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Q8THG2

- RBL_METAC

UniProt

Q8THG2 - RBL_METAC

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Protein
Ribulose bisphosphate carboxylase
Gene
rbcL, MA_4555
Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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

Enzyme regulationi

Reversibly inhibited by O2.UniRule annotation

Temperature dependencei

Active from 25 to 40 degrees Celsius.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

BioCyciMACE188937:GI2O-4613-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:MA_4555
OrganismiMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Taxonomic identifieri188937 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
ProteomesiUP000002487: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 428428Ribulose bisphosphate carboxylaseUniRule annotation
PRO_0000062672Add
BLAST

Amino acid modifications

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

Proteomic databases

PRIDEiQ8THG2.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi188937.MA4555.

Structurei

3D structure databases

ProteinModelPortaliQ8THG2.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1850.
KOiK01601.
OMAiFTQDWAS.
PhylomeDBiQ8THG2.

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.

Q8THG2-1 [UniParc]FASTAAdd to Basket

« Hide

MRRDYVDPGY SPKDTDLICE FHIEPAAGIS FEEASTHMAG ESSIDSWTEI    50
STLSPELAAR LKPHVFYLDA DTQTVRVAYS EDLFELGSVP QVLSAVAGNI 100
FSMKIVDNLR LQDITFPKSM LREFEGPNFG LPGVRDIVGV KDRPLVGTIV 150
KPKVGLTSEM HAEVAYNAFA GGCDLVKDDE NLTDQKFNGF EKRAELTLKI 200
AEKAEAETGE RKMYLCNITA PTCEEMIRRL HVLKDLGASY AMIDIVPTGW 250
TALQTLREAA ADEGLALHAH RCMHSAFTRN PRHGVSMLLV AKLCRLIGLD 300
QLHIGTVVGK MHGDKDEVLS IRDECVLDTV PADPEQHVLA QDWGGLKPMF 350
PVASGGLAPT MIPDLYSIFG KEVIMQFGGG IHAHPMGTAA GAAACRQALE 400
ASLEGISLQD YAKDHKELEA ALGKWLEK 428
Length:428
Mass (Da):46,787
Last modified:June 1, 2002 - v1
Checksum:iB03BFCBD9E8AFED5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE010299 Genomic DNA. Translation: AAM07894.1.
RefSeqiNP_619414.1. NC_003552.1.

Genome annotation databases

EnsemblBacteriaiAAM07894; AAM07894; MA_4555.
GeneIDi1476449.
KEGGimac:MA4555.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE010299 Genomic DNA. Translation: AAM07894.1 .
RefSeqi NP_619414.1. NC_003552.1.

3D structure databases

ProteinModelPortali Q8THG2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 188937.MA4555.

Proteomic databases

PRIDEi Q8THG2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM07894 ; AAM07894 ; MA_4555 .
GeneIDi 1476449.
KEGGi mac:MA4555.

Phylogenomic databases

eggNOGi COG1850.
KOi K01601.
OMAi FTQDWAS.
PhylomeDBi Q8THG2.

Enzyme and pathway databases

BioCyci MACE188937:GI2O-4613-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

« Hide 'large scale' publications
  1. "The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity."
    Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.
    , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B.
    Genome Res. 12:532-542(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.
  2. "Synthesis of catalytically active form III ribulose 1,5-bisphosphate carboxylase/oxygenase in archaea."
    Finn M.W., Tabita F.R.
    J. Bacteriol. 185:3049-3059(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.

Entry informationi

Entry nameiRBL_METAC
AccessioniPrimary (citable) accession number: Q8THG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: June 1, 2002
Last modified: September 3, 2014
This is version 86 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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