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Q8PXG9

- RBL_METMA

UniProt

Q8PXG9 - RBL_METMA

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Protein

Ribulose bisphosphate carboxylase

Gene
rbcL, MM_1249
Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Status
Reviewed - 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 sitei151 – 1511Proton acceptor By similarity
Binding sitei153 – 1531Substrate By similarity
Metal bindingi177 – 1771Magnesium; via carbamate group By similarity
Metal bindingi179 – 1791Magnesium By similarity
Metal bindingi180 – 1801Magnesium By similarity
Active sitei270 – 2701Proton acceptor By similarity
Binding sitei271 – 2711Substrate By similarity
Binding sitei303 – 3031Substrate By similarity
Sitei310 – 3101Transition state stabilizer By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. oxidoreductase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. AMP catabolic process Source: UniProtKB-HAMAP
  2. carbon fixation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Oxidoreductase

Keywords - Biological processi

Carbon dioxide fixation

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMMAZ192952:GCK2-1279-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase (EC:4.1.1.39)
Short name:
RuBisCO
Gene namesi
Name:rbcL
Ordered Locus Names:MM_1249
OrganismiMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Taxonomic identifieri192952 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
ProteomesiUP000000595: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Ribulose bisphosphate carboxylaseUniRule annotationPRO_0000062674Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei177 – 1771N6-carboxylysine By similarity

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi192952.MM_1249.

Structurei

3D structure databases

ProteinModelPortaliQ8PXG9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni354 – 3563Substrate binding By similarity
Regioni376 – 3794Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.

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.

Q8PXG9-1 [UniParc]FASTAAdd to Basket

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MRRDYIDIGY SPKETDLVCE FHIEPTAGVN FEEAATHLAG ESSIDSWTEI    50
ATLSPELAEK LKPHVFYADE GAQTVRVAYS EELFELGSVP QVLSAVAGNI 100
LSMKIVDNVR LQDIAFPKSM INEFKGPNFG LPGIRKLVGV QDRPLIGTIV 150
KPKVGLNSEK HAEVAYNSFV GGCDLVKDDE NLSDQKFNSF EKRAELTLKL 200
AEKAESETGE KKMYLCNVTA PTCREMIRRM NFLKDLGASY VMVDIVPAGW 250
TAIQTLREEA EDAGLALHAH RCMHSAYTRN PRHGISMLVV AKLCRLIGLD 300
QLHIGTVVGK MHGEKHEVLN LRDQCVLDKV PADESQHILA QDWRGLKPMF 350
PVASGGLAPT MIPDLYSIFG KDVIMQFGGG IHAHPMGTVA GATACRQALE 400
ASLEGISLQD YAKNHKELET ALGKWLKK 428
Length:428
Mass (Da):47,138
Last modified:October 1, 2002 - v1
Checksum:i89262149EDB15A12
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE008384 Genomic DNA. Translation: AAM30945.1.
RefSeqiNP_633273.1. NC_003901.1.
WP_011033198.1. NC_003901.1.

Genome annotation databases

EnsemblBacteriaiAAM30945; AAM30945; MM_1249.
GeneIDi1479591.
KEGGimma:MM_1249.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE008384 Genomic DNA. Translation: AAM30945.1 .
RefSeqi NP_633273.1. NC_003901.1.
WP_011033198.1. NC_003901.1.

3D structure databases

ProteinModelPortali Q8PXG9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 192952.MM_1249.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM30945 ; AAM30945 ; MM_1249 .
GeneIDi 1479591.
KEGGi mma:MM_1249.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci MMAZ192952:GCK2-1279-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01133. RuBisCO_L_type3.
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

  1. "The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
    Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R.
    , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
    J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Entry informationi

Entry nameiRBL_METMA
AccessioniPrimary (citable) accession number: Q8PXG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: October 1, 2002
Last modified: September 3, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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.

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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