P31570 (BTUR_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cob(I)yrinic acid a,c-diamide adenosyltransferase
EC=2.5.1.17

Alternative name(s):
Cob(I)alamin adenosyltransferase
Corrinoid adenosyltransferase

Gene names

Name:	btuR
Synonyms:	cobA
Ordered Locus Names:	STM1718

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella typhimurium

Protein attributes

Sequence length	196 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids.
Catalytic activity	ATP + cob(I)yrinic acid a,c-diamide = triphosphate + adenosylcob(III)yrinic acid a,c-diamide. ATP + cobinamide = triphosphate + adenosylcobinamide.
Pathway	Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the Cob(I)alamin adenosyltransferase family.

Ontologies

Keywords
Biological process	Cobalamin biosynthesis Porphyrin biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cobalamin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway porphyrin-containing compound biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cob(I)yrinic acid a,c-diamide adenosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 196

196

Cob(I)yrinic acid a,c-diamide adenosyltransferase

PRO_0000065010

Regions

Nucleotide binding

36 – 42

7

ATP By similarity

Secondary structure

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196

Helix Strand Turn

Details...

Helix

7 – 23

17

Beta strand

31 – 39

9

Helix

41 – 54

14

Beta strand

59 – 65

7

Helix

72 – 77

6

Helix

78 – 80

3

Beta strand

83 – 86

4

Helix

95 – 97

3

Helix

98 – 115

18

Beta strand

122 – 127

6

Helix

129 – 134

6

Helix

140 – 148

9

Beta strand

155 – 159

5

Helix

165 – 170

6

Beta strand

172 – 176

5

Helix

183 – 186

4

Turn

192 – 194

3

Sequences

	Sequence		Length	Mass (Da)
	P31570 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: AE02E11176513CC4	FASTA	196	21,726
	10 20 30 40 50 60 MSDERYQQRQ QKVKDRVDAR VAQAQEERGI IIVFTGNGKG KTTAAFGTAA RAVGHGKNVG 70 80 90 100 110 120 VVQFIKGTWP NGERNLLEPH GVEFQVMATG FTWETQNREA DTAACMAVWQ HGKRMLADPL 130 140 150 160 170 180 LDMVVLDELT YMVAYDYLPL EEVISALNAR PGHQTVIITG RGCHRDILDL ADTVSELRPV 190 KHAFDAGVKA QMGIDY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequencing and overexpression of cobA which encodes ATP:corrinoid adenosyltransferase in Salmonella typhimurium." Suh S.-J., Escalante-Semerena J.C. Gene 129:93-97(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LT2.
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"Purification and initial characterization of the ATP:corrinoid adenosyltransferase encoded by the cobA gene of Salmonella typhimurium." Suh S.-J., Escalante-Semerena J.C. J. Bacteriol. 177:921-925(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21, CHARACTERIZATION.
[4]	"cobA function is required for both de novo cobalamin biosynthesis and assimilation of exogenous corrinoids in Salmonella typhimurium." Escalante-Semerena J.C., Suh S.-J., Roth J.R. J. Bacteriol. 172:273-280(1990) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[5]	"The ATP:Co(I)rrinoid adenosyltransferase (CobA) enzyme of Salmonella enterica requires the 2'-OH group of ATP for function and yields inorganic triphosphate as its reaction byproduct." Fonseca M.V., Buan N.R., Horswill A.R., Rayment I., Escalante-Semerena J.C. J. Biol. Chem. 277:33127-33131(2002) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[6]	"Three-dimensional structure of ATP:corrinoid adenosyltransferase from Salmonella typhimurium in its free state, complexed with MgATP, or complexed with hydroxycobalamin and MgATP." Bauer C.B., Fonseca M.V., Holden H.M., Thoden J.B., Thompson T.B., Escalante-Semerena J.C., Rayment I. Biochemistry 40:361-374(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-183.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L08890 Unassigned DNA. Translation: AAA71929.1.
AE006468 Genomic DNA. Translation: AAL20636.1.

PIR

JN0721.

RefSeq

NP_460677.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G5R	X-ray	2.10	A	1-196	[»]
1G5T	X-ray	1.80	A	1-196	[»]
1G64	X-ray	2.10	A/B	1-196	[»]
4HUT	X-ray	1.95	A/B	6-196	[»]

ProteinModelPortal

P31570.

SMR

P31570. Positions 7-196.

ModBase

Search...

Protein-protein interaction databases

STRING

99287.STM1718.

Proteomic databases

PaxDb

P31570.

PRIDE

P31570.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAL20636; AAL20636; STM1718.

GeneID

1253237.

KEGG

stm:STM1718.

PATRIC

32381951. VBISalEnt20916_1815.

Phylogenomic databases

eggNOG

COG2109.

HOGENOM

HOG000260311.

KO

K00798.

OMA

WHTMGEG.

ProtClustDB

PRK05986.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-13220.

UniPathway

UPA00148; UER00233.

Family and domain databases

InterPro

IPR003724. AdoCbl_synth_CblAdoTrfase_CobA.
IPR025826. Co_AT_N_dom.
[Graphical view]

Pfam

PF12557. Co_AT_N. 1 hit.
PF02572. CobA_CobO_BtuR. 1 hit.
[Graphical view]

PIRSF

PIRSF015617. Adensltrnsf_CobA. 1 hit.

TIGRFAMs

TIGR00708. cobA. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P31570.

Entry information

Entry name

BTUR_SALTY

Accession

Primary (citable) accession number: P31570

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	May 1, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program