PANK2_ARATH
ID PANK2_ARATH Reviewed; 901 AA.
AC Q8L5Y9; O49372; O49374;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Pantothenate kinase 2 {ECO:0000303|PubMed:16897480};
DE Short=AtPANK2 {ECO:0000303|PubMed:16897480};
DE AltName: Full=Pantothenic acid kinase 2 {ECO:0000303|PubMed:16897480};
DE Includes:
DE RecName: Full=Pantothenate kinase {ECO:0000303|PubMed:16897480};
DE EC=2.7.1.33 {ECO:0000269|PubMed:16897480};
DE Includes:
DE RecName: Full=4'-phosphopantetheine phosphatase {ECO:0000303|PubMed:27322068};
DE EC=3.1.3.- {ECO:0000269|PubMed:27322068};
GN Name=PANK2; OrderedLocusNames=At4g32180; ORFNames=F10M6.180, F10N7.10;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-901.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, 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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND COFACTOR.
RX PubMed=27322068; DOI=10.1038/nchembio.2108;
RA Huang L., Khusnutdinova A., Nocek B., Brown G., Xu X., Cui H., Petit P.,
RA Flick R., Zallot R., Balmant K., Ziemak M.J., Shanklin J.,
RA de Crecy-Lagard V., Fiehn O., Gregory J.F. III, Joachimiak A.,
RA Savchenko A., Yakunin A.F., Hanson A.D.;
RT "A family of metal-dependent phosphatases implicated in metabolite damage-
RT control.";
RL Nat. Chem. Biol. 12:621-627(2016).
CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate the first step
CC in CoA biosynthesis. May play a role in the physiological regulation of
CC the intracellular CoA concentration. Functionally redudant with PANK1
CC (PubMed:16897480). The phosphatase activity shows preference for normal
CC or oxidatively damaged intermediates of 4'-phosphopantetheine, which
CC provides strong indirect evidence that the phosphatase activity pre-
CC empts damage in the CoA pathway (PubMed:27322068). Hydrolyzing excess
CC 4'-phosphopantetheine could constitute a directed overflow mechanism to
CC prevent its oxidation to the S-sulfonate, sulfonate, or other forms
CC (PubMed:27322068). Hydrolyzing 4'-phosphopantetheine sulfonate or S-
CC sulfonate would forestall their conversion to inactive forms of CoA and
CC acyl carrier protein (PubMed:27322068). {ECO:0000269|PubMed:16897480,
CC ECO:0000269|PubMed:27322068}.
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:16897480};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16374;
CC Evidence={ECO:0000305|PubMed:16897480};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantothenate + H2O = (R)-pantothenate +
CC phosphate; Xref=Rhea:RHEA:68332, ChEBI:CHEBI:10986,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29032, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000269|PubMed:27322068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68333;
CC Evidence={ECO:0000305|PubMed:27322068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantetheine + H2O = (R)-pantetheine + phosphate;
CC Xref=Rhea:RHEA:68328, ChEBI:CHEBI:15377, ChEBI:CHEBI:16753,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:61723;
CC Evidence={ECO:0000269|PubMed:27322068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68329;
CC Evidence={ECO:0000305|PubMed:27322068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantetheine sulfonate + H2O = (R)-pantetheine
CC sulfonate + phosphate; Xref=Rhea:RHEA:68336, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:177300, ChEBI:CHEBI:177301;
CC Evidