ID F8EUC5_ZYMMT Unreviewed; 275 AA.
AC F8EUC5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=Zymop_1252 {ECO:0000313|EMBL:AEI38146.1};
OS Zymomonas mobilis subsp. pomaceae (strain ATCC 29192 / DSM 22645 / JCM
OS 10191 / CCUG 17912 / NBRC 13757 / NCIMB 11200 / NRRL B-4491 / Barker I).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=579138 {ECO:0000313|EMBL:AEI38146.1, ECO:0000313|Proteomes:UP000000491};
RN [1] {ECO:0000313|EMBL:AEI38146.1, ECO:0000313|Proteomes:UP000000491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29192 / DSM 22645 / JCM 10191 / CCUG 17912 / NBRC 13757 /
RC NCIMB 11200 / NRRL B-4491 / Barker I
RC {ECO:0000313|Proteomes:UP000000491};
RX PubMed=21742897; DOI=10.1128/JB.05273-11;
RA Kouvelis V.N., Davenport K.W., Brettin T.S., Bruce D., Detter C., Han C.S.,
RA Nolan M., Tapia R., Damoulaki A., Kyrpides N.C., Typas M.A., Pappas K.M.;
RT "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. pomaceae
RT lectotype strain ATCC 29192.";
RL J. Bacteriol. 193:5049-5050(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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01274}.
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DR EMBL; CP002865; AEI38146.1; -; Genomic_DNA.
DR RefSeq; WP_013934541.1; NC_015709.1.
DR AlphaFoldDB; F8EUC5; -.
DR STRING; 579138.Zymop_1252; -.
DR KEGG; zmp:Zymop_1252; -.
DR PATRIC; fig|579138.3.peg.1329; -.
DR eggNOG; COG1521; Bacteria.
DR HOGENOM; CLU_066627_1_0_5; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000000491; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01274}.
FT ACT_SITE 110
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 108..111
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 130
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
SQ SEQUENCE 275 AA; 29928 MW; 3B434757F83B3A57 CRC64;
MLLAIDAGNT NIVFALVDGR EIRARWRIAT EGRRTADEYA VWLVQLMAIG GFTREEVDSV
VICTVVPRAL HNLEVLSAKY FGVKALIVGR TPLEWGIKID VISPETVGAD RLVNAIGAHH
LHSGHKIAID FGTAATFDWI DDKGTYRGGI IAPGINLSLD SLVATAARLP RIAIEIPDNN
QVIGRSTEES MHSGIYWGYI AMMEGLTSRM KREIDQPVTV MATGGLASLF AVHTDVFDVI
EPDLTIQGMA LLYERAALPK FTAQAGGFEA DFLPL
//
