COAA_BRADU
ID COAA_BRADU Reviewed; 318 AA.
AC Q89WM2;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Pantothenate kinase {ECO:0000255|HAMAP-Rule:MF_00215};
DE EC=2.7.1.33 {ECO:0000255|HAMAP-Rule:MF_00215};
DE AltName: Full=Pantothenic acid kinase {ECO:0000255|HAMAP-Rule:MF_00215};
GN Name=coaA {ECO:0000255|HAMAP-Rule:MF_00215}; Synonyms=panK;
GN OrderedLocusNames=blr0656;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00215};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5. {ECO:0000255|HAMAP-Rule:MF_00215}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00215}.
CC -!- SIMILARITY: Belongs to the prokaryotic pantothenate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00215}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC45921.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000040; BAC45921.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_767296.1; NC_004463.1.
DR RefSeq; WP_027543772.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89WM2; -.
DR SMR; Q89WM2; -.
DR STRING; 224911.27348905; -.
DR EnsemblBacteria; BAC45921; BAC45921; BAC45921.
DR GeneID; 64020518; -.
DR KEGG; bja:blr0656; -.
DR PATRIC; fig|224911.44.peg.25; -.
DR eggNOG; COG1072; Bacteria.
DR HOGENOM; CLU_053818_1_1_5; -.
DR InParanoid; Q89WM2; -.
DR OMA; RKYTQVS; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004594; F:pantothenate kinase activity; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..318
FT /note="Pantothenate kinase"
FT /id="PRO_0000194420"
FT BINDING 96..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00215"
SQ SEQUENCE 318 AA; 36712 MW; 07FB31D15C5471C1 CRC64;
MDIRAPEQQY NPYRVYTREQ WARLRDDTPM TLEPGEFDRL RSLHDRLDLQ EVEDIYLPLS
RLLSIYVDAM QRLYYAERQF LNIRDRKMPY IIGVAGSVAV GKSTTARVLQ ALLARWSPRP
KVDLITTDGF LYPNAVLDRQ GIMQKKGFPE SYDLPLLLGF LSDIKAGRRH VRAPVYSHLT
YDIVPNQWVE IDQPDILIVE GVNVLQTGKL PRDGKAVPVV SDFFDFSVYI DADEAALRRW
YIKRFLALRD TAFTNPKSYF NRYALLSDEE ATATAIAIWE RTNLANLEDN ILPTRPRATL
ILKKGPDHVV ESVALRRL