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B0JVL8

- RBL_MICAN

UniProt

B0JVL8 - RBL_MICAN

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Protein

Ribulose bisphosphate carboxylase large chain

Gene
cbbL, rbcL, MAE_47890
Organism
Microcystis aeruginosa (strain NIES-843)
Status
Reviewed - 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 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 sitei119 – 1191Substrate; in homodimeric partner By similarity
Binding sitei169 – 1691Substrate By similarity
Active sitei171 – 1711Proton acceptor By similarity
Binding sitei173 – 1731Substrate By similarity
Metal bindingi197 – 1971Magnesium; via carbamate group By similarity
Metal bindingi199 – 1991Magnesium By similarity
Metal bindingi200 – 2001Magnesium By similarity
Active sitei290 – 2901Proton acceptor By similarity
Binding sitei291 – 2911Substrate By similarity
Binding sitei323 – 3231Substrate By similarity
Sitei330 – 3301Transition state stabilizer By similarity
Binding sitei375 – 3751Substrate By similarity

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

Enzyme and pathway databases

BioCyciMAER449447:GHO8-4825-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chain (EC:4.1.1.39)
Short name:
RuBisCO large subunit
Gene namesi
Name:cbbL
Synonyms:rbcL
Ordered Locus Names:MAE_47890
OrganismiMicrocystis aeruginosa (strain NIES-843)
Taxonomic identifieri449447 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesMicrocystis
ProteomesiUP000001510: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471Ribulose bisphosphate carboxylase large chainUniRule annotationPRO_0000355751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei197 – 1971N6-carboxylysine By similarity
Disulfide bondi243 – 243Interchain; in linked form By similarity

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 bond

Proteomic databases

PaxDbiB0JVL8.
PRIDEiB0JVL8.

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.

Protein-protein interaction databases

STRINGi449447.MAE_47890.

Structurei

3D structure databases

ProteinModelPortaliB0JVL8.
SMRiB0JVL8. Positions 8-465.

Family & Domainsi

Sequence similaritiesi

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.

B0JVL8-1 [UniParc]FASTAAdd to Basket

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MVQAKSKGFQ AGVKDYRLTY YTPDYTPKDT DLLACFRVTP QPGVPPEEAG    50
AAVAAESSTG TWTTVWTDNL TDLDRYKGRC YDIEPVPNED NQFFCFVAYP 100
LDLFEEGSVT NILTSIVGNV FGFKALRGLR LEDIRFPVAL IKTFQGPPHG 150
ITVERDKLNK YGRPLLGCTI KPKLGLSAKN YGRAVYECLR GGLDFTKDDE 200
NINSQPFMRW RDRFLFVQEA IVKSQAETNE VKGHYLNVTA PTCEQMMQRA 250
EFAAEIKTPI IMHDYLTGGF TANTTLAKFC RDKGLLLHIH RAMHAVIDRQ 300
KNHGIHFRVL AKCLRLSGGD HLHSGTVVGK LEGERGITMG FVDLMREDYV 350
EEDRARGIFF TQDYASLPGV MPVASGGIHV WHMPALVEIF GDDSCLQFGG 400
GTLGHPWGNA PGATANRVAL EACIQARNEG RSLAREGNDV IREACRWSPE 450
LAAACELWKE IKFEFEAMDT L 471
Length:471
Mass (Da):52,544
Last modified:March 18, 2008 - v1
Checksum:i0758222DD0F46B6C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009552 Genomic DNA. Translation: BAG04611.1.
RefSeqiYP_001659803.1. NC_010296.1.

Genome annotation databases

EnsemblBacteriaiBAG04611; BAG04611; MAE_47890.
GeneIDi5865621.
KEGGimar:MAE_47890.
PATRICi22634095. VBIMicAer59304_4356.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP009552 Genomic DNA. Translation: BAG04611.1 .
RefSeqi YP_001659803.1. NC_010296.1.

3D structure databases

ProteinModelPortali B0JVL8.
SMRi B0JVL8. Positions 8-465.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 449447.MAE_47890.

Proteomic databases

PaxDbi B0JVL8.
PRIDEi B0JVL8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAG04611 ; BAG04611 ; MAE_47890 .
GeneIDi 5865621.
KEGGi mar:MAE_47890.
PATRICi 22634095. VBIMicAer59304_4356.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci MAER449447:GHO8-4825-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NIES-843.

Entry informationi

Entry nameiRBL_MICAN
AccessioniPrimary (citable) accession number: B0JVL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: March 18, 2008
Last modified: May 14, 2014
This is version 42 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" By similarity.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi