ID C0XPX9_CORLD Unreviewed; 313 AA.
AC C0XPX9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Pantothenate kinase {ECO:0000256|ARBA:ARBA00015080, ECO:0000256|HAMAP-Rule:MF_00215};
DE EC=2.7.1.33 {ECO:0000256|ARBA:ARBA00012102, ECO:0000256|HAMAP-Rule:MF_00215};
DE AltName: Full=Pantothenic acid kinase {ECO:0000256|HAMAP-Rule:MF_00215};
GN Name=coaA {ECO:0000256|HAMAP-Rule:MF_00215,
GN ECO:0000313|EMBL:EEI17710.1};
GN ORFNames=HMPREF0298_0499 {ECO:0000313|EMBL:EEI17710.1};
OS Corynebacterium lipophiloflavum (strain ATCC 700352 / DSM 44291 / CCUG
OS 37336 / JCM 10383 / DMMZ 1944).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=525263 {ECO:0000313|EMBL:EEI17710.1, ECO:0000313|Proteomes:UP000006196};
RN [1] {ECO:0000313|EMBL:EEI17710.1, ECO:0000313|Proteomes:UP000006196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700352 / DSM 44291 / CCUG 37336 / JCM 10383 / DMMZ 1944
RC {ECO:0000313|Proteomes:UP000006196};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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_00215, ECO:0000256|RuleBase:RU003530};
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_00215, ECO:0000256|RuleBase:RU003530}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000256|RuleBase:RU003530}.
CC -!- SIMILARITY: Belongs to the prokaryotic pantothenate kinase family.
CC {ECO:0000256|ARBA:ARBA00006087, ECO:0000256|HAMAP-Rule:MF_00215,
CC ECO:0000256|RuleBase:RU003530}.
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:EEI17710.1}.
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DR EMBL; ACHJ01000031; EEI17710.1; -; Genomic_DNA.
DR AlphaFoldDB; C0XPX9; -.
DR STRING; 525263.HMPREF0298_0499; -.
DR eggNOG; COG1072; Bacteria.
DR HOGENOM; CLU_053818_1_1_11; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000006196; 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 CDD; cd02025; PanK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00554; panK_bact; 1.
DR PANTHER; PTHR10285:SF139; PANTOTHENATE KINASE; 1.
DR PANTHER; PTHR10285; URIDINE KINASE; 1.
DR Pfam; PF00485; PRK; 1.
DR PIRSF; PIRSF000545; Pantothenate_kin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00215};
KW Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00215,
KW ECO:0000256|RuleBase:RU003530};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000256|RuleBase:RU003530};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000313|EMBL:EEI17710.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00215};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000313|EMBL:EEI17710.1}.
FT DOMAIN 93..239
FT /note="Phosphoribulokinase/uridine kinase"
FT /evidence="ECO:0000259|Pfam:PF00485"
FT BINDING 98..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00215"
SQ SEQUENCE 313 AA; 35474 MW; 867EAE8182FB8C8F CRC64;
MGAMSRPADS SPSSPYVDFR REDWSRRRAA MPQVLTEDEL AQLAGIGENI DLREVADIYL
PISRLIHLRV EAAQRLNTAT AMFLGESMRV PYIIGVAGSV AVGKSTTARL LQVLLQRWES
HPRVDLVTTD GFLYPTKTLR ERGLLLRKGF PESYDRRNLM RFVTDVKSGA PAVEAPVYSH
KLYDIVAGEH QLVDKPDILI LEGLNVLQTG PTLMISDLFD FSVYVDAKTE HIEQWYIDRF
LQLRTTAFRE PDAHFARFAE LDDASATREA REIWQSINLP NLVENILPTR VRASLVLGKG
ADHSVQRVRM RKM
//
