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P96486

- RBL_SYNPW

UniProt

P96486 - RBL_SYNPW

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Synechococcus sp. (strain WH7803)
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

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:SynWH7803_0678
OrganismiSynechococcus sp. (strain WH7803)
Taxonomic identifieri32051 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001566: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471Ribulose bisphosphate carboxylase large chainPRO_0000062652Add
BLAST

Amino acid modifications

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

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi32051.SynWH7803_0678.

Structurei

3D structure databases

ProteinModelPortaliP96486.
SMRiP96486. 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.

P96486-1 [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 RFPMAFIKSC YGPPNGIQVE
160 170 180 190 200
RDRMNKYGRP LLGCTIKPKL GLSGKNYGRV VYECLRGGLD FTKDDENINS
210 220 230 240 250
QPFQRWQNRF EFVAEAIKLS EQETGERKGH YLNVTANTPE EMYERAEFAK
260 270 280 290 300
ELGMPIIMHD FITGGFTANT GLSKWCRKNG MLLHIHRAMH AVIDRHPKHG
310 320 330 340 350
IHFRVLAKCL RLSGGDQLHT GTVVGKLEGD RQTTLGYIDQ LRESFVPEDR
360 370 380 390 400
SRGNFFDQDW GSMPGVFAVA SGGIHVWHMP ALVTIFGDDS VLQFGGGTHG
410 420 430 440 450
HPWGSAAGAA ANRVALEACV KARNAGRHLE KESRDILMEA GKHSPELAIA
460 470
LETWKEIKFE FDTVDKLDVQ N
Length:471
Mass (Da):52,848
Last modified:May 1, 1997 - v1
Checksum:i96638DF99FD6BF1D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U46156 Genomic DNA. Translation: AAB48080.1.
CT971583 Genomic DNA. Translation: CAK23104.1.
RefSeqiWP_011932588.1. NC_009481.1.
YP_001224401.1. NC_009481.1.

Genome annotation databases

EnsemblBacteriaiCAK23104; CAK23104; SynWH7803_0678.
GeneIDi5147701.
KEGGisyx:SynWH7803_0678.
PATRICi23827459. VBISynSp43824_0695.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U46156 Genomic DNA. Translation: AAB48080.1 .
CT971583 Genomic DNA. Translation: CAK23104.1 .
RefSeqi WP_011932588.1. NC_009481.1.
YP_001224401.1. NC_009481.1.

3D structure databases

ProteinModelPortali P96486.
SMRi P96486. Positions 15-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 32051.SynWH7803_0678.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAK23104 ; CAK23104 ; SynWH7803_0678 .
GeneIDi 5147701.
KEGGi syx:SynWH7803_0678.
PATRICi 23827459. VBISynSp43824_0695.

Phylogenomic databases

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

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. "Regulation, unique gene organization, and unusual primary structure of carbon fixation genes from a marine phycoerythrin-containing cyanobacterium."
    Watson G.M., Tabita F.R.
    Plant Mol. Biol. 32:1103-1115(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Genoscope
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: WH7803.

Entry informationi

Entry nameiRBL_SYNPW
AccessioniPrimary (citable) accession number: P96486
Secondary accession number(s): A5GJI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: October 1, 2014
This is version 83 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3