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.

Q7V6F8

- RBL_PROMM

UniProt

Q7V6F8 - RBL_PROMM

(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, PMT_1205
Organism
Prochlorococcus marinus (strain MIT 9313)
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

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:PMT_1205
OrganismiProchlorococcus marinus (strain MIT 9313)
Taxonomic identifieri74547 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001423: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 470470Ribulose bisphosphate carboxylase large chainUniRule annotationPRO_0000062638Add
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

STRINGi74547.PMT1205.

Structurei

3D structure databases

ProteinModelPortaliQ7V6F8.
SMRiQ7V6F8. Positions 15-459.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
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.

Q7V6F8-1 [UniParc]FASTAAdd to Basket

« Hide

MSKKYDAGVK EYRDTYWTPD 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
SRGNFFDQDW GSMPGVFAVA SGGIHVWHMP ALLAIFGDDS CLQFGGGTHG 400
HPWGSAAGAA ANRVALEACV KARNAGREIE KESRDILMEA AKHSPELAIA 450
LETWKEIKFE FDTVDKLDVQ 470
Length:470
Mass (Da):52,573
Last modified:October 1, 2003 - v1
Checksum:i341368654FDD59C3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX548175 Genomic DNA. Translation: CAE21380.1.
RefSeqiNP_895035.1. NC_005071.1.
WP_011130576.1. NC_005071.1.

Genome annotation databases

EnsemblBacteriaiCAE21380; CAE21380; PMT_1205.
GeneIDi1728877.
KEGGipmt:PMT1205.
PATRICi23010821. VBIProMar135351_1559.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX548175 Genomic DNA. Translation: CAE21380.1 .
RefSeqi NP_895035.1. NC_005071.1.
WP_011130576.1. NC_005071.1.

3D structure databases

ProteinModelPortali Q7V6F8.
SMRi Q7V6F8. Positions 15-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 74547.PMT1205.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE21380 ; CAE21380 ; PMT_1205 .
GeneIDi 1728877.
KEGGi pmt:PMT1205.
PATRICi 23010821. VBIProMar135351_1559.

Phylogenomic databases

eggNOGi COG1850.
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 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 9313.

Entry informationi

Entry nameiRBL_PROMM
AccessioniPrimary (citable) accession number: Q7V6F8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: October 1, 2003
Last modified: September 3, 2014
This is version 66 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