COAA_VIBVY
ID COAA_VIBVY Reviewed; 307 AA.
AC Q7MGQ9;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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}; OrderedLocusNames=VV3168;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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}.
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DR EMBL; BA000037; BAC95932.1; -; Genomic_DNA.
DR RefSeq; WP_011151385.1; NC_005139.1.
DR AlphaFoldDB; Q7MGQ9; -.
DR SMR; Q7MGQ9; -.
DR STRING; 672.VV93_v1c28840; -.
DR EnsemblBacteria; BAC95932; BAC95932; BAC95932.
DR KEGG; vvy:VV3168; -.
DR PATRIC; fig|196600.6.peg.3136; -.
DR eggNOG; COG1072; Bacteria.
DR HOGENOM; CLU_053818_1_1_6; -.
DR OMA; RKYTQVS; -.
DR OrthoDB; 1793376at2; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000002675; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004594; F:pantothenate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
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..307
FT /note="Pantothenate kinase"
FT /id="PRO_0000194462"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00215"
SQ SEQUENCE 307 AA; 35338 MW; EC20E0D34FE312F5 CRC64;
MSPFLSFSRA TWSELRNSVP MTLSEEDLKA LQGINENLTM QEAVEVYLPL SRLLNLYVQA
RQSRNSVLHQ FLNNDEHAPP FVIGIAGSVA VGKSTTARVL CALLSRWENH PKVELVTTDG
FLYPKKMLNQ RGIMHKKGFP ESYDMKKLVQ FVSDVKAGKP ELEVPVYSHI TYDITEEVKR
VDRPDVLIIE GLNVLQSGMD YPHDPHRVFV SDFLDFSIYV DAESNTIEQW YVERFLKFRK
GAFTQPGSYF SHYTQLSEQQ AIEKAQQIWR DINGINLTEN ILPTKERAQL ILRKGQNHLV
EEILLRK