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P00879

- RBL_NOSS1

UniProt

P00879 - RBL_NOSS1

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, rbc, rbcA, rbcL, alr1524
Organism
Nostoc sp. (strain PCC 7120 / UTEX 2576)
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 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
Complete GO annotation...

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

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:rbc, rbcA, rbcL
Ordered Locus Names:alr1524
OrganismiNostoc sp. (strain PCC 7120 / UTEX 2576)
Taxonomic identifieri103690 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
ProteomesiUP000002483: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 476476Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000062619Add
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

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 By similarity.

Protein-protein interaction databases

STRINGi103690.alr1524.

Structurei

3D structure databases

ProteinModelPortaliP00879.
SMRiP00879. Positions 13-470.

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.

P00879-1 [UniParc]FASTAAdd to Basket

« Hide

MSYAQTKTQT KSGYKAGVQD YRLTYYTPDY TPKDTDILAA FRVTPQPGVP    50
FEEAAAAVAA ESSTGTWTTV WTDLLTDLDR YKGRCYDIEP VPGEDNQFIA 100
YIAYPLDLFE EGSITNVLTS IVGNVFGFKA LRALRLEDIR FPVAYIKTFQ 150
GPPHGIQVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF 200
TKDDENINSA PFQRWRDRFL FVADAITKAQ AETGEIKGHY LNVTAPTCEE 250
MLKRAEYAKE LKQPIIMHDY LTAGFTANTT LARWCRDNGV LLHIHRAMHA 300
VIDRQKNHGI HFRVLAKALR LSGGDHIHTG TVVGKLEGER GITMGFVDLL 350
RENYVEQDKS RGIYFTQDWA SLPGVMAVAS GGIHVWHMPA LVEIFGDDSV 400
LQFGGGTLGH PWGNAPGATA NRVALEACVQ ARNEGRNLAR EGNDVIREAA 450
KWSPELAVAC ELWKEIKFEF EAMDTV 476
Length:476
Mass (Da):53,045
Last modified:January 23, 2002 - v3
Checksum:iABEDB246FA2E6A01
GO

Mass spectrometryi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911V → G in AAA22041. 1 Publication
Sequence conflicti91 – 911V → G in AAA22024. 1 Publication
Sequence conflicti91 – 911V → G in AAA22027. 1 Publication
Sequence conflicti91 – 911V → G in AAA22028. 1 Publication
Sequence conflicti98 – 981F → S in AAA22041. 1 Publication
Sequence conflicti98 – 981F → S in AAA22024. 1 Publication
Sequence conflicti98 – 981F → S in AAA22027. 1 Publication
Sequence conflicti98 – 981F → S in AAA22028. 1 Publication
Sequence conflicti120 – 1201S → Y in AAA22041. 1 Publication
Sequence conflicti120 – 1201S → Y in AAA22024. 1 Publication
Sequence conflicti120 – 1201S → Y in AAA22027. 1 Publication
Sequence conflicti120 – 1201S → Y in AAA22028. 1 Publication
Sequence conflicti127 – 1271G → V in AAA22041. 1 Publication
Sequence conflicti127 – 1271G → V in AAA22024. 1 Publication
Sequence conflicti127 – 1271G → V in AAA22027. 1 Publication
Sequence conflicti127 – 1271G → V in AAA22028. 1 Publication
Sequence conflicti279 – 2791T → N in AAA22041. 1 Publication
Sequence conflicti279 – 2791T → N in AAA22024. 1 Publication
Sequence conflicti279 – 2791T → N in AAA22027. 1 Publication
Sequence conflicti279 – 2791T → N in AAA22028. 1 Publication
Sequence conflicti290 – 2901V → L in AAA22041. 1 Publication
Sequence conflicti290 – 2901V → L in AAA22024. 1 Publication
Sequence conflicti290 – 2901V → L in AAA22027. 1 Publication
Sequence conflicti290 – 2901V → L in AAA22028. 1 Publication
Sequence conflicti399 – 3991S → F in AAA22041. 1 Publication
Sequence conflicti399 – 3991S → F in AAA22024. 1 Publication
Sequence conflicti399 – 3991S → F in AAA22027. 1 Publication
Sequence conflicti399 – 3991S → F in AAA22028. 1 Publication
Sequence conflicti416 – 4161P → R in AAA22041. 1 Publication
Sequence conflicti416 – 4161P → R in AAA22024. 1 Publication
Sequence conflicti416 – 4161P → R in AAA22027. 1 Publication
Sequence conflicti416 – 4161P → R in AAA22028. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
RefSeqiNP_485564.1. NC_003272.1.
WP_010995693.1. NC_003272.1.

Genome annotation databases

EnsemblBacteriaiBAB77890; BAB77890; BAB77890.
GeneIDi1105116.
KEGGiana:alr1524.
PATRICi22773054. VBINosSp37423_2010.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi A01099. RKAIL7.
AF1996.
RefSeqi NP_485564.1. NC_003272.1.
WP_010995693.1. NC_003272.1.

3D structure databases

ProteinModelPortali P00879.
SMRi P00879. Positions 13-470.
ModBasei Search...

Protein-protein interaction databases

STRINGi 103690.alr1524.

Proteomic databases

PRIDEi P00879.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB77890 ; BAB77890 ; BAB77890 .
GeneIDi 1105116.
KEGGi ana:alr1524.
PATRICi 22773054. VBINosSp37423_2010.

Phylogenomic databases

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

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. "Isolation and sequence of the gene for the large subunit of ribulose-1,5-bisphosphate carboxylase from the cyanobacterium Anabaena 7120."
    Curtis S.E., Haselkorn R.
    Proc. Natl. Acad. Sci. U.S.A. 80:1835-1839(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cotranscription of genes encoding the small and large subunits of ribulose-1,5-bisphosphate carboxylase in the cyanobacterium Anabaena 7120."
    Nierzwicki-Bauer S.A., Curtis S.E., Haselkorn R.
    Proc. Natl. Acad. Sci. U.S.A. 81:5961-5965(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 7120 / UTEX 2576.
  4. Singh H., Rajaram H., Apte S.K.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 16-22, MASS SPECTROMETRY.

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: September 3, 2014
This is version 109 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" By similarity.

Keywords - Technical termi

Complete proteome, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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