COAA_MYCTU
ID COAA_MYCTU Reviewed; 312 AA.
AC P9WPA7; L0T5P3; O53440; P63810;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Pantothenate kinase;
DE EC=2.7.1.33;
DE AltName: Full=Pantothenic acid kinase;
GN Name=coaA; OrderedLocusNames=Rv1092c; ORFNames=MTV017.45c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP +
CC H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC EC=2.7.1.33;
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the prokaryotic pantothenate kinase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP43845.1; -; Genomic_DNA.
DR PIR; B70896; B70896.
DR RefSeq; NP_215608.1; NC_000962.3.
DR RefSeq; WP_003405790.1; NZ_NVQJ01000021.1.
DR PDB; 2GES; X-ray; 2.40 A; A=1-312.
DR PDB; 2GET; X-ray; 2.35 A; A=1-312.
DR PDB; 2GEU; X-ray; 2.90 A; A=1-312.
DR PDB; 2GEV; X-ray; 2.35 A; A=1-312.
DR PDB; 2ZS7; X-ray; 2.65 A; A=1-312.
DR PDB; 2ZS8; X-ray; 2.80 A; A=1-312.
DR PDB; 2ZS9; X-ray; 2.70 A; A=1-312.
DR PDB; 2ZSA; X-ray; 2.50 A; A=1-312.
DR PDB; 2ZSB; X-ray; 2.75 A; A=1-312.
DR PDB; 2ZSD; X-ray; 2.50 A; A=1-312.
DR PDB; 2ZSE; X-ray; 2.50 A; A=1-312.
DR PDB; 2ZSF; X-ray; 2.80 A; A=1-312.
DR PDB; 3AEZ; X-ray; 2.20 A; A=1-312.
DR PDB; 3AF0; X-ray; 2.50 A; A=1-312.
DR PDB; 3AF1; X-ray; 2.50 A; A=1-312.
DR PDB; 3AF2; X-ray; 2.30 A; A=1-312.
DR PDB; 3AF3; X-ray; 2.35 A; A=1-312.
DR PDB; 3AF4; X-ray; 2.60 A; A=1-312.
DR PDB; 3AVO; X-ray; 2.55 A; A=1-312.
DR PDB; 3AVP; X-ray; 2.60 A; A=1-312.
DR PDB; 3AVQ; X-ray; 3.00 A; A=1-312.
DR PDB; 4BFS; X-ray; 2.90 A; A=1-312.
DR PDB; 4BFT; X-ray; 2.29 A; A/B=1-312.
DR PDB; 4BFU; X-ray; 2.28 A; A/B=1-312.
DR PDB; 4BFV; X-ray; 2.29 A; A/B=1-312.
DR PDB; 4BFW; X-ray; 2.27 A; A/B=1-312.
DR PDB; 4BFX; X-ray; 2.70 A; A/B=1-312.
DR PDB; 4BFY; X-ray; 2.30 A; A/B=1-312.
DR PDB; 4BFZ; X-ray; 2.10 A; A/B=1-312.
DR PDB; 5XLV; X-ray; 1.80 A; A/B=1-312.
DR PDB; 5XLW; X-ray; 2.26 A; A/B=1-312.
DR PDB; 5XMB; X-ray; 3.20 A; A/B/C/D=1-312.
DR PDBsum; 2GES; -.
DR PDBsum; 2GET; -.
DR PDBsum; 2GEU; -.
DR PDBsum; 2GEV; -.
DR PDBsum; 2ZS7; -.
DR PDBsum; 2ZS8; -.
DR PDBsum; 2ZS9; -.
DR PDBsum; 2ZSA; -.
DR PDBsum; 2ZSB; -.
DR PDBsum; 2ZSD; -.
DR PDBsum; 2ZSE; -.
DR PDBsum; 2ZSF; -.
DR PDBsum; 3AEZ; -.
DR PDBsum; 3AF0; -.
DR PDBsum; 3AF1; -.
DR PDBsum; 3AF2; -.
