UniProt: A0A0Q8YY31

Database: UniProt
Entry: A0A0Q8YY31_9ACTN

LinkDB:  A0A0Q8YY31_9ACTN 
Original site:  A0A0Q8YY31_9ACTN

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (4)   
   InterPro (3)   
   Pfam (1)   
All databases (12)   

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ID   A0A0Q8YY31_9ACTN        Unreviewed;       322 AA.
AC   A0A0Q8YY31;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
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   ORFNames=ASE41_09040 {ECO:0000313|EMBL:KRC95856.1};
OS   Streptomyces sp. Root264.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1736503 {ECO:0000313|EMBL:KRC95856.1, ECO:0000313|Proteomes:UP000051177};
RN   [1] {ECO:0000313|EMBL:KRC95856.1, ECO:0000313|Proteomes:UP000051177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root264 {ECO:0000313|EMBL:KRC95856.1,
RC   ECO:0000313|Proteomes:UP000051177};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC95856.1, ECO:0000313|Proteomes:UP000051177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root264 {ECO:0000313|EMBL:KRC95856.1,
RC   ECO:0000313|Proteomes:UP000051177};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KRC95856.1}.
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DR   EMBL; LMIZ01000078; KRC95856.1; -; Genomic_DNA.
DR   RefSeq; WP_057584662.1; NZ_LMIZ01000078.1.
DR   AlphaFoldDB; A0A0Q8YY31; -.
DR   STRING; 1736503.ASE41_09040; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000051177; 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:KRC95856.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051177};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000313|EMBL:KRC95856.1}.
FT   DOMAIN          95..239
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
FT   BINDING         100..107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00215"
SQ   SEQUENCE   322 AA;  36392 MW;  CCE9F4046846BD9B CRC64;
     MPRSAHRHKP EATPYVDLTR SEWSALREKT PLPLTAEELE KLRGLGDVID LDEVRDIYLP
     LSRLLNLYVG ATDGLRGALN TFLGEKGSQS GTPFVIGVAG SVAVGKSTVA RLLQALLSRW
     PEHPRVELVT TDGFLLPTRE LEARGLMSRK GFPESYDRRA LTRFVADIKA GKGEVTAPVY
     SHLIYDIVPD RRLAVRRPDI LIVEGLNVLQ PALPGSDGRT RVGLADYFDF SVYVDASTED
     IERWYLSRFR KLRQTAFQNP DSYFRKYTQV SEEEALDYAR TLWRTINKPN LVENIAPTRG
     RAGLVVRKGP DHKVQRLRLR KL
//

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