(data stored in ACNUC7421 zone)

SWISSPROT: D6ZBT9_SEGRD

ID   D6ZBT9_SEGRD            Unreviewed;       259 AA.
AC   D6ZBT9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   RecName: Full=Type III pantothenate kinase {ECO:0000256|HAMAP-Rule:MF_01274};
DE            EC=2.7.1.33 {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=Srot_0429 {ECO:0000313|EMBL:ADG96916.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96916.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96916.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC       first step in CoA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01274,
CC       ECO:0000256|SAAS:SAAS00088441}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP
CC         + H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456216; EC=2.7.1.33; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01274, ECO:0000256|SAAS:SAAS01124593};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|SAAS:SAAS00611758};
CC   -!- COFACTOR:
CC       Name=NH4(+); Xref=ChEBI:CHEBI:28938; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01274};
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01274};
CC       Note=A monovalent cation. Ammonium or potassium.
CC       {ECO:0000256|HAMAP-Rule:MF_01274};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC       (R)-pantothenate: step 1/5. {ECO:0000256|HAMAP-Rule:MF_01274,
CC       ECO:0000256|SAAS:SAAS00088429}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01274,
CC       ECO:0000256|SAAS:SAAS00701620}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274,
CC       ECO:0000256|SAAS:SAAS00088436}.
CC   -!- SIMILARITY: Belongs to the type III pantothenate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01274, ECO:0000256|SAAS:SAAS00701623}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01274}.
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DR   EMBL; CP001958; ADG96916.1; -; Genomic_DNA.
DR   RefSeq; WP_013137372.1; NC_014168.1.
DR   STRING; 640132.Srot_0429; -.
DR   EnsemblBacteria; ADG96916; ADG96916; Srot_0429.
DR   KEGG; srt:Srot_0429; -.
DR   eggNOG; ENOG4105CGM; Bacteria.
DR   eggNOG; COG1521; LUCA.
DR   HOGENOM; HOG000066025; -.
DR   KO; K03525; -.
DR   OMA; HEPWLTL; -.
DR   OrthoDB; 2039419at2; -.
DR   BioCyc; SROT640132:G1GLH-430-MONOMER; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000002247; 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   HAMAP; MF_01274; Pantothen_kinase_3; 1.
DR   InterPro; IPR004619; Type_III_PanK.
DR   PANTHER; PTHR34265; PTHR34265; 1.
DR   Pfam; PF03309; Pan_kinase; 1.
DR   TIGRFAMs; TIGR00671; baf; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZBT9.
DR   SWISS-2DPAGE; D6ZBT9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01274,
KW   ECO:0000256|SAAS:SAAS00461390};
KW   Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_01274,
KW   ECO:0000256|SAAS:SAAS00461336};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274,
KW   ECO:0000256|SAAS:SAAS00461333};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01274,
KW   ECO:0000256|SAAS:SAAS00461374};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01274};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01274,
KW   ECO:0000256|SAAS:SAAS00461342};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_01274,
KW   ECO:0000256|SAAS:SAAS00173372};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01274,
KW   ECO:0000256|SAAS:SAAS00461385}.
FT   NP_BIND       6     13       ATP. {ECO:0000256|HAMAP-Rule:MF_01274}.
FT   REGION      109    112       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01274}.
FT   ACT_SITE    111    111       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01274}.
FT   METAL       131    131       Monovalent cation. {ECO:0000256|HAMAP-
FT                                Rule:MF_01274}.
FT   BINDING     134    134       ATP. {ECO:0000256|HAMAP-Rule:MF_01274}.
FT   BINDING     186    186       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01274}.
SQ   SEQUENCE   259 AA;  27265 MW;  75F326F53C2222FA CRC64;
     MLLVLDIGNS NVSFGLYEGS GSAARLVGSW RAHTDPKLTG DEIYLAAEGF LGEHIDRVDG
     VSALSTVPAL LRELRLMIPR YFPGRRSLVV EPGVRTGVPL LVDNPKGVGA DRVVNALAAF
     QQCQSACVVV DAGTTTVVDA VSAKGEFLGG AIAPGMAISV DALSQWAATI PKVELVRPRS
     VIGKSTVESL QSGVLFGFAG QVDGLVRRMI GEIGEARVVL TGGLAPLLVD ELATPFAHEP
     ALTLTGLRMV FERHIRSAR
//

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