ID N9P7D4_9GAMM Unreviewed; 246 AA.
AC N9P7D4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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 ORFNames=F897_01222 {ECO:0000313|EMBL:ENX10105.1};
OS Acinetobacter variabilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=70346 {ECO:0000313|EMBL:ENX10105.1, ECO:0000313|Proteomes:UP000013101};
RN [1] {ECO:0000313|EMBL:ENX10105.1, ECO:0000313|Proteomes:UP000013101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 2171 {ECO:0000313|EMBL:ENX10105.1,
RC ECO:0000313|Proteomes:UP000013101};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. NIPH 2171.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01274}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENX10105.1}.
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DR EMBL; APRS01000008; ENX10105.1; -; Genomic_DNA.
DR RefSeq; WP_005234243.1; NZ_KB850113.1.
DR AlphaFoldDB; N9P7D4; -.
DR STRING; 70346.F897_01222; -.
DR PATRIC; fig|1217693.3.peg.1176; -.
DR HOGENOM; CLU_066627_0_1_6; -.
DR OrthoDB; 9781305at2; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000013101; Unassembled WGS sequence.
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 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01274}.
FT ACT_SITE 104
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 102..105
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
SQ SEQUENCE 246 AA; 27243 MW; B14F59CF7C2BB016 CRC64;
MKKLWLDIGN TRLKYWITEQ NQIIEHAAEM HLQSPADLLL GLIQHFKSLG LHQVGISSVL
DKANNVRIQS ILTCLNIPVV FAKVQARYAG LICGYDDPSQ LGIDRWLQVL AVAKSADQNY
CVISCGTALT IDLAQGQEHL GGYILPNLYL QRDSLIQNTK GIKIPDVAFE ELSPGRNTID
AVHHGILFGL LSTIEKVLQD FPAQLILTGG DAALFAQHLE RFQPVIEPDL LLKGLQHFAD
HLPDTV
//
