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Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)
Status
Unreviewed-Annotation score: 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.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
Active sitei165 – 1651Proton acceptorUniRule annotation
Binding sitei167 – 1671SubstrateUniRule annotation
Metal bindingi191 – 1911Magnesium; via carbamate groupUniRule annotation
Metal bindingi193 – 1931MagnesiumUniRule annotation
Metal bindingi194 – 1941MagnesiumUniRule annotation
Active sitei283 – 2831Proton acceptorUniRule annotation
Binding sitei284 – 2841SubstrateUniRule annotation
Binding sitei316 – 3161SubstrateUniRule annotation
Sitei324 – 3241Transition state stabilizerUniRule annotation

GO - Molecular functioni

GO - Biological processi

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 lineageiArchaeaEuryarchaeotaHalobacteriaHaloferacalesHaloferacaceaeHaloferax
ProteomesiUP000006469 Componenti: Chromosome UP000027075 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

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

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni352 – 3543Substrate bindingUniRule annotation
Regioni374 – 3774Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

KOiK01601.
OMAiHAAFTRN.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01133. RuBisCO_L_type3.
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

        10         20         30         40         50
MGITYEDFLD LEYEPTDEDL VCTFRIDPAT GMSMEAAASR VASESSNGTW
60 70 80 90 100
AALQPGADFT DMGATTFSIA ERSSAGSQTG SDDIDGGNIQ VAYPAGLFEP
110 120 130 140 150
GNMPQVLSCI AGNIMGMKAV DSIRLMDCEW PEPVVSSYPG PLYGSSVREE
160 170 180 190 200
IFGVSDRPIT ATVPKPKVGL STAEHAQVGY DAWVGGVDLL KDDENLTDQD
210 220 230 240 250
FNPFADRLTE SLSLRDDAED ETGEKKSYLI NVTADTQTML DRVDEVAAQG
260 270 280 290 300
GEYVMVDIIT AGWASLQTVR ERTEKHGLAI HAHRAMHAAF DRMPTHGVSM
310 320 330 340 350
RVLAQISRLC GVDQLHTGTA GLGKLANEDT VGINDWLKGD LYGRNDVLPV
360 370 380 390 400
ASGGLHPGLL PDLLDATGTN TCIQLGGGIH GHPDGTRSGA IALRSAIDAY
410 420
VEGKSITEAA EETPELAVAL DKWGTETPR
Length:429
Mass (Da):45,707
Last modified:September 5, 2012 - v1
Checksum:iC183A31F88DEC184
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001868 Genomic DNA. Translation: AFK18685.1.
CP007551 Genomic DNA. Translation: AHZ21945.1.
AOLO01000006 Genomic DNA. Translation: EMA03454.1.
RefSeqiWP_004572703.1. NZ_AOLO01000006.1.
YP_006348672.1. NC_017941.2.

Genome annotation databases

EnsemblBacteriaiAFK18685; AFK18685; HFX_0967.
AHZ21945; AHZ21945; BM92_04375.
EMA03454; EMA03454; C439_05630.
GeneIDi13027133.
KEGGihme:HFX_0967.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001868 Genomic DNA. Translation: AFK18685.1.
CP007551 Genomic DNA. Translation: AHZ21945.1.
AOLO01000006 Genomic DNA. Translation: EMA03454.1.
RefSeqiWP_004572703.1. NZ_AOLO01000006.1.
YP_006348672.1. NC_017941.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFK18685; AFK18685; HFX_0967.
AHZ21945; AHZ21945; BM92_04375.
EMA03454; EMA03454; C439_05630.
GeneIDi13027133.
KEGGihme:HFX_0967.

Phylogenomic databases

KOiK01601.
OMAiHAAFTRN.

Enzyme and pathway databases

BioCyciHMED523841:GLDU-961-MONOMER.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01133. RuBisCO_L_type3.
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.
ProtoNetiSearch...

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-4Imported 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: June 24, 2015
This is version 28 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.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.