O26249 (CBIT_METTH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable cobalt-precorrin-6Y C(15)-methyltransferase [decarboxylating]
EC=2.1.1.-

Gene names

Name:	cbiT
Ordered Locus Names:	MTH_146

Organism

Methanobacterium thermoautotrophicum (strain Delta H)

Taxonomic identifier

187420 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probably catalyzes the methylation of either C-15 or C-5 in cobalt-precorrin-6Y to form cobalt-precorrin-7W. Methylation of C-15 would probably be followed by a spontaneous decarboxylation of C-12. Ref.2
Pathway	Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 8/10. HAMAP MF_00786
Subunit structure	Homotetramer. Ref.2
Sequence similarities	Belongs to the methyltransferase superfamily. Archaeal-type CbiT family.
Caution	Was originally thought to be a precorrin-8w decarboxylase.

Ontologies

Keywords
Biological process	Cobalamin biosynthesis
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cobalamin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein methyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 192

192

Probable cobalt-precorrin-6Y C(15)-methyltransferase [decarboxylating] HAMAP MF_00786

PRO_0000134941

Regions

Region

41 – 45

5

S-adenosyl-L-methionine binding HAMAP MF_00786

Sites

Binding site

17

1

S-adenosyl-L-methionine

Binding site

62

1

S-adenosyl-L-methionine

Binding site

91

1

S-adenosyl-L-methionine; via amide nitrogen

Secondary structure

1

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192

Helix Strand Turn

Details...

Helix

4 – 6

3

Helix

19 – 29

11

Beta strand

36 – 41

6

Helix

46 – 52

7

Beta strand

55 – 63

9

Helix

65 – 77

13

Beta strand

84 – 89

6

Helix

91 – 95

5

Beta strand

101 – 106

6

Helix

113 – 122

10

Beta strand

124 – 134

11

Helix

137 – 149

13

Beta strand

154 – 166

13

Beta strand

171 – 175

5

Beta strand

179 – 184

6

Sequences

	Sequence		Length	Mass (Da)
	O26249 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 7BFA35D8BD3C3982	FASTA	192	20,714
	10 20 30 40 50 60 MIPDDEFIKN PSVPGPTAME VRCLIMCLAE PGKNDVAVDV GCGTGGVTLE LAGRVRRVYA 70 80 90 100 110 120 IDRNPEAIST TEMNLQRHGL GDNVTLMEGD APEALCKIPD IDIAVVGGSG GELQEILRII 130 140 150 160 170 180 KDKLKPGGRI IVTAILLETK FEAMECLRDL GFDVNITELN IARGRALDRG TMMVSRNPVA 190 LIYTGVSHEN KD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics." Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N. J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Delta H.
[2]	"The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase." Keller J.P., Smith P.M., Benach J., Christendat D., deTitta G.T., Hunt J.F. Structure 10:1475-1487(2002) [PubMed: 12429089] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE, SUBUNIT, FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000666 Genomic DNA. Translation: AAB84652.1.

PIR

D69061.

RefSeq

NP_275289.1. NC_000916.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F38	X-ray	2.40	A/B/C/D	1-192	[»]
1KXZ	X-ray	2.70	A/B/C/D/E/F/G/H	1-192	[»]
1L3B	X-ray	2.65	A/B/C/D/E/F/G/H	1-192	[»]
1L3C	X-ray	2.31	A/B/C/D	1-192	[»]
1L3I	X-ray	1.95	A/B/C/D/E/F	1-192	[»]

ProteinModelPortal

O26249.

SMR

O26249. Positions 1-186.

ModBase

Search...

Protein-protein interaction databases

STRING

O26249.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1470107.

GenomeReviews

Gene locus MTH_146 in contig AE000666_GR.

KEGG

mth:MTH146.

NMPDR

fig|187420.1.peg.144.

Phylogenomic databases

eggNOG

arNOG09110.

HOGENOM

HBG553505.

OMA

IRAVSIG.

ProtClustDB

CLSK797838.

Enzyme and pathway databases

BioCyc

MTHE187420:MTH146-MONOMER.

Family and domain databases

HAMAP

MF_00786. CbiT.
[Tree]

InterPro

IPR014008. Cbl_synth_MTase_CbiT.
IPR023475. Cbl_synth_MTase_CbiT_arc-type.
[Graphical view]

KO

K02191.

TIGRFAMs

TIGR02469. CbiT. 1 hit.

ProtoNet

Search...

Entry information

Entry name

CBIT_METTH

Accession

Primary (citable) accession number: O26249

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	January 1, 1998
Last modified:	November 16, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program