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Type III pantothenate kinase (EC 2.7.1.33) (PanK-III) (Pantothenic acid kinase)

 A0A0T6M5T4_HELPX        Unreviewed;       221 AA.
A0A0T6M5T4;
17-FEB-2016, integrated into UniProtKB/TrEMBL.
17-FEB-2016, sequence version 1.
07-JUN-2017, entry version 12.
RecName: Full=Type III pantothenate kinase {ECO:0000256|HAMAP-Rule:MF_01274};
EC=2.7.1.33 {ECO:0000256|HAMAP-Rule:MF_01274};
AltName: Full=PanK-III {ECO:0000256|HAMAP-Rule:MF_01274};
AltName: Full=Pantothenic acid kinase {ECO:0000256|HAMAP-Rule:MF_01274};
Name=coaX {ECO:0000256|HAMAP-Rule:MF_01274};
ORFNames=AOD76_0202325 {ECO:0000313|EMBL:OKB27592.1};
Helicobacter pylori (Campylobacter pylori).
Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
Helicobacteraceae; Helicobacter.
NCBI_TaxID=210 {ECO:0000313|EMBL:OKB27592.1, ECO:0000313|Proteomes:UP000051935};
[1] {ECO:0000313|EMBL:OKB27592.1, ECO:0000313|Proteomes:UP000051935}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=UM276R {ECO:0000313|EMBL:OKB27592.1,
ECO:0000313|Proteomes:UP000051935};
Loke M.F., Vadivelu J., Tay A.C.Y., Thirriot F., Lee W.C., Goh K.L.,
Hanafi A.;
"The effects of Helicobacter pylori levofloxacin and metronidazole
resistance on the compensatory response.";
Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
first step in CoA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00384421}.
-!- CATALYTIC ACTIVITY: ATP + (R)-pantothenate = ADP + (R)-4'-
phosphopantothenate. {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00384435}.
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000256|SAAS:SAAS00611758};
-!- COFACTOR:
Name=NH4(+); Xref=ChEBI:CHEBI:28938;
Evidence={ECO:0000256|HAMAP-Rule:MF_01274};
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000256|HAMAP-Rule:MF_01274};
Note=A monovalent cation. Ammonium or potassium.
{ECO:0000256|HAMAP-Rule:MF_01274};
-!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
(R)-pantothenate: step 1/5. {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00384485}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00701620}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00384519}.
-!- SIMILARITY: Belongs to the type III pantothenate kinase family.
{ECO:0000256|HAMAP-Rule:MF_01274, ECO:0000256|SAAS:SAAS00701623}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:OKB27592.1}.
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EMBL; LJXK02000003; OKB27592.1; -; Genomic_DNA.
RefSeq; WP_058339441.1; NZ_LJXK02000003.1.
EnsemblBacteria; KRV53682; KRV53682; AOD76_05825.
EnsemblBacteria; KRV53958; KRV53958; AOD74_02840.
UniPathway; UPA00241; UER00352.
Proteomes; UP000051935; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004594; F:pantothenate kinase activity; IEA:UniProtKB-HAMAP.
GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-HAMAP.
HAMAP; MF_01274; Pantothen_kinase_3; 1.
InterPro; IPR004619; Type_III_PanK.
PANTHER; PTHR34265; PTHR34265; 1.
Pfam; PF03309; Pan_kinase; 1.
TIGRFAMs; TIGR00671; baf; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00088442};
Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00088444};
Complete proteome {ECO:0000313|Proteomes:UP000051935};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00088451};
Kinase {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00088438, ECO:0000313|EMBL:OKB27592.1};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01274};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00088442};
Potassium {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00461364};
Transferase {ECO:0000256|HAMAP-Rule:MF_01274,
ECO:0000256|SAAS:SAAS00088438, ECO:0000313|EMBL:OKB27592.1}.
NP_BIND 15 22 ATP. {ECO:0000256|HAMAP-Rule:MF_01274}.
REGION 83 86 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01274}.
ACT_SITE 85 85 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01274}.
METAL 100 100 Monovalent cation. {ECO:0000256|HAMAP-
Rule:MF_01274}.
BINDING 79 79 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01274}.
BINDING 103 103 ATP. {ECO:0000256|HAMAP-Rule:MF_01274}.
BINDING 155 155 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01274}.
SEQUENCE 221 AA; 24565 MW; 64C0EBDBF6D69547 CRC64;
MPECFKDLKD LVLCDIGNTC IHFAQNYQLF SSDKEDLKRL GIQKEIFYIS VNEENEKALL
NCYPNAKNIA GFFHLETDYV GLGIDRQMAC LAVNNGVIVD AGSAITIDLI QEGKHLGGCI
LPGLTQYIHA YQKSAKILEQ PFKALDSLEV LPKNTRDAVN YGMILSVISC IQHLAKNQKI
YLCGGDAKYL SAFLPHSVCK ERLVFDGMEI ALKKAGILEC K


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