Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

D6CTT0

- D6CTT0_THIA3

UniProt

D6CTT0 - D6CTT0_THIA3

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ribulose bisphosphate carboxylase

Gene

cbbM

Organism
Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site.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

Note: Binds 1 magnesium ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei113 – 1131Substrate; in homodimeric partnerUniRule annotation
Active sitei168 – 1681Proton acceptorUniRule annotation
Binding sitei170 – 1701SubstrateUniRule annotation
Metal bindingi193 – 1931Magnesium; via carbamate groupUniRule annotation
Metal bindingi195 – 1951MagnesiumUniRule annotation
Metal bindingi196 – 1961MagnesiumUniRule annotation
Active sitei289 – 2891Proton acceptorUniRule annotation
Binding sitei290 – 2901SubstrateUniRule annotation
Binding sitei323 – 3231SubstrateUniRule annotation
Sitei331 – 3311Transition state stabilizerUniRule annotation
Binding sitei370 – 3701SubstrateUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationImported, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciTARS426114-WGS:GSYJ-1952-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylaseUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCOUniRule annotation
Gene namesi
Name:cbbMUniRule annotationImported
Ordered Locus Names:THI_2041Imported
OrganismiThiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As)Imported
Taxonomic identifieri426114 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesThiomonas
ProteomesiUP000002372: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei193 – 1931N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliD6CTT0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000230831.
KOiK01601.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01339. RuBisCO_L_type2.
InterProiIPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
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.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D6CTT0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAHDQSSRYA NLDLKESDLI AGGKHILVAY KMKPKAGYDY LATAAHFAAE
60 70 80 90 100
SSTGTNVEVS TTDDFTKGVD ALVYFIDEAT EDMRIAYPIE LFDRNVIDGR
110 120 130 140 150
FMIVSFLTLV IGNNQGMGDV EYGKMIDFYV PERAIQMFDG PATDISNLWR
160 170 180 190 200
ILGRPIKDGG YIAGTIIKPK LGLRPEPFAQ AAYQFWLGGD FIKNDEPQGN
210 220 230 240 250
QVFAPVKKVI PLVYDAMKRA QDETGEAKLF SMNITADDYH EMCARADFAL
260 270 280 290 300
EVFGPDADKL AFLVDGYVGG PGMVTTARRQ YPNQYLHYHR AGHGAITSPS
310 320 330 340 350
SKRGYTAFVL AKMSRLQGAS GIHVGTMGYG KMEGEGDDRN IAYMIERDEC
360 370 380 390 400
QGPVYYQKWY GMKPTTPIIS GGMNALRLPG FFENLGHGNV INTAGGGSYG
410 420 430 440 450
HIDSPAAGAK SLRQAYECWK AGADPIEYAK EHIEFARAFE SFPGDADKLF
460
PGWRDKLGVH K
Length:461
Mass (Da):50,819
Last modified:July 13, 2010 - v1
Checksum:i15B9E0F51FEAA8D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FP475956 Genomic DNA. Translation: CAZ88699.1.
RefSeqiWP_013106007.1. NC_014145.1.
YP_003624515.1. NC_014145.1.

Genome annotation databases

EnsemblBacteriaiCAZ88699; CAZ88699; THI_2041.
GeneIDi13879779.
KEGGithi:THI_2041.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FP475956 Genomic DNA. Translation: CAZ88699.1 .
RefSeqi WP_013106007.1. NC_014145.1.
YP_003624515.1. NC_014145.1.

3D structure databases

ProteinModelPortali D6CTT0.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAZ88699 ; CAZ88699 ; THI_2041 .
GeneIDi 13879779.
KEGGi thi:THI_2041.

Phylogenomic databases

HOGENOMi HOG000230831.
KOi K01601.

Enzyme and pathway databases

BioCyci TARS426114-WGS:GSYJ-1952-MONOMER.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01339. RuBisCO_L_type2.
InterProi IPR020871. RuBisCO.
IPR020878. RuBisCo_large_chain_AS.
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.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Genoscope - CEA
    Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 3As.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 22701 / CIP 110005 / 3AsImported.

Entry informationi

Entry nameiD6CTT0_THIA3
AccessioniPrimary (citable) accession number: D6CTT0
Entry historyi
Integrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: November 26, 2014
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In contrast to form I RuBisCO, the form II RuBisCO are composed solely of large subunits.UniRule annotation

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3