1.

Genome annotation databases

EnsemblBacteriaiABI45662; ABI45662; sync_1967.
GeneIDi4261670.
KEGGisyg:sync_1967.
PATRICi23795002. VBISynSp88089_2056.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000435 Genomic DNA. Translation: ABI45662.1 .
RefSeqi WP_011619883.1. NC_008319.1.
YP_731170.1. NC_008319.1.

3D structure databases

ProteinModelPortali Q0I8Q2.
SMRi Q0I8Q2. Positions 15-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 64471.sync_1967.

Proteomic databases

PRIDEi Q0I8Q2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABI45662 ; ABI45662 ; sync_1967 .
GeneIDi 4261670.
KEGGi syg:sync_1967.
PATRICi 23795002. VBISynSp88089_2056.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SSP64471:GIVP-1967-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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CC9311.

Entry informationi

Entry nameiRBL_SYNS3
AccessioniPrimary (citable) accession number: Q0I8Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 3, 2006
Last modified: October 1, 2014
This is version 56 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3