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K9RV09

- K9RV09_SYNP3

UniProt

K9RV09 - K9RV09_SYNP3

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Protein

Ribulose bisphosphate carboxylase large chain

Gene
cbbL, rbcL, Syn6312_2007
Organism
Synechococcus sp. (strain ATCC 27167 / PCC 6312)
Status
Unreviewed - 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 in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site By similarity.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 sitei123 – 1231Substrate; in homodimeric partner By similarityUniRule annotation
Binding sitei173 – 1731Substrate By similarityUniRule annotation
Active sitei175 – 1751Proton acceptor By similarityUniRule annotation
Binding sitei177 – 1771Substrate By similarityUniRule annotation
Metal bindingi201 – 2011Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi203 – 2031Magnesium By similarityUniRule annotation
Metal bindingi204 – 2041Magnesium By similarityUniRule annotation
Active sitei294 – 2941Proton acceptor By similarityUniRule annotation
Binding sitei295 – 2951Substrate By similarityUniRule annotation
Binding sitei327 – 3271Substrate By similarityUniRule annotation
Sitei334 – 3341Transition state stabilizer By similarityUniRule annotation
Binding sitei379 – 3791Substrate By similarityUniRule 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-carboxylysine By similarityUniRule annotation
Disulfide bondi247 – 247Interchain; in linked form By similarityUniRule 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 By similarity.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 By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliK9RV09.

Family & Domainsi

Sequence similaritiesi

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

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MSYAQKAPGK AGYKAGVQDY RLTYYTPDYT PKDTDILAAF RVTPQPGVPY    50
EEAAAAVAAE SSTGTWTTVW TDLLTDLDRY KGRCYDIESV PGEDNQFIAY 100
IAYPLDLFEE GSVTNLLTSL VGNVFGFKAL KALRLEDLRI PVAYLKTFQG 150
PPHGIQVERD KINKYGRPLL GCTIKPKLGL SAKNYGRAVY ECLRGGLDFT 200
KDDENINSQP FQRWRDRFLF VADAIHKAQA ETGEVKGHYL NVTAATCEEM 250
LKRAEFAKEL EMPIIMHDFL TGGFTANTTL AHWCRDNGVL LHIHRAMHAV 300
IDRQKNHGIH FRVLAKCLRM SGGDHIHTGT VVGKLEGDKA ITLGFIDLLR 350
ENYIEQDRSR GVYFTQDWAS MGGVMAVASG GIHVWHMPAL VEIFGDDSVL 400
QFGGGTLGHP WGNAPGATAN RVALEACVQA RNEGRDLMRE GGDIIREACK 450
WSPELAAACE LWKEIKFEFE AVDTV 475
Length:475
Mass (Da):52,773
Last modified:March 6, 2013 - v1
Checksum:iBF456F1B027C9C50
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CP003558 Genomic DNA. Translation: AFY61139.1 .
RefSeqi WP_015124682.1. NC_019680.1.
YP_007061682.1. NC_019680.1.

3D structure databases

ProteinModelPortali K9RV09.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFY61139 ; AFY61139 ; Syn6312_2007 .
GeneIDi 14076217.
KEGGi syne:Syn6312_2007.

Phylogenomic databases

KOi K01601.

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: ATCC 27167 / PCC 6312.

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: September 3, 2014
This is version 11 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" By similarity.UniRule annotation

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi