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Q44176

- RBL_SYNP2

UniProt

Q44176 - RBL_SYNP2

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Protein

Ribulose bisphosphate carboxylase large chain

Gene
cbbL, rbcL, SYNPCC7002_A1798
Organism
Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum)
Status
Reviewed - 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 sitei118 – 1181Substrate; in homodimeric partner By similarity
Binding sitei168 – 1681Substrate By similarity
Active sitei170 – 1701Proton acceptor By similarity
Binding sitei172 – 1721Substrate By similarity
Metal bindingi196 – 1961Magnesium; via carbamate group By similarity
Metal bindingi198 – 1981Magnesium By similarity
Metal bindingi199 – 1991Magnesium By similarity
Active sitei289 – 2891Proton acceptor By similarity
Binding sitei290 – 2901Substrate By similarity
Binding sitei322 – 3221Substrate By similarity
Sitei329 – 3291Transition state stabilizer By similarity
Binding sitei374 – 3741Substrate 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

BioCyciSSP32049:GKF7-1799-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:SYNPCC7002_A1798
OrganismiSynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum)
Taxonomic identifieri32049 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001688: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Ribulose bisphosphate carboxylase large chainUniRule annotationPRO_0000062650Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei196 – 1961N6-carboxylysine By similarity
Disulfide bondi242 – 242Interchain; 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

PRIDEiQ44176.

PTM databases

PhosSiteiP13051899.

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

STRINGi32049.SYNPCC7002_A1798.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PEMX-ray2.95R459-465[»]
ProteinModelPortaliQ44176.
SMRiQ44176. Positions 5-470.

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.

Q44176-1 [UniParc]FASTAAdd to Basket

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MQTKSAGFNA GVQDYRLTYY TPDYTPKDTD LLACFRMTPQ PGVPPEECAA    50
AVAAESSTGT WTTVWTDGLT DLDRYKGRCY NVEPVPGEDN QYFCFVAYPL 100
DLFEEGSVTN VLTSLVGNVF GFKALRALRL EDIRFPVALI KTYQGPPHGI 150
TVERDLLNKY GRPLLGCTIK PKLGLSAKNY GRAVYECLRG GLDFTKDDEN 200
INSQPFMRWR DRFLFVQEAI EKSQAETNEV KGHYLNVTAG TCEEMLKRAE 250
FAKEIGTPII MHDFLTGGFT ANTTLAKWCR DNGVLLHIHR AMHAVIDRQK 300
NHGIHFRVLA KCLRLSGGDH LHSGTVVGKL EGDRAATLGF VDLMREDYVE 350
EDRSRGVFFT QDYASLPGTM PVASGGIHVW HMPALVEIFG DDSCLQFGGG 400
TLGHPWGNAP GATANRVALE ACVQARNEGR SLAREGNDVL REAGKWSPEL 450
AAALDLWKEI KFEFDTVDTL 470
Length:470
Mass (Da):52,159
Last modified:July 1, 1997 - v2
Checksum:i7D43456FD17D9775
GO

Sequence cautioni

The sequence ACA99786.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D13971 Genomic DNA. Translation: BAA03076.1.
CP000951 Genomic DNA. Translation: ACA99786.1. Different initiation.
RefSeqiWP_012307409.1. NC_010475.1.
YP_001735042.1. NC_010475.1.

Genome annotation databases

EnsemblBacteriaiACA99786; ACA99786; SYNPCC7002_A1798.
GeneIDi6056494.
KEGGisyp:SYNPCC7002_A1798.
PATRICi23818226. VBISynSp37135_2054.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D13971 Genomic DNA. Translation: BAA03076.1 .
CP000951 Genomic DNA. Translation: ACA99786.1 . Different initiation.
RefSeqi WP_012307409.1. NC_010475.1.
YP_001735042.1. NC_010475.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2PEM X-ray 2.95 R 459-465 [» ]
ProteinModelPortali Q44176.
SMRi Q44176. Positions 5-470.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 32049.SYNPCC7002_A1798.

PTM databases

PhosSitei P13051899.

Proteomic databases

PRIDEi Q44176.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACA99786 ; ACA99786 ; SYNPCC7002_A1798 .
GeneIDi 6056494.
KEGGi syp:SYNPCC7002_A1798.
PATRICi 23818226. VBISynSp37135_2054.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SSP32049:GKF7-1799-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

« Hide 'large scale' publications
  1. "Cloning and characterization of RubisCO large subunit and small subunit from Synechococcus sp. PCC7002."
    Akiyama H., Kanai S., Hirano M., Sugimoto M., Kiyohara M.
    Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequence of Synechococcus sp. PCC 7002."
    Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.
    Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27264 / PCC 7002 / PR-6.

Entry informationi

Entry nameiRBL_SYNP2
AccessioniPrimary (citable) accession number: Q44176
Secondary accession number(s): B1XPS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: September 3, 2014
This is version 86 of the entry and version 2 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

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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