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Q31BY4

- RBL_PROM9

UniProt

Q31BY4 - RBL_PROM9

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, rbcL, PMT9312_0550
Organism
Prochlorococcus marinus (strain MIT 9312)
Status
Reviewed - Annotation score: 3 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 sitei115 – 1151Substrate; in homodimeric partner By similarity
Binding sitei165 – 1651Substrate By similarity
Active sitei167 – 1671Proton acceptor By similarity
Binding sitei169 – 1691Substrate By similarity
Metal bindingi193 – 1931Magnesium; via carbamate group By similarity
Metal bindingi195 – 1951Magnesium By similarity
Metal bindingi196 – 1961Magnesium By similarity
Active sitei286 – 2861Proton acceptor By similarity
Binding sitei287 – 2871Substrate By similarity
Binding sitei319 – 3191Substrate By similarity
Sitei326 – 3261Transition state stabilizer By similarity
Binding sitei371 – 3711Substrate 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

BioCyciPMAR74546:GHRG-569-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:PMT9312_0550
OrganismiProchlorococcus marinus (strain MIT 9312)
Taxonomic identifieri74546 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000002715: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 471471Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000251453Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei193 – 1931N6-carboxylysine By similarity

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains By similarity.

Protein-protein interaction databases

STRINGi74546.PMT9312_0550.

Structurei

3D structure databases

ProteinModelPortaliQ31BY4.
SMRiQ31BY4. Positions 15-459.

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.
InterProiIPR020888. 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.

Sequencei

Sequence statusi: Complete.

Q31BY4-1 [UniParc]FASTAAdd to Basket

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MSKKYDAGVK EYRDTYWTPE YVPLDTDLLA CFKCTGQEGV PREEVAAAVA    50
AESSTGTWST VWSELLTDLE FYKGRCYRIE DVPGDPEAFY AFIAYPLDLF 100
EEGSITNVLT SLVGNVFGFK ALRHLRLEDI RFPIAFIKTC GGPPNGIVVE 150
RDRLNKYGRP LLGCTIKPKL GLSGKNYGRV VYECLRGGLD LTKDDENINS 200
QPFQRWRERF EFVAEAVKLA QQETGEVKGH YLNCTANTPE ELYERAEFAK 250
ELDMPIIMHD YITGGFTANT GLANWCRKNG MLLHIHRAMH AVIDRHPKHG 300
IHFRVLAKCL RLSGGDQLHT GTVVGKLEGD RQTTLGYIDN LRESFVPEDR 350
SRGNFFDQDW GSMPGVFAVA SGGIHVWHMP ALLAIFGDDS CLQFGGGTHG 400
HPWGSAAGAA ANRVALEACV KARNAGREIE KESRDILMEA AKHSPELAIA 450
LETWKEIKFE FDTVDKLDVQ G 471
Length:471
Mass (Da):52,574
Last modified:December 6, 2005 - v1
Checksum:iF02490497AD6D2AD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000111 Genomic DNA. Translation: ABB49611.1.
RefSeqiYP_397047.1. NC_007577.1.

Genome annotation databases

EnsemblBacteriaiABB49611; ABB49611; PMT9312_0550.
GeneIDi3765349.
KEGGipmi:PMT9312_0550.
PATRICi23004778. VBIProMar70153_0570.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000111 Genomic DNA. Translation: ABB49611.1 .
RefSeqi YP_397047.1. NC_007577.1.

3D structure databases

ProteinModelPortali Q31BY4.
SMRi Q31BY4. Positions 15-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 74546.PMT9312_0550.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB49611 ; ABB49611 ; PMT9312_0550 .
GeneIDi 3765349.
KEGGi pmi:PMT9312_0550.
PATRICi 23004778. VBIProMar70153_0570.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci PMAR74546:GHRG-569-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 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.
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of Prochlorococcus marinus str. MIT 9312."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MIT 9312.

Entry informationi

Entry nameiRBL_PROM9
AccessioniPrimary (citable) accession number: Q31BY4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: December 6, 2005
Last modified: May 14, 2014
This is version 54 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

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