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Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Prochlorococcus marinus (strain MIT 9211)
Status
Reviewed-Annotation score: 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.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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei115 – 1151Substrate; in homodimeric partnerUniRule annotation
Binding sitei165 – 1651SubstrateUniRule annotation
Active sitei167 – 1671Proton acceptorUniRule annotation
Binding sitei169 – 1691SubstrateUniRule annotation
Metal bindingi193 – 1931Magnesium; via carbamate groupUniRule annotation
Metal bindingi195 – 1951MagnesiumUniRule annotation
Metal bindingi196 – 1961MagnesiumUniRule annotation
Active sitei286 – 2861Proton acceptorUniRule annotation
Binding sitei287 – 2871SubstrateUniRule annotation
Binding sitei319 – 3191SubstrateUniRule annotation
Sitei326 – 3261Transition state stabilizerUniRule annotation
Binding sitei371 – 3711SubstrateUniRule annotation

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

Enzyme and pathway databases

BioCyciPMAR93059:GHJV-571-MONOMER.

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:rbcLUniRule annotation
Ordered Locus Names:P9211_05521
OrganismiProchlorococcus marinus (strain MIT 9211)
Taxonomic identifieri93059 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000000788 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Ribulose bisphosphate carboxylase large chainPRO_1000142751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei193 – 1931N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains.UniRule annotation

Protein-protein interaction databases

STRINGi93059.P9211_05521.

Structurei

3D structure databases

ProteinModelPortaliA9BEH3.
SMRiA9BEH3. Positions 15-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.
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.

A9BEH3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKKYDAGVK EYRDTYWTPE YVPLDTDLLA CFKCTGQEGV PREEVAAAVA
60 70 80 90 100
AESSTGTWST VWSELLTDLE FYKGRCYRIE DVPGDKESFY AFIAYPLDLF
110 120 130 140 150
EEGSITNVLT SLVGNVFGFK ALRHLRLEDI RFPMAFIKTC GGPPNGIVVE
160 170 180 190 200
RDRLNKYGRP LLGCTIKPKL GLSGKNYGRV VYECLRGGLD LTKDDENINS
210 220 230 240 250
QPFQRWRERF EFVAEAVKLA QQETGEVKGH YLNCTATTPE EMYERAEFAK
260 270 280 290 300
ELDMPIIMHD YITGGFTANT GLANWCRKNG MLLHIHRAMH AVIDRHPKHG
310 320 330 340 350
IHFRVLAKCL RLSGGDQLHT GTVVGKLEGD RQTTLGYIDN LRESFVPEDR
360 370 380 390 400
TRGNFFDQDW GSMPGVFAVA SGGIHVWHMP ALLAIFGDDS CLQFGGGTHG
410 420 430 440 450
HPWGSAAGAA ANRVALEACV KARNAGREIE KESRDILMEA AKHSPELAIA
460 470
LETWKEIKFE FDTVDKLDVQ
Length:470
Mass (Da):52,601
Last modified:January 15, 2008 - v1
Checksum:i9590E77ECAE4F3F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000878 Genomic DNA. Translation: ABX08483.1.
RefSeqiWP_012195105.1. NC_009976.1.
YP_001550437.1. NC_009976.1.

Genome annotation databases

EnsemblBacteriaiABX08483; ABX08483; P9211_05521.
KEGGipmj:P9211_05521.
PATRICi22986598. VBIProMar136502_0582.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000878 Genomic DNA. Translation: ABX08483.1.
RefSeqiWP_012195105.1. NC_009976.1.
YP_001550437.1. NC_009976.1.

3D structure databases

ProteinModelPortaliA9BEH3.
SMRiA9BEH3. Positions 15-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93059.P9211_05521.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX08483; ABX08483; P9211_05521.
KEGGipmj:P9211_05521.
PATRICi22986598. VBIProMar136502_0582.

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiHAAFTRN.
OrthoDBiEOG6ZKXMS.

Enzyme and pathway databases

BioCyciPMAR93059:GHJV-571-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MIT 9211.

Entry informationi

Entry nameiRBL_PROM4
AccessioniPrimary (citable) accession number: A9BEH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 15, 2008
Last modified: April 1, 2015
This is version 46 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".UniRule annotation

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.