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B5IH56

- B5IH56_ACIB4

UniProt

B5IH56 - B5IH56_ACIB4

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Protein

Ribulose bisphosphate carboxylase

Gene

rbcL

Organism
Aciduliprofundum boonei (strain DSM 19572 / T469)
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.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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei149 – 1491Proton acceptorUniRule annotation
Binding sitei151 – 1511SubstrateUniRule annotation
Metal bindingi175 – 1751Magnesium; via carbamate groupUniRule annotation
Metal bindingi177 – 1771MagnesiumUniRule annotation
Metal bindingi178 – 1781MagnesiumUniRule annotation
Active sitei265 – 2651Proton acceptorUniRule annotation
Binding sitei266 – 2661SubstrateUniRule annotation
Binding sitei298 – 2981SubstrateUniRule annotation
Sitei305 – 3051Transition state stabilizerUniRule annotation

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

LyaseUniRule annotationImported, OxidoreductaseUniRule annotation

Keywords - Biological processi

Carbon dioxide fixationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciABOO439481:GJNL-1119-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 annotation
Ordered Locus Names:Aboo_1084Imported
ORF Names:ABOONEI_952Imported
OrganismiAciduliprofundum boonei (strain DSM 19572 / T469)Imported
Taxonomic identifieri439481 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaAciduliprofundum
ProteomesiUP000001400: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei175 – 1751N6-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

Structurei

3D structure databases

ProteinModelPortaliB5IH56.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni347 – 3493Substrate bindingUniRule annotation
Regioni369 – 3724Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.
OMAiFTQDWAS.

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.

B5IH56-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTYIDLNYQP RESDLLVWFR AEPPAGKDMK YVADRIAEES SIGTWTDLKT
60 70 80 90 100
LLPEIWEKLR ARVYEIDEKN KYVKIAYPLH LFEIKNMPAI LASVAGNVFG
110 120 130 140 150
MKSVEALRVL DIRFPKELIQ GYLGPKYGVQ GVREMTKVYD RPFLGTIIKP
160 170 180 190 200
KIGLPAKMHA EVAYEAWVGG LDIVKDDENL ASQEFNRFEE RLALTLEKKD
210 220 230 240 250
IAEEETGEKK IYLVNITAPY KEMIRRAELV QDSGNEFVMI DVFISGFSAV
260 270 280 290 300
QSYREEGFKM AIHAHRAMHA AITRNPEHGI NMLTLAKVYR LLGVDNLHIG
310 320 330 340 350
TAVGKMEGSA KEVSEIREEI QLENVPANES RFEQKWYEIK PVLAVASGGL
360 370 380 390 400
HPGHVPAVVD ILGKDIVIQA GGGVHGHPEG TRAGAKAMRE ALEAKMQGIP
410 420
LEEYAKEHKE LREALEKFLH
Length:420
Mass (Da):47,364
Last modified:October 14, 2008 - v1
Checksum:iC8667540053F3B77
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001941 Genomic DNA. Translation: ADD08893.1.
DS990535 Genomic DNA. Translation: EDY34409.1.
RefSeqiWP_008086508.1. NZ_DS990535.1.
YP_003483455.1. NC_013926.1.

Genome annotation databases

EnsemblBacteriaiADD08893; ADD08893; Aboo_1084.
EDY34409; EDY34409; ABOONEI_952.
GeneIDi8828042.
KEGGiabi:Aboo_1084.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001941 Genomic DNA. Translation: ADD08893.1 .
DS990535 Genomic DNA. Translation: EDY34409.1 .
RefSeqi WP_008086508.1. NZ_DS990535.1.
YP_003483455.1. NC_013926.1.

3D structure databases

ProteinModelPortali B5IH56.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADD08893 ; ADD08893 ; Aboo_1084 .
EDY34409 ; EDY34409 ; ABOONEI_952 .
GeneIDi 8828042.
KEGGi abi:Aboo_1084.

Phylogenomic databases

HOGENOMi HOG000230831.
KOi K01601.
OMAi FTQDWAS.

Enzyme and pathway databases

BioCyci ABOO439481:GJNL-1119-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. "Electron microscopy encounters with unusual thermophiles helps direct genomic analysis of Aciduliprofundum boonei."
    Reysenbach A.L., Flores G.E.
    Geobiology 6:331-336(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: T469Imported.
  2. "Complete sequence of Aciduliprofundum boonei T469."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., Woyke T.
    Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: T469Imported.
  3. "Complete sequence of Aciduliprofundum boonei T469."
    Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L., Woyke T.
    Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 19572 / T469Imported.

Entry informationi

Entry nameiB5IH56_ACIB4
AccessioniPrimary (citable) accession number: B5IH56
Entry historyi
Integrated into UniProtKB/TrEMBL: October 14, 2008
Last sequence update: October 14, 2008
Last modified: October 29, 2014
This is version 41 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