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Protein

Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)

Gene

cbiT

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.1 Publication

Catalytic activityi

Cobalt-precorrin-6B + S-adenosyl-L-methionine = cobalt-precorrin-7 + S-adenosyl-L-homocysteine + CO2.UniRule annotation

Pathwayi: adenosylcobalamin biosynthesis

This protein is involved in step 8 of the subpathway that synthesizes cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route).UniRule annotation
Proteins known to be involved in the 10 steps of the subpathway in this organism are:
  1. Sirohydrochlorin cobaltochelatase (cbiX)
  2. no protein annotated in this organism
  3. Probable cobalt-factor III C(17)-methyltransferase (cbiH)
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. Cobalt-precorrin-5B C(1)-methyltransferase (cbiD)
  7. Cobalt-precorrin-6A reductase (cbiJ)
  8. Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) (cbiT)
  9. Cobalt-precorrin-8 methylmutase (cbiC)
  10. Cobyrinate a,c-diamide synthase (cbiA)
This subpathway is part of the pathway adenosylcobalamin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route), the pathway adenosylcobalamin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei17S-adenosyl-L-methionineUniRule annotation1 Publication1
Binding sitei62S-adenosyl-L-methionineUniRule annotation1 Publication1
Binding sitei91S-adenosyl-L-methionine; via amide nitrogenUniRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Cobalamin biosynthesis

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.289. 3256.
UniPathwayiUPA00148; UER00229.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)UniRule annotation (EC:2.1.1.196UniRule annotation)
Gene namesi
Name:cbiTUniRule annotation
Ordered Locus Names:MTH_146
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000005223 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001349411 – 192Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating)Add BLAST192

Proteomic databases

PRIDEiO26249.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi187420.MTH146.

Structurei

Secondary structure

1192
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 6Combined sources3
Helixi19 – 29Combined sources11
Beta strandi36 – 41Combined sources6
Helixi46 – 52Combined sources7
Beta strandi55 – 63Combined sources9
Helixi65 – 77Combined sources13
Beta strandi84 – 89Combined sources6
Helixi91 – 95Combined sources5
Beta strandi101 – 107Combined sources7
Helixi113 – 122Combined sources10
Beta strandi124 – 134Combined sources11
Helixi137 – 149Combined sources13
Beta strandi155 – 167Combined sources13
Beta strandi170 – 175Combined sources6
Beta strandi179 – 183Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F38X-ray2.40A/B/C/D1-192[»]
1KXZX-ray2.70A/B/C/D/E/F/G/H1-192[»]
1L3BX-ray2.65A/B/C/D/E/F/G/H1-192[»]
1L3CX-ray2.31A/B/C/D1-192[»]
1L3IX-ray1.95A/B/C/D/E/F1-192[»]
ProteinModelPortaliO26249.
SMRiO26249.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO26249.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni41 – 45S-adenosyl-L-methionine binding5

Sequence similaritiesi

Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG00977. Archaea.
COG2242. LUCA.
KOiK02191.
OMAiKFVYAID.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00786. CbiT. 1 hit.
InterProiIPR023475. CbiT.
IPR014008. Cbl_synth_MTase_CbiT.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF13847. Methyltransf_31. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR02469. CbiT. 1 hit.

Sequencei

Sequence statusi: Complete.

O26249-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPDDEFIKN PSVPGPTAME VRCLIMCLAE PGKNDVAVDV GCGTGGVTLE
60 70 80 90 100
LAGRVRRVYA IDRNPEAIST TEMNLQRHGL GDNVTLMEGD APEALCKIPD
110 120 130 140 150
IDIAVVGGSG GELQEILRII KDKLKPGGRI IVTAILLETK FEAMECLRDL
160 170 180 190
GFDVNITELN IARGRALDRG TMMVSRNPVA LIYTGVSHEN KD
Length:192
Mass (Da):20,714
Last modified:January 1, 1998 - v1
Checksum:i7BFA35D8BD3C3982
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB84652.1.
PIRiD69061.
RefSeqiWP_010875785.1. NC_000916.1.

Genome annotation databases

EnsemblBacteriaiAAB84652; AAB84652; MTH_146.
GeneIDi1470107.
KEGGimth:MTH_146.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB84652.1.
PIRiD69061.
RefSeqiWP_010875785.1. NC_000916.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F38X-ray2.40A/B/C/D1-192[»]
1KXZX-ray2.70A/B/C/D/E/F/G/H1-192[»]
1L3BX-ray2.65A/B/C/D/E/F/G/H1-192[»]
1L3CX-ray2.31A/B/C/D1-192[»]
1L3IX-ray1.95A/B/C/D/E/F1-192[»]
ProteinModelPortaliO26249.
SMRiO26249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi187420.MTH146.

Proteomic databases

PRIDEiO26249.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB84652; AAB84652; MTH_146.
GeneIDi1470107.
KEGGimth:MTH_146.

Phylogenomic databases

eggNOGiarCOG00977. Archaea.
COG2242. LUCA.
KOiK02191.
OMAiKFVYAID.

Enzyme and pathway databases

UniPathwayiUPA00148; UER00229.
BRENDAi2.1.1.289. 3256.

Miscellaneous databases

EvolutionaryTraceiO26249.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00786. CbiT. 1 hit.
InterProiIPR023475. CbiT.
IPR014008. Cbl_synth_MTase_CbiT.
IPR025714. Methyltranfer_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF13847. Methyltransf_31. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR02469. CbiT. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCBIT_METTH
AccessioniPrimary (citable) accession number: O26249
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be a precorrin-8w decarboxylase.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.