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B0CCC1

- RBL_ACAM1

UniProt

B0CCC1 - RBL_ACAM1

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, rbcL, AM1_1785
Organism
Acaryochloris marina (strain MBIC 11017)
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 sitei124 – 1241Substrate; in homodimeric partner By similarity
Binding sitei174 – 1741Substrate By similarity
Active sitei176 – 1761Proton acceptor By similarity
Binding sitei178 – 1781Substrate By similarity
Metal bindingi202 – 2021Magnesium; via carbamate group By similarity
Metal bindingi204 – 2041Magnesium By similarity
Metal bindingi205 – 2051Magnesium By similarity
Active sitei295 – 2951Proton acceptor By similarity
Binding sitei296 – 2961Substrate By similarity
Binding sitei328 – 3281Substrate By similarity
Sitei335 – 3351Transition state stabilizer By similarity
Binding sitei380 – 3801Substrate 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

BioCyciAMAR329726:GCZJ-1776-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:AM1_1785
OrganismiAcaryochloris marina (strain MBIC 11017)
Taxonomic identifieri329726 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesAcaryochloris
ProteomesiUP000000268: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 476476Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_1000142747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-carboxylysine By similarity
Disulfide bondi248 – 248Interchain; 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

PRIDEiB0CCC1.

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

STRINGi329726.AM1_1785.

Structurei

3D structure databases

ProteinModelPortaliB0CCC1.
SMRiB0CCC1. Positions 10-476.

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.

B0CCC1-1 [UniParc]FASTAAdd to Basket

« Hide

MSYSQTRTQS KAGYDAGVKD YKLTYYTPDY TPKDTDILAA FRMTPQPGVP    50
PEEAGAAVAA ESSTGTWTTV WTDLLTDLDR YKGRCYDIEA VANEDNQYIA 100
YIAYPLDLFE EGSVVNLLTS LVGNVFGFKA LRALRLEDIR IPVAYMKTFQ 150
GPPHGITVER DKINKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF 200
TKDDENINSQ PFMRWRDRFL FVAEAIHKAQ AETGEIKGHY LNVTAATCEE 250
MLKRAEFAKE LEMPIIMHDF ITGGFTANTT LSHWCRDNGV LLHIHRAMHA 300
VIDRQKNHGM HFRVLSKCLR MSGGDHIHTG TVVGKLEGEK GITMGFVDLL 350
RENYVEKDLS RGIYFTQDWA SMGGVMAVAS GGIHVWHMPA LVEIFGDDSV 400
LQFGGGTLGH PWGCAPGATA NRVALEACVQ ARNEGRDMAR EGGDILREAA 450
KWSPELAVAL EVWKEIKFEF EAMDTV 476
Length:476
Mass (Da):52,981
Last modified:February 26, 2008 - v1
Checksum:i4991C37529C5BBC1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000828 Genomic DNA. Translation: ABW26806.1.
RefSeqiYP_001516120.1. NC_009925.1.

Genome annotation databases

EnsemblBacteriaiABW26806; ABW26806; AM1_1785.
GeneIDi5680601.
KEGGiamr:AM1_1785.
PATRICi20617942. VBIAcaMar40141_1609.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000828 Genomic DNA. Translation: ABW26806.1 .
RefSeqi YP_001516120.1. NC_009925.1.

3D structure databases

ProteinModelPortali B0CCC1.
SMRi B0CCC1. Positions 10-476.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 329726.AM1_1785.

Proteomic databases

PRIDEi B0CCC1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABW26806 ; ABW26806 ; AM1_1785 .
GeneIDi 5680601.
KEGGi amr:AM1_1785.
PATRICi 20617942. VBIAcaMar40141_1609.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci AMAR329726:GCZJ-1776-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: MBIC 11017.

Entry informationi

Entry nameiRBL_ACAM1
AccessioniPrimary (citable) accession number: B0CCC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 26, 2008
Last modified: May 14, 2014
This is version 41 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