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A1WVW0

- RBL_HALHL

UniProt

A1WVW0 - RBL_HALHL

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Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, Hhal_1046
Organism
Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1))
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. 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 sitei116 – 1161Substrate; in homodimeric partner By similarity
Binding sitei166 – 1661Substrate By similarity
Active sitei168 – 1681Proton acceptor By similarity
Binding sitei170 – 1701Substrate By similarity
Metal bindingi194 – 1941Magnesium; via carbamate group By similarity
Metal bindingi196 – 1961Magnesium By similarity
Metal bindingi197 – 1971Magnesium By similarity
Active sitei287 – 2871Proton acceptor By similarity
Binding sitei288 – 2881Substrate By similarity
Binding sitei320 – 3201Substrate By similarity
Sitei327 – 3271Transition state stabilizer By similarity
Binding sitei372 – 3721Substrate 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. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Monooxygenase, Oxidoreductase

Keywords - Biological processi

Calvin cycle, Carbon dioxide fixation

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciHHAL349124:GI3I-1080-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
Ordered Locus Names:Hhal_1046
OrganismiHalorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1))
Taxonomic identifieri349124 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeHalorhodospira
ProteomesiUP000000647: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Ribulose bisphosphate carboxylase large chainUniRule annotation
PRO_0000299963Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941N6-carboxylysine By similarity

Proteomic databases

PRIDEiA1WVW0.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi349124.Hhal_1046.

Structurei

3D structure databases

ProteinModelPortaliA1WVW0.
SMRiA1WVW0. Positions 16-460.

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.

A1WVW0-1 [UniParc]FASTAAdd to Basket

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MASKTYTAGV KDYRETYWEP DYKIKDSDLL AVFKVTPQPG VDREEAAAAV    50
AAESSTGTWT TVWTDLLTDL EHYKGRAYKV EDVPGDDEAF YAFIAYPIDL 100
FEEGSIVNVF TSLVGNVFGF KAVRALRLED VRFPLHFVMT CPGPPNGIQV 150
ERDKMNKYGR PLLGCTIKPK LGLSAKNYGR AVYECLRGGL DFTKDDENVN 200
SQPFMRWRDR FEFVMEAIQK AEEETGERKG HYLNVTAPTP EEMYKRAEFA 250
KELGAPIIMH DYITAGFCAH QGLANWCRDN GMLLHIHRAM HAVLDRNPNH 300
GIHFRVLTKI LRLMGGDQLH TGTVVGKLEG DRQSTLGWID LLRKPYIEED 350
RSRGLFFDQD WGAMPGAFAV ASGGIHVWHM PALLSIFGDD AVFQFGGGTL 400
GHPWGNAAGA AANRVALEAC VKARNEGREL EKEGKEILTE AAKSSPELKA 450
AMETWKEIKF EFDTVDKLDT AHR 473
Length:473
Mass (Da):52,990
Last modified:February 6, 2007 - v1
Checksum:i077A3134C8BE2B06
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000544 Genomic DNA. Translation: ABM61822.1.
RefSeqiWP_011813845.1. NC_008789.1.
YP_001002624.1. NC_008789.1.

Genome annotation databases

EnsemblBacteriaiABM61822; ABM61822; Hhal_1046.
GeneIDi4709802.
KEGGihha:Hhal_1046.
PATRICi22096399. VBIHalHal112047_1041.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000544 Genomic DNA. Translation: ABM61822.1 .
RefSeqi WP_011813845.1. NC_008789.1.
YP_001002624.1. NC_008789.1.

3D structure databases

ProteinModelPortali A1WVW0.
SMRi A1WVW0. Positions 16-460.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349124.Hhal_1046.

Proteomic databases

PRIDEi A1WVW0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM61822 ; ABM61822 ; Hhal_1046 .
GeneIDi 4709802.
KEGGi hha:Hhal_1046.
PATRICi 22096399. VBIHalHal112047_1041.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci HHAL349124:GI3I-1080-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 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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 244 / SL1.

Entry informationi

Entry nameiRBL_HALHL
AccessioniPrimary (citable) accession number: A1WVW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 2007
Last modified: September 3, 2014
This is version 50 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