(data stored in SCRATCH zone)

SWISSPROT: D3VHN3_XENNA

ID   D3VHN3_XENNA            Unreviewed;       316 AA.
AC   D3VHN3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Pantothenate kinase {ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000256|RuleBase:RU003530, ECO:0000256|SAAS:SAAS00765426};
DE            EC=2.7.1.33 {ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000256|RuleBase:RU003530, ECO:0000256|SAAS:SAAS00765418};
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:CBJ88372.1};
GN   OrderedLocusNames=XNC1_0289 {ECO:0000313|EMBL:CBJ88372.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88372.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88372.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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_00215, ECO:0000256|RuleBase:RU003530,
CC         ECO:0000256|SAAS:SAAS01123999};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC       (R)-pantothenate: step 1/5. {ECO:0000256|HAMAP-Rule:MF_00215,
CC       ECO:0000256|RuleBase:RU003530, ECO:0000256|SAAS:SAAS00765445}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00215,
CC       ECO:0000256|RuleBase:RU003530, ECO:0000256|SAAS:SAAS00768780}.
CC   -!- SIMILARITY: Belongs to the prokaryotic pantothenate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000256|RuleBase:RU003530,
CC       ECO:0000256|SAAS:SAAS00765429}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; FN667742; CBJ88372.1; -; Genomic_DNA.
DR   RefSeq; WP_013183215.1; NC_014228.1.
DR   STRING; 406817.XNC1_0289; -.
DR   EnsemblBacteria; CBJ88372; CBJ88372; XNC1_0289.
DR   KEGG; xne:XNC1_0289; -.
DR   eggNOG; ENOG4105CS9; Bacteria.
DR   eggNOG; COG1072; LUCA.
DR   HOGENOM; HOG000248571; -.
DR   KO; K00867; -.
DR   OMA; LMQRKGF; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000008075; Chromosome.
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   CDD; cd02025; PanK; 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   PANTHER; PTHR10285:SF139; PTHR10285:SF139; 1.
DR   Pfam; PF00485; PRK; 1.
DR   PIRSF; PIRSF000545; Pantothenate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00554; panK_bact; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VHN3.
DR   SWISS-2DPAGE; D3VHN3.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00215,
KW   ECO:0000256|SAAS:SAAS00768779};
KW   Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00215,
KW   ECO:0000256|RuleBase:RU003530, ECO:0000256|SAAS:SAAS00765455};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00215,
KW   ECO:0000256|RuleBase:RU003530, ECO:0000256|SAAS:SAAS00768784};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00215,
KW   ECO:0000256|SAAS:SAAS00768783, ECO:0000313|EMBL:CBJ88372.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00215,
KW   ECO:0000256|SAAS:SAAS00768775};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00215,
KW   ECO:0000256|SAAS:SAAS00768777, ECO:0000313|EMBL:CBJ88372.1}.
FT   DOMAIN       90    243       PRK. {ECO:0000259|Pfam:PF00485}.
FT   NP_BIND      95    102       ATP. {ECO:0000256|HAMAP-Rule:MF_00215}.
SQ   SEQUENCE   316 AA;  36262 MW;  B9368259434119A5 CRC64;
     MNNKESFLTT PYLQFDREHW ATLRDSVPLT LTEEEVVALK GINEEISINE VVEIYLPLSR
     LLNFYISSNL RRQAVLEQFL GTDEQKVPYV IGIAGSVAVG KSTTARLLQA LLSRWPEHRR
     VKLVTTDGFL HSNNVLNERG LMKKKGFPES YDMRSLVKFV ADIKSGTEKV SAPVYSHLSY
     DIVPNEQLII EKPDILILEG LNVLQSGMDY PHEPHHVFVS DFVDFSIYVD ASEELLEQWY
     ISRFLKFRQG AFSDPDSYFH DYSKLTTEEA IKIASNIWQE INGLNLQQNI LPTRERASLI
     MTKGNNHSIE SVRLRK
//

If you have problems or comments...

PBIL Back to PBIL home page