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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Status
Reviewed-Annotation score: 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.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

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei124Substrate; in homodimeric partnerUniRule annotation1
Binding sitei174SubstrateUniRule annotation1
Active sitei176Proton acceptorUniRule annotation1
Binding sitei178SubstrateUniRule annotation1
Metal bindingi202Magnesium; via carbamate groupUniRule annotation1
Metal bindingi204MagnesiumUniRule annotation1
Metal bindingi205MagnesiumUniRule annotation1
Active sitei295Proton acceptorUniRule annotation1
Binding sitei296SubstrateUniRule annotation1
Binding sitei328SubstrateUniRule annotation1
Sitei335Transition state stabilizerUniRule annotation1
Binding sitei380SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation, Photorespiration, Photosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

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:rbc, rbcA, rbcLUniRule annotation
Ordered Locus Names:alr1524
OrganismiNostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Taxonomic identifieri103690 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
Proteomesi
  • UP000002483 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000626191 – 476Ribulose bisphosphate carboxylase large chainAdd BLAST476

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei202N6-carboxylysineUniRule annotation1
Disulfide bondi248Interchain; 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 bond

Proteomic databases

PRIDEiP00879.

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

STRINGi103690.alr1524.

Structurei

3D structure databases

ProteinModelPortaliP00879.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RuBisCO large chain family. Type I subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
OrthoDBiPOG091H14UZ.

Family and domain databases

CDDicd08212. RuBisCO_large_I. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[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.

P00879-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSYAQTKTQT KSGYKAGVQD YRLTYYTPDY TPKDTDILAA FRVTPQPGVP
60 70 80 90 100
FEEAAAAVAA ESSTGTWTTV WTDLLTDLDR YKGRCYDIEP VPGEDNQFIA
110 120 130 140 150
YIAYPLDLFE EGSITNVLTS IVGNVFGFKA LRALRLEDIR FPVAYIKTFQ
160 170 180 190 200
GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF
210 220 230 240 250
TKDDENINSA PFQRWRDRFL FVADAITKAQ AETGEIKGHY LNVTAPTCEE
260 270 280 290 300
MLKRAEYAKE LKQPIIMHDY LTAGFTANTT LARWCRDNGV LLHIHRAMHA
310 320 330 340 350
VIDRQKNHGI HFRVLAKALR LSGGDHIHTG TVVGKLEGER GITMGFVDLL
360 370 380 390 400
RENYVEQDKS RGIYFTQDWA SLPGVMAVAS GGIHVWHMPA LVEIFGDDSV
410 420 430 440 450
LQFGGGTLGH PWGNAPGATA NRVALEACVQ ARNEGRNLAR EGNDVIREAA
460 470
KWSPELAVAC ELWKEIKFEF EAMDTV
Length:476
Mass (Da):53,045
Last modified:January 23, 2002 - v3
Checksum:iABEDB246FA2E6A01
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti91V → G in AAA22041 (PubMed:16593300).Curated1
Sequence conflicti91V → G in AAA22024 (PubMed:6091125).Curated1
Sequence conflicti91V → G in AAA22027 (PubMed:6091125).Curated1
Sequence conflicti91V → G in AAA22028 (PubMed:6091125).Curated1
Sequence conflicti98F → S in AAA22041 (PubMed:16593300).Curated1
Sequence conflicti98F → S in AAA22024 (PubMed:6091125).Curated1
Sequence conflicti98F → S in AAA22027 (PubMed:6091125).Curated1
Sequence conflicti98F → S in AAA22028 (PubMed:6091125).Curated1
Sequence conflicti120S → Y in AAA22041 (PubMed:16593300).Curated1
Sequence conflicti120S → Y in AAA22024 (PubMed:6091125).Curated1
Sequence conflicti120S → Y in AAA22027 (PubMed:6091125).Curated1
Sequence conflicti120S → Y in AAA22028 (PubMed:6091125).Curated1
Sequence conflicti127G → V in AAA22041 (PubMed:16593300).Curated1
Sequence conflicti127G → V in AAA22024 (PubMed:6091125).Curated1
Sequence conflicti127G → V in AAA22027 (PubMed:6091125).Curated1
Sequence conflicti127G → V in AAA22028 (PubMed:6091125).Curated1
Sequence conflicti279T → N in AAA22041 (PubMed:16593300).Curated1
Sequence conflicti279T → N in AAA22024 (PubMed:6091125).Curated1
Sequence conflicti279T → N in AAA22027 (PubMed:6091125).Curated1
Sequence conflicti279T → N in AAA22028 (PubMed:6091125).Curated1
Sequence conflicti290V → L in AAA22041 (PubMed:16593300).Curated1
Sequence conflicti290V → L in AAA22024 (PubMed:6091125).Curated1
Sequence conflicti290V → L in AAA22027 (PubMed:6091125).Curated1
Sequence conflicti290V → L in AAA22028 (PubMed:6091125).Curated1
Sequence conflicti399S → F in AAA22041 (PubMed:16593300).Curated1
Sequence conflicti399S → F in AAA22024 (PubMed:6091125).Curated1
Sequence conflicti399S → F in AAA22027 (PubMed:6091125).Curated1
Sequence conflicti399S → F in AAA22028 (PubMed:6091125).Curated1
Sequence conflicti416P → R in AAA22041 (PubMed:16593300).Curated1
Sequence conflicti416P → R in AAA22024 (PubMed:6091125).Curated1
Sequence conflicti416P → R in AAA22027 (PubMed:6091125).Curated1
Sequence conflicti416P → R in AAA22028 (PubMed:6091125).Curated1

Mass spectrometryi

Molecular mass is 53411 Da from positions 1 - 476. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01540 Genomic DNA. Translation: AAA22041.1.
L02520 Genomic DNA. Translation: AAA22024.1.
L02521 Genomic DNA. Translation: AAA22027.1.
L02522 Genomic DNA. Translation: AAA22028.1.
BA000019 Genomic DNA. Translation: BAB77890.1.
PIRiA01099. RKAIL7.
AF1996.
RefSeqiWP_010995693.1. NC_003272.1.

Genome annotation databases

EnsemblBacteriaiBAB77890; BAB77890; BAB77890.
KEGGiana:alr1524.
PATRICi22773054. VBINosSp37423_2010.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01540 Genomic DNA. Translation: AAA22041.1.
L02520 Genomic DNA. Translation: AAA22024.1.
L02521 Genomic DNA. Translation: AAA22027.1.
L02522 Genomic DNA. Translation: AAA22028.1.
BA000019 Genomic DNA. Translation: BAB77890.1.
PIRiA01099. RKAIL7.
AF1996.
RefSeqiWP_010995693.1. NC_003272.1.

3D structure databases

ProteinModelPortaliP00879.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi103690.alr1524.

Proteomic databases

PRIDEiP00879.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB77890; BAB77890; BAB77890.
KEGGiana:alr1524.
PATRICi22773054. VBINosSp37423_2010.

Phylogenomic databases

eggNOGiENOG4105DT1. Bacteria.
COG1850. LUCA.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.
OrthoDBiPOG091H14UZ.

Family and domain databases

CDDicd08212. RuBisCO_large_I. 1 hit.
Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1. 1 hit.
InterProiIPR033966. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR020888. RuBisCO_lsuI.
[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]
ProtoNetiSearch...

Entry informationi

Entry nameiRBL_NOSS1
AccessioniPrimary (citable) accession number: P00879
Secondary accession number(s): Q60124
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2002
Last modified: November 30, 2016
This is version 122 of the entry and version 3 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".UniRule annotation

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.