P63810 (COAA_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pantothenate kinase
EC=2.7.1.33

Alternative name(s):
Pantothenic acid kinase

Gene names

Name:	coaA
Ordered Locus Names:	Rv1092c, MT1124
ORF Names:	MTV017.45c

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate. HAMAP MF_00215
Pathway	Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. HAMAP MF_00215
Subcellular location	Cytoplasm Probable HAMAP MF_00215.
Miscellaneous	Was identified as a high-confidence drug target. HAMAP MF_00215
Sequence similarities	Belongs to the prokaryotic pantothenate kinase family.

Ontologies

Keywords
Biological process	Coenzyme A biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	coenzyme A biosynthetic process Inferred from direct assay. Source: MTBBASE growth Inferred from mutant phenotype. Source: MTBBASE
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: MTBBASE
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW pantothenate kinase activity Inferred from direct assay. Source: MTBBASE protein homodimerization activity Inferred from physical interaction. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 312

312

Pantothenate kinase HAMAP MF_00215

PRO_0000194439

Regions

Nucleotide binding

97 – 104

8

ATP Potential

Secondary structure

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312

Helix Strand Turn

Details...

Beta strand

9 – 14

6

Helix

15 – 18

4

Helix

19 – 22

4

Helix

31 – 37

7

Helix

46 – 51

6

Helix

53 – 78

26

Beta strand

91 – 97

7

Helix

103 – 115

13

Beta strand

123 – 127

5

Helix

128 – 131

4

Helix

135 – 139

5

Turn

140 – 142

3

Helix

144 – 146

3

Helix

150 – 152

3

Helix

155 – 167

13

Beta strand

172 – 178

7

Turn

179 – 182

4

Beta strand

183 – 192

10

Beta strand

196 – 201

6

Helix

214 – 217

4

Beta strand

219 – 225

7

Helix

228 – 242

15

Turn

243 – 248

6

Helix

255 – 258

4

Helix

262 – 275

14

Helix

277 – 283

7

Helix

286 – 291

6

Beta strand

293 – 298

6

Beta strand

304 – 310

7

Sequences

	Sequence		Length	Mass (Da)
	P63810 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: F075B543AE75788D	FASTA	312	35,657
	10 20 30 40 50 60 MSRLSEPSPY VEFDRRQWRA LRMSTPLALT EEELVGLRGL GEQIDLLEVE EVYLPLARLI 70 80 90 100 110 120 HLQVAARQRL FAATAEFLGE PQQNPDRPVP FIIGVAGSVA VGKSTTARVL QALLARWDHH 130 140 150 160 170 180 PRVDLVTTDG FLYPNAELQR RNLMHRKGFP ESYNRRALMR FVTSVKSGSD YACAPVYSHL 190 200 210 220 230 240 HYDIIPGAEQ VVRHPDILIL EGLNVLQTGP TLMVSDLFDF SLYVDARIED IEQWYVSRFL 250 260 270 280 290 300 AMRTTAFADP ESHFHHYAAF SDSQAVVAAR EIWRTINRPN LVENILPTRP RATLVLRKDA 310 DHSINRLRLR KL

References

[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis." Raman K., Yeturu K., Chandra N. BMC Syst. Biol. 2:109-109(2008) [PubMed: 19099550] [Abstract] Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842575 Genomic DNA. Translation: CAA17208.1.
AE000516 Genomic DNA. Translation: AAK45382.1.

PIR

B70896.

RefSeq

NP_215608.1. NC_000962.2.
NP_335568.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GES	X-ray	2.40	A	1-312	[»]
2GET	X-ray	2.35	A	1-312	[»]
2GEU	X-ray	2.90	A	1-312	[»]
2GEV	X-ray	2.35	A	1-312	[»]
2ZS7	X-ray	2.65	A	1-312	[»]
2ZS8	X-ray	2.80	A	1-312	[»]
2ZS9	X-ray	2.70	A	1-312	[»]
2ZSA	X-ray	2.50	A	1-312	[»]
2ZSB	X-ray	2.75	A	1-312	[»]
2ZSD	X-ray	2.50	A	1-312	[»]
2ZSE	X-ray	2.50	A	1-312	[»]
2ZSF	X-ray	2.80	A	1-312	[»]
3AEZ	X-ray	2.20	A	1-312	[»]
3AF0	X-ray	2.50	A	1-312	[»]
3AF1	X-ray	2.50	A	1-312	[»]
3AF2	X-ray	2.30	A	1-312	[»]
3AF3	X-ray	2.35	A	1-312	[»]
3AF4	X-ray	2.60	A	1-312	[»]
3AVO	X-ray	2.55	A	1-312	[»]
3AVP	X-ray	2.60	A	1-312	[»]
3AVQ	X-ray	3.00	A	1-312	[»]

ProteinModelPortal

P63810.

SMR

P63810. Positions 5-312.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000001075; EBMYCP00000001075; EBMYCG00000001075.
EBMYCT00000069066; EBMYCP00000067125; EBMYCG00000069061.

GeneID

885120.
924980.

GenomeReviews

Gene locus MT1124 in contig AE000516_GR.
Gene locus Rv1092c in contig AL123456_GR.

KEGG

mtc:MT1124.
mtu:Rv1092c.

PATRIC

18124234. VBIMycTub22151_1237.

TIGR

MT1124.

Organism-specific databases

TubercuList

Rv1092c.

Phylogenomic databases

GeneTree

EBGT00050000016369.

HOGENOM

HBG732538.

OMA

EVYLPLS.

PhylomeDB

P63810.

ProtClustDB

PRK05439.

Family and domain databases

HAMAP

MF_00215. Pantothen_kinase_1.
[Tree]

InterPro

IPR004566. PanK_bact.
IPR006083. PRK/URK.
[Graphical view]

KO

K00867.

PANTHER

PTHR10285:SF7. PanK_bact. 1 hit.

Pfam

PF00485. PRK. 1 hit.
[Graphical view]

PIRSF

PIRSF000545. Pantothenate_kin. 1 hit.

TIGRFAMs

TIGR00554. PanK_bact. 1 hit.

ProtoNet

Search...

Entry information

Entry name

COAA_MYCTU

Accession

Primary (citable) accession number: P63810
Secondary accession number(s): O53440

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program