Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

K9U766

- K9U766_9CYAN

UniProt

K9U766 - K9U766_9CYAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Chroococcidiopsis thermalis PCC 7203
Status
Unreviewed - 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

Note: Binds 1 magnesium ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei124 – 1241Substrate; in homodimeric partnerUniRule annotation
Binding sitei174 – 1741SubstrateUniRule annotation
Active sitei176 – 1761Proton acceptorUniRule annotation
Binding sitei178 – 1781SubstrateUniRule annotation
Metal bindingi202 – 2021Magnesium; via carbamate groupUniRule annotation
Metal bindingi204 – 2041MagnesiumUniRule annotation
Metal bindingi205 – 2051MagnesiumUniRule annotation
Active sitei295 – 2951Proton acceptorUniRule annotation
Binding sitei296 – 2961SubstrateUniRule annotation
Binding sitei328 – 3281SubstrateUniRule annotation
Sitei335 – 3351Transition state stabilizerUniRule annotation
Binding sitei380 – 3801SubstrateUniRule 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

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
ORF Names:Chro_5313Imported
OrganismiChroococcidiopsis thermalis PCC 7203Imported
Taxonomic identifieri251229 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaPleurocapsalesChroococcidiopsis
ProteomesiUP000010384: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-carboxylysineUniRule annotation
Disulfide bondi248 – 248Interchain; 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

ProteinModelPortaliK9U766.
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.

K9U766-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSYAQTRTQT KSGYQAGVKD YRLTYYTPDY TPKDTDVLAC FRVSPQPGVP
60 70 80 90 100
PEEAGAAVAA ESSTGTWTTV WTDLLTDLDR YKGRCYYIEP VPGEDNQFFC
110 120 130 140 150
FVAYPLDLFE EGSVTNMLTS IVGNVFGFKA LKALRLEDMR IPVAYLKTFQ
160 170 180 190 200
GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF
210 220 230 240 250
TKDDENINSQ PFMRWRDRFL FVQEAIGKAQ AETGEVKGHY LNVTAPTCEE
260 270 280 290 300
MMKRAEFAKE LGTPIIMHDY LTGGFTANTT LAKYCRDNGL LLHIHRAMHA
310 320 330 340 350
VIDRQRNHGI HFRVLAKCLR MSGGDHLHSG TVVGKLEGER GITMGFVDLM
360 370 380 390 400
RENYIEEDRS RGIFFTQDWA SMPGVMPVAS GGIHIWHMPA LVEIFGDDSC
410 420 430 440 450
LQFGGGTLGH PWGNAPGATA NRVALEACVQ ARNEGRDLAR EGNDVIREAA
460 470
KWSPELAVAC ELWKEIKFEF KAVDTL
Length:476
Mass (Da):53,151
Last modified:March 6, 2013 - v1
Checksum:i4BD7BDAD52BDCFD2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003597 Genomic DNA. Translation: AFY90680.1.
RefSeqiWP_015157218.1. NC_019695.1.
YP_007094549.1. NC_019695.1.

Genome annotation databases

EnsemblBacteriaiAFY90680; AFY90680; Chro_5313.
GeneIDi14121123.
KEGGicthe:Chro_5313.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003597 Genomic DNA. Translation: AFY90680.1 .
RefSeqi WP_015157218.1. NC_019695.1.
YP_007094549.1. NC_019695.1.

3D structure databases

ProteinModelPortali K9U766.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFY90680 ; AFY90680 ; Chro_5313 .
GeneIDi 14121123.
KEGGi cthe:Chro_5313.

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.
    Strain: PCC 7203Imported.

Entry informationi

Entry nameiK9U766_9CYAN
AccessioniPrimary (citable) accession number: K9U766
Entry historyi
Integrated into UniProtKB/TrEMBL: March 6, 2013
Last sequence update: March 6, 2013
Last modified: November 26, 2014
This is version 14 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