DR PDBsum; 3AF3; -.
DR PDBsum; 3AF4; -.
DR PDBsum; 3AVO; -.
DR PDBsum; 3AVP; -.
DR PDBsum; 3AVQ; -.
DR PDBsum; 4BFS; -.
DR PDBsum; 4BFT; -.
DR PDBsum; 4BFU; -.
DR PDBsum; 4BFV; -.
DR PDBsum; 4BFW; -.
DR PDBsum; 4BFX; -.
DR PDBsum; 4BFY; -.
DR PDBsum; 4BFZ; -.
DR PDBsum; 5XLV; -.
DR PDBsum; 5XLW; -.
DR PDBsum; 5XMB; -.
DR AlphaFoldDB; P9WPA7; -.
DR SMR; P9WPA7; -.
DR STRING; 83332.Rv1092c; -.
DR BindingDB; P9WPA7; -.
DR PaxDb; P9WPA7; -.
DR DNASU; 885120; -.
DR GeneID; 45425066; -.
DR GeneID; 885120; -.
DR KEGG; mtu:Rv1092c; -.
DR TubercuList; Rv1092c; -.
DR eggNOG; COG0572; Bacteria.
DR OMA; RKYTQVS; -.
DR PhylomeDB; P9WPA7; -.
DR BRENDA; 2.7.1.33; 3445.
DR SABIO-RK; P9WPA7; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004594; F:pantothenate kinase activity; IDA:MTBBASE.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:MTBBASE.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd02025; PanK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00215; Pantothen_kinase_1; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004566; PanK.
DR InterPro; IPR006083; PRK/URK.
DR PANTHER; PTHR10285:SF139; PTHR10285:SF139; 1.
DR Pfam; PF00485; PRK; 1.
DR PIRSF; PIRSF000545; Pantothenate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00554; panK_bact; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..312
FT /note="Pantothenate kinase"
FT /id="PRO_0000194439"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:5XLV"
FT HELIX 15..20
FT /evidence="ECO:0007829|PDB:5XLV"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:4BFW"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:5XLV"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:5XLV"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:4BFZ"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:5XLV"
FT HELIX 53..77
FT /evidence="ECO:0007829|PDB:5XLV"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:5XLW"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3AEZ"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:5XLV"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:5XLV"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:4BFX"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:5XLV"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:5XLV"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:5XLV"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5XLV"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:5XLV"
FT HELIX 155..166
FT /evidence="ECO:0007829|PDB:5XLV"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5XLV"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:5XLV"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:5XLV"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:5XLV"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:5XLV"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:4BFZ"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:5XLV"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:5XLV"
FT HELIX 228..242
FT /evidence="ECO:0007829|PDB:5XLV"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:5XLV"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:5XLV"
FT TURN 250..254
FT /evidence="ECO:0007829|PDB:5XLW"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:5XLV"
FT HELIX 262..275
FT /evidence="ECO:0007829|PDB:5XLV"
FT HELIX 277..284
FT /evidence="ECO:0007829|PDB:5XLV"
FT HELIX 286..291
FT /evidence="ECO:0007829|PDB:5XLV"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:5XLV"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:5XLV"
SQ SEQUENCE 312 AA; 35657 MW; F075B543AE75788D CRC64;
MSRLSEPSPY VEFDRRQWRA LRMSTPLALT EEELVGLRGL GEQIDLLEVE EVYLPLARLI
HLQVAARQRL FAATAEFLGE PQQNPDRPVP FIIGVAGSVA VGKSTTARVL QALLARWDHH
PRVDLVTTDG FLYPNAELQR RNLMHRKGFP ESYNRRALMR FVTSVKSGSD YACAPVYSHL
HYDIIPGAEQ VVRHPDILIL EGLNVLQTGP TLMVSDLFDF SLYVDARIED IEQWYVSRFL
AMRTTAFADP ESHFHHYAAF SDSQAVVAAR EIWRTINRPN LVENILPTRP RATLVLRKDA
DHSINRLRLR KL
