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I3R375

- I3R375_HALMT

UniProt

I3R375 - I3R375_HALMT

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Protein
Ribulose bisphosphate carboxylase
Gene
rbcL, HFX_0967, BM92_04375, C439_05630
Organism
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)
Status
Unreviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the addition of molecular CO2 and H2O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase 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
Active sitei165 – 1651Proton acceptor By similarityUniRule annotation
Binding sitei167 – 1671Substrate By similarityUniRule annotation
Metal bindingi191 – 1911Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi193 – 1931Magnesium By similarityUniRule annotation
Metal bindingi194 – 1941Magnesium By similarityUniRule annotation
Active sitei283 – 2831Proton acceptor By similarityUniRule annotation
Binding sitei284 – 2841Substrate By similarityUniRule annotation
Binding sitei316 – 3161Substrate By similarityUniRule annotation
Sitei324 – 3241Transition state stabilizer By similarityUniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. ribulose-bisphosphate carboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbon fixation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationImported, OxidoreductaseUniRule annotation

Keywords - Biological processi

Carbon dioxide fixationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciHMED523841:GLDU-961-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCOUniRule annotation
Gene namesi
Name:rbcLUniRule annotationImported
Ordered Locus Names:HFX_0967Imported
ORF Names:BM92_04375Imported, C439_05630Imported
OrganismiHaloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)Imported
Taxonomic identifieri523841 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloferax
ProteomesiUP000006469: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911N6-carboxylysine By similarityUniRule annotation

Interactioni

Subunit structurei

Homodimer or homodecamer. In contrast to form I RuBisCO, the form III RuBisCO is composed solely of large subunits By similarity.UniRule annotation

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni352 – 3543Substrate binding By similarityUniRule annotation
Regioni374 – 3774Substrate binding By similarityUniRule annotation

Sequence similaritiesi

Belongs to the RuBisCO large chain family.UniRule annotation

Phylogenomic databases

KOiK01601.
OMAiVIVTFRV.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
InterProiIPR017712. RuBisCO_III.
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.
TIGRFAMsiTIGR03326. rubisco_III. 1 hit.

Sequencei

Sequence statusi: Complete.

I3R375-1 [UniParc]FASTAAdd to Basket

« Hide

MGITYEDFLD LEYEPTDEDL VCTFRIDPAT GMSMEAAASR VASESSNGTW    50
AALQPGADFT DMGATTFSIA ERSSAGSQTG SDDIDGGNIQ VAYPAGLFEP 100
GNMPQVLSCI AGNIMGMKAV DSIRLMDCEW PEPVVSSYPG PLYGSSVREE 150
IFGVSDRPIT ATVPKPKVGL STAEHAQVGY DAWVGGVDLL KDDENLTDQD 200
FNPFADRLTE SLSLRDDAED ETGEKKSYLI NVTADTQTML DRVDEVAAQG 250
GEYVMVDIIT AGWASLQTVR ERTEKHGLAI HAHRAMHAAF DRMPTHGVSM 300
RVLAQISRLC GVDQLHTGTA GLGKLANEDT VGINDWLKGD LYGRNDVLPV 350
ASGGLHPGLL PDLLDATGTN TCIQLGGGIH GHPDGTRSGA IALRSAIDAY 400
VEGKSITEAA EETPELAVAL DKWGTETPR 429
Length:429
Mass (Da):45,707
Last modified:September 5, 2012 - v1
Checksum:iC183A31F88DEC184
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001868 Genomic DNA. Translation: AFK18685.1.
CP007551 Genomic DNA. Translation: AHZ21945.1.
AOLO01000006 Genomic DNA. Translation: EMA03454.1.
RefSeqiYP_006348672.1. NC_017941.1.

Genome annotation databases

EnsemblBacteriaiAFK18685; AFK18685; HFX_0967.
EMA03454; EMA03454; C439_05630.
GeneIDi13027133.
KEGGihme:HFX_0967.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001868 Genomic DNA. Translation: AFK18685.1 .
CP007551 Genomic DNA. Translation: AHZ21945.1 .
AOLO01000006 Genomic DNA. Translation: EMA03454.1 .
RefSeqi YP_006348672.1. NC_017941.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AFK18685 ; AFK18685 ; HFX_0967 .
EMA03454 ; EMA03454 ; C439_05630 .
GeneIDi 13027133.
KEGGi hme:HFX_0967.

Phylogenomic databases

KOi K01601.
OMAi VIVTFRV.

Enzyme and pathway databases

BioCyci HMED523841:GLDU-961-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
InterProi IPR017712. RuBisCO_III.
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.
TIGRFAMsi TIGR03326. rubisco_III. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the haloarchaeal phasin (PhaP) that functions in polyhydroxyalkanoate accumulation and granule formation in Haloferax mediterranei."
    Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.
    Appl. Environ. Microbiol. 78:1946-1952(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: CGMCC 1.2087Imported.
  2. "Complete genome sequence of the metabolically versatile halophilic archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-hydroxyvalerate) producer."
    Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y., Zhou J., Hu S., Xiang H.
    J. Bacteriol. 194:4463-4464(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4 and CGMCC 1.2087Imported.
  3. Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A., Eisen J.A., Facciotti M.T.
    Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC 33500Imported.
  4. "Transcriptional profiles of Haloferax mediterranei on the basis of nitrogen availability."
    Bautista V.
    Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC 33500Imported.
  5. Wang L., Yang H., Xiang H.
    Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: CGMCC 1.2087.

Entry informationi

Entry nameiI3R375_HALMT
AccessioniPrimary (citable) accession number: I3R375
Entry historyi
Integrated into UniProtKB/TrEMBL: September 5, 2012
Last sequence update: September 5, 2012
Last modified: September 3, 2014
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

Because the Archaea possessing a type III RuBisCO are all anaerobic, it is most likely that only the carboxylase activity of RuBisCO, and not the competitive oxygenase activity (by which RuBP reacts with O2 to form one molecule of 3-phosphoglycerate and one molecule of 2-phosphoglycolate), is biologically relevant in these strains By similarity.UniRule annotation

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi