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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Synechococcus sp. (strain ATCC 27167 / PCC 6312)
Status
Unreviewed-Annotation score: Annotation score: 4 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

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei123 – 1231Substrate; in homodimeric partnerUniRule annotation
Binding sitei173 – 1731SubstrateUniRule annotation
Active sitei175 – 1751Proton acceptorUniRule annotation
Binding sitei177 – 1771SubstrateUniRule annotation
Metal bindingi201 – 2011Magnesium; via carbamate groupUniRule annotation
Metal bindingi203 – 2031MagnesiumUniRule annotation
Metal bindingi204 – 2041MagnesiumUniRule annotation
Active sitei294 – 2941Proton acceptorUniRule annotation
Binding sitei295 – 2951SubstrateUniRule annotation
Binding sitei327 – 3271SubstrateUniRule annotation
Sitei334 – 3341Transition state stabilizerUniRule annotation
Binding sitei379 – 3791SubstrateUniRule 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

LyaseUniRule annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation, PhotorespirationUniRule annotation, PhotosynthesisUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

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:Syn6312_2007Imported
OrganismiSynechococcus sp. (strain ATCC 27167 / PCC 6312)Imported
Taxonomic identifieri195253 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000010379: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei201 – 2011N6-carboxylysineUniRule annotation
Disulfide bondi247 – 247Interchain; 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 bondUniRule annotation

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

ProteinModelPortaliK9RV09.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

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.

K9RV09-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYAQKAPGK AGYKAGVQDY RLTYYTPDYT PKDTDILAAF RVTPQPGVPY
60 70 80 90 100
EEAAAAVAAE SSTGTWTTVW TDLLTDLDRY KGRCYDIESV PGEDNQFIAY
110 120 130 140 150
IAYPLDLFEE GSVTNLLTSL VGNVFGFKAL KALRLEDLRI PVAYLKTFQG
160 170 180 190 200
PPHGIQVERD KINKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT
210 220 230 240 250
KDDENINSQP FQRWRDRFLF VADAIHKAQA ETGEVKGHYL NVTAATCEEM
260 270 280 290 300
LKRAEFAKEL EMPIIMHDFL TGGFTANTTL AHWCRDNGVL LHIHRAMHAV
310 320 330 340 350
IDRQKNHGIH FRVLAKCLRM SGGDHIHTGT VVGKLEGDKA ITLGFIDLLR
360 370 380 390 400
ENYIEQDRSR GVYFTQDWAS MGGVMAVASG GIHVWHMPAL VEIFGDDSVL
410 420 430 440 450
QFGGGTLGHP WGNAPGATAN RVALEACVQA RNEGRDLMRE GGDIIREACK
460 470
WSPELAAACE LWKEIKFEFE AVDTV
Length:475
Mass (Da):52,773
Last modified:March 6, 2013 - v1
Checksum:iBF456F1B027C9C50
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003558 Genomic DNA. Translation: AFY61139.1.
RefSeqiWP_015124682.1. NC_019680.1.
YP_007061682.1. NC_019680.1.

Genome annotation databases

EnsemblBacteriaiAFY61139; AFY61139; Syn6312_2007.
GeneIDi14076217.
KEGGisyne:Syn6312_2007.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003558 Genomic DNA. Translation: AFY61139.1.
RefSeqiWP_015124682.1. NC_019680.1.
YP_007061682.1. NC_019680.1.

3D structure databases

ProteinModelPortaliK9RV09.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFY61139; AFY61139; Syn6312_2007.
GeneIDi14076217.
KEGGisyne:Syn6312_2007.

Phylogenomic databases

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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27167 / PCC 6312Imported.

Entry informationi

Entry nameiK9RV09_SYNP3
AccessioniPrimary (citable) accession number: K9RV09
Entry historyi
Integrated into UniProtKB/TrEMBL: March 6, 2013
Last sequence update: March 6, 2013
Last modified: January 7, 2015
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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 proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.