PANK1_ARATH
ID PANK1_ARATH Reviewed; 383 AA.
AC O80765; Q0WNV9; Q66GL8;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Pantothenate kinase 1 {ECO:0000303|PubMed:16897480};
DE Short=AtPANK1 {ECO:0000303|PubMed:16897480};
DE EC=2.7.1.33 {ECO:0000269|PubMed:12860978};
DE AltName: Full=AtCoaA {ECO:0000303|PubMed:12860978};
DE AltName: Full=Pantothenic acid kinase 1 {ECO:0000303|PubMed:16897480};
GN Name=PANK1; Synonyms=COAA; OrderedLocusNames=At1g60440; ORFNames=T13D8.31;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=cv. Columbia;
RX PubMed=12860978; DOI=10.1074/jbc.m306321200;
RA Kupke T., Hernandez-Acosta P., Culianez-Macia F.A.;
RT "4'-phosphopantetheine and coenzyme A biosynthesis in plants.";
RL J. Biol. Chem. 278:38229-38237(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16897480; DOI=10.1007/s11103-006-0037-4;
RA Tilton G.B., Wedemeyer W.J., Browse J., Ohlrogge J.;
RT "Plant coenzyme A biosynthesis: characterization of two pantothenate
RT kinases from Arabidopsis.";
RL Plant Mol. Biol. 61:629-642(2006).
CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate the first step
CC in CoA biosynthesis (PubMed:12860978). May play a role in the
CC physiological regulation of the intracellular CoA concentration
CC (PubMed:16897480). Functionally redudant with PANK2 (PubMed:16897480).
CC {ECO:0000269|PubMed:12860978, ECO:0000269|PubMed:16897480}.
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:0000269|PubMed:12860978};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16374;
CC Evidence={ECO:0000269|PubMed:12860978};
CC -!- ACTIVITY REGULATION: Regulated by feedback inhibition by malonyl-CoA.
CC {ECO:0000250}.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5. {ECO:0000269|PubMed:12860978}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves and developing seeds.
CC Expressed in roots, stems and flowers. {ECO:0000269|PubMed:16897480}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but homozygous double mutants pank1-1 and pank2-1 are
CC embryonic lethal. {ECO:0000269|PubMed:16897480}.
CC -!- SIMILARITY: Belongs to the type II pantothenate kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24069.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004473; AAC24069.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33687.1; -; Genomic_DNA.
DR EMBL; BT011005; AAR25641.1; -; mRNA.
DR EMBL; BT015384; AAU05507.1; -; mRNA.
DR EMBL; AK229327; BAF01190.1; -; mRNA.
DR RefSeq; NP_176247.2; NM_104731.5.
DR AlphaFoldDB; O80765; -.
DR SMR; O80765; -.
DR BioGRID; 27563; 1.
DR STRING; 3702.AT1G60440.1; -.
DR iPTMnet; O80765; -.
DR PaxDb; O80765; -.
DR PRIDE; O80765; -.
DR ProteomicsDB; 236324; -.
DR DNASU; 842339; -.
DR EnsemblPlants; AT1G60440.1; AT1G60440.1; AT1G60440.
DR GeneID; 842339; -.
DR Gramene; AT1G60440.1; AT1G60440.1; AT1G60440.
DR KEGG; ath:AT1G60440; -.
DR Araport; AT1G60440; -.
DR TAIR; locus:2195638; AT1G60440.
DR eggNOG; KOG2201; Eukaryota.
DR HOGENOM; CLU_011154_3_0_1; -.
DR InParanoid; O80765; -.
DR OMA; DDCVEFM; -.
DR OrthoDB; 865329at2759; -.
DR PhylomeDB; O80765; -.
DR UniPathway; UPA00241; UER00352.
DR PRO; PR:O80765; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O80765; baseline and differential.
DR Genevisible; O80765; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004594; F:pantothenate kinase activity; IDA:TAIR.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004567; Type_II_PanK.
DR PANTHER; PTHR12280; PTHR12280; 1.
DR Pfam; PF03630; Fumble; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00555; panK_eukar; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coenzyme A biosynthesis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..383
FT /note="Pantothenate kinase 1"
FT /id="PRO_0000161808"
SQ SEQUENCE 383 AA; 42421 MW; 328F97CE1A50A245 CRC64;
MDPTQISHLA LDIGGTLIKL VYFSANGDYS EESRNGCSVV KGRLCFAKFE TRKIDDCLEF
IRFNILHHSG VQQPNGEGHD KLYVKATGGG AFKFADLFKE KLGILFDKED EMCSLVGGVN
FLLKTVPREA FTYLDGQKKF VEIDHNDLYP YLLVNIGSGV SMIKVDGDGK YERISGTSLG
GGTFLGLGKL LTKCKSFDEL LELSHHGNNR VIDMLVGDIY GGTDYSKIGL SSTAIASSFG
KAISDGKELE DYQPEDVARS LLRMISNNIG QIAYLNALRF GLKRIFFGGF FIRGLEYTMD
TISVAVHFWS RGEAKAMFLR HEGFLGALGA FTSYNDQSHN DLKPHHHTVQ RAILNCSGHN
FRHIPVTSNL NESETIECSI NLV
