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C7QSC5

- C7QSC5_CYAP0

UniProt

C7QSC5 - C7QSC5_CYAP0

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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Cyanothece sp. (strain PCC 8802) (Synechococcus sp. (strain RF-2))
Status
Unreviewed - 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

Binds 1 magnesium ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei120 – 1201Substrate; in homodimeric partnerUniRule annotation
Binding sitei170 – 1701SubstrateUniRule annotation
Active sitei172 – 1721Proton acceptorUniRule annotation
Binding sitei174 – 1741SubstrateUniRule annotation
Metal bindingi198 – 1981Magnesium; via carbamate groupUniRule annotation
Metal bindingi200 – 2001MagnesiumUniRule annotation
Metal bindingi201 – 2011MagnesiumUniRule annotation
Active sitei291 – 2911Proton acceptorUniRule annotation
Binding sitei292 – 2921SubstrateUniRule annotation
Binding sitei324 – 3241SubstrateUniRule annotation
Sitei331 – 3311Transition state stabilizerUniRule annotation
Binding sitei376 – 3761SubstrateUniRule 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

Enzyme and pathway databases

BioCyciCSP395962:GJC3-1637-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:Cyan8802_1628Imported
OrganismiCyanothece sp. (strain PCC 8802) (Synechococcus sp. (strain RF-2))Imported
Taxonomic identifieri395962 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece
ProteomesiUP000000415: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981N6-carboxylysineUniRule annotation
Disulfide bondi244 – 244Interchain; 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

Protein-protein interaction databases

STRINGi395962.Cyan8802_1628.

Structurei

3D structure databases

ProteinModelPortaliC7QSC5.
SMRiC7QSC5. Positions 9-466.
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.

C7QSC5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVQAKSKSGF EAGVKDYRLT YYTPDYTPKD TDLLACFRMT PQPGVPPEEA
60 70 80 90 100
GAAVAAESST GTWTTVWTDN LTDLDRYKGR CYDIEKVENE DNQYFCFIAY
110 120 130 140 150
PLDLFEEGSV TNVLTSLVGN VFGFKALRAL RLEDIRFPVA LIKTFQGPPH
160 170 180 190 200
GITVERDKLN KYGRPLLGCT IKPKLGLSAK NYGRAVYECL RGGLDFTKDD
210 220 230 240 250
ENINSQPFMR WRDRFLFVQD AIEKAQAETN EVKGHYLNVT AGTCEEMLKR
260 270 280 290 300
AEFAKEIKTP IIMHDFLTGG FTANTTLAKF CRDNGLLLHI HRAMHAVIDR
310 320 330 340 350
QKNHGIHFRV LAKCLRLSGG DHLHSGTVVG KLEGERGITM GFVDLMREDY
360 370 380 390 400
VEEDRSRGIF FTQDYASMPG TMPVASGGIH VWHMPALVEI FGDDSCLQFG
410 420 430 440 450
GGTLGHPWGN APGATANRVA LEACIQARNE GRSLAREGND VIREACKWSP
460 470
ELAAACELWK EIKFEFEAMD TL
Length:472
Mass (Da):52,735
Last modified:October 13, 2009 - v1
Checksum:i9E7709AB3A482831
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001701 Genomic DNA. Translation: ACV00534.1.
RefSeqiYP_003137369.1. NC_013161.1.

Genome annotation databases

EnsemblBacteriaiACV00534; ACV00534; Cyan8802_1628.
GeneIDi8390940.
KEGGicyh:Cyan8802_1628.
PATRICi21584769. VBICyaSp112625_1713.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001701 Genomic DNA. Translation: ACV00534.1 .
RefSeqi YP_003137369.1. NC_013161.1.

3D structure databases

ProteinModelPortali C7QSC5.
SMRi C7QSC5. Positions 9-466.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 395962.Cyan8802_1628.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACV00534 ; ACV00534 ; Cyan8802_1628 .
GeneIDi 8390940.
KEGGi cyh:Cyan8802_1628.
PATRICi 21584769. VBICyaSp112625_1713.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci CSP395962:GJC3-1637-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. "Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
    Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
    MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 8802Imported.

Entry informationi

Entry nameiC7QSC5_CYAP0
AccessioniPrimary (citable) accession number: C7QSC5
Entry historyi
Integrated into UniProtKB/TrEMBL: October 13, 2009
Last sequence update: October 13, 2009
Last modified: October 29, 2014
This is version 39 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 proteomeImported

External Data

Dasty 3