(data stored in ACNUC7421 zone)

SWISSPROT: C8W3U5_DESAS

ID   C8W3U5_DESAS            Unreviewed;       254 AA.
AC   C8W3U5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 65.
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=Dtox_0246 {ECO:0000313|EMBL:ACV61199.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61199.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61199.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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}.
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DR   EMBL; CP001720; ACV61199.1; -; Genomic_DNA.
DR   RefSeq; WP_015755920.1; NC_013216.1.
DR   STRING; 485916.Dtox_0246; -.
DR   EnsemblBacteria; ACV61199; ACV61199; Dtox_0246.
DR   KEGG; dae:Dtox_0246; -.
DR   eggNOG; ENOG4105CGM; Bacteria.
DR   eggNOG; COG1521; LUCA.
DR   HOGENOM; HOG000066025; -.
DR   KO; K03525; -.
DR   OMA; HEPWLTL; -.
DR   OrthoDB; 2039419at2; -.
DR   BioCyc; DACE485916:G1GFV-251-MONOMER; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000002217; 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; C8W3U5.
DR   SWISS-2DPAGE; C8W3U5.
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:UP000002217};
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:UP000002217};
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      107    110       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01274}.
FT   ACT_SITE    109    109       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01274}.
FT   METAL       129    129       Monovalent cation. {ECO:0000256|HAMAP-
FT                                Rule:MF_01274}.
FT   BINDING     100    100       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01274}.
FT   BINDING     132    132       ATP. {ECO:0000256|HAMAP-Rule:MF_01274}.
FT   BINDING     184    184       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01274}.
SQ   SEQUENCE   254 AA;  27445 MW;  6A929308FDB5A7CD CRC64;
     MLLVFDVGNT NIVLGLYSKK KLLENWRIST DRGCTADEYG ILVRSLFASC SIPTGEVRAM
     VISSVVPPLM STLEEMSKKY FKVAPLFVGP GVKTGIAIKY DNPKEVGADR IVNAVAGYEL
     YRGPLVIVDF GTATTFCAVS EKGEYLGGAI APGIGISAEA LFSRAAKLSR VDIVKPELAI
     AKNTVNSMQA GIFYGFVGQV KELVRRIKQE MSGNPYVVAT GGFAALIAQE TDNIDKVDPF
     LTLTGLRIIY ERNC
//

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