ID A4AU63_MARSH Unreviewed; 242 AA.
AC A4AU63;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Type III pantothenate kinase {ECO:0000256|ARBA:ARBA00040883, ECO:0000256|HAMAP-Rule:MF_01274};
DE EC=2.7.1.33 {ECO:0000256|ARBA:ARBA00012102, ECO:0000256|HAMAP-Rule:MF_01274};
DE AltName: Full=PanK-III {ECO:0000256|HAMAP-Rule:MF_01274};
DE AltName: Full=Pantothenic acid kinase {ECO:0000256|HAMAP-Rule:MF_01274};
GN Name=coaX {ECO:0000256|HAMAP-Rule:MF_01274};
GN OrderedLocusNames=FB2170_08414 {ECO:0000313|EMBL:EAR00514.1};
OS Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00514.1, ECO:0000313|Proteomes:UP000001602};
RN [1] {ECO:0000313|EMBL:EAR00514.1, ECO:0000313|Proteomes:UP000001602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX PubMed=21037013; DOI=10.1128/JB.01207-10;
RA Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA Cho J.C.;
RT "Complete genome sequence of strain HTCC2170, a novel member of the genus
RT Maribacter in the family Flavobacteriaceae.";
RL J. Bacteriol. 193:303-304(2011).
CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC first step in CoA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01274}.
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:0000256|ARBA:ARBA00001206,
CC ECO:0000256|HAMAP-Rule:MF_01274};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- COFACTOR:
CC Name=NH4(+); Xref=ChEBI:CHEBI:28938;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01274};
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01274};
CC Note=A monovalent cation. Ammonium or potassium. {ECO:0000256|HAMAP-
CC Rule:MF_01274};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5. {ECO:0000256|ARBA:ARBA00005225,
CC ECO:0000256|HAMAP-Rule:MF_01274}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01274}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01274}.
CC -!- SIMILARITY: Belongs to the type III pantothenate kinase family.
CC {ECO:0000256|ARBA:ARBA00038036, ECO:0000256|HAMAP-Rule:MF_01274}.
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DR EMBL; CP002157; EAR00514.1; -; Genomic_DNA.
DR RefSeq; WP_013306339.1; NC_014472.1.
DR AlphaFoldDB; A4AU63; -.
DR STRING; 313603.FB2170_08414; -.
DR KEGG; fbc:FB2170_08414; -.
DR eggNOG; COG1521; Bacteria.
DR HOGENOM; CLU_066627_2_0_10; -.
DR OrthoDB; 9804707at2; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000001602; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_01274; Pantothen_kinase_3; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004619; Type_III_PanK.
DR NCBIfam; TIGR00671; baf; 1.
DR PANTHER; PTHR34265; TYPE III PANTOTHENATE KINASE; 1.
DR PANTHER; PTHR34265:SF1; TYPE III PANTOTHENATE KINASE; 1.
DR Pfam; PF03309; Pan_kinase; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01274};
KW Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993, ECO:0000256|HAMAP-
KW Rule:MF_01274};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01274};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01274};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01274};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01274};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01274};
KW Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01274}.
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 6..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 94..97
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 117
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
SQ SEQUENCE 242 AA; 26725 MW; 304853827EF3A2D1 CRC64;
MNLIIDVGNT YVKLAVFEKD NLLFDEVGDT KNLAEEVKKI FKKYTKIDWA IISSVVSLDI
DDIKALTTFC NLHVLDHSSK TPFKSQYASP TTLGVDRIAL AAAGYFHNQD KNTLVIDAGT
CITYDMVTGQ GDYLGGAISP GIMMRYKALN NQTSKLPLLG KEPPIDLIGT TTETSIHSGI
INGVCAEIDG IIEQYSSRFE DLTVILTGGD AQFLSKRLKN TIFAHSKFLL EGLNYLLDYN
KR
//