SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A9BEH3

- RBL_PROM4

UniProt

A9BEH3 - RBL_PROM4

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ribulose bisphosphate carboxylase large chain

Gene
cbbL, rbcL, P9211_05521
Organism
Prochlorococcus marinus (strain MIT 9211)
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

BioCyciPMAR93059:GHJV-571-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:P9211_05521
OrganismiProchlorococcus marinus (strain MIT 9211)
Taxonomic identifieri93059 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000000788: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Ribulose bisphosphate carboxylase large chainUniRule annotationPRO_1000142751Add
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

STRINGi93059.P9211_05521.

Structurei

3D structure databases

ProteinModelPortaliA9BEH3.
SMRiA9BEH3. 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.

A9BEH3-1 [UniParc]FASTAAdd to Basket

« Hide

MSKKYDAGVK EYRDTYWTPE YVPLDTDLLA CFKCTGQEGV PREEVAAAVA    50
AESSTGTWST VWSELLTDLE FYKGRCYRIE DVPGDKESFY AFIAYPLDLF 100
EEGSITNVLT SLVGNVFGFK ALRHLRLEDI RFPMAFIKTC GGPPNGIVVE 150
RDRLNKYGRP LLGCTIKPKL GLSGKNYGRV VYECLRGGLD LTKDDENINS 200
QPFQRWRERF EFVAEAVKLA QQETGEVKGH YLNCTATTPE EMYERAEFAK 250
ELDMPIIMHD YITGGFTANT GLANWCRKNG MLLHIHRAMH AVIDRHPKHG 300
IHFRVLAKCL RLSGGDQLHT GTVVGKLEGD RQTTLGYIDN LRESFVPEDR 350
TRGNFFDQDW GSMPGVFAVA SGGIHVWHMP ALLAIFGDDS CLQFGGGTHG 400
HPWGSAAGAA ANRVALEACV KARNAGREIE KESRDILMEA AKHSPELAIA 450
LETWKEIKFE FDTVDKLDVQ 470
Length:470
Mass (Da):52,601
Last modified:January 15, 2008 - v1
Checksum:i9590E77ECAE4F3F5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi5731046.
KEGGipmj:P9211_05521.
PATRICi22986598. VBIProMar136502_0582.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000878 Genomic DNA. Translation: ABX08483.1 .
RefSeqi WP_012195105.1. NC_009976.1.
YP_001550437.1. NC_009976.1.

3D structure databases

ProteinModelPortali A9BEH3.
SMRi A9BEH3. Positions 15-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 93059.P9211_05521.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX08483 ; ABX08483 ; P9211_05521 .
GeneIDi 5731046.
KEGGi pmj:P9211_05521.
PATRICi 22986598. VBIProMar136502_0582.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci PMAR93059:GHJV-571-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. 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: September 3, 2014
This is version 42 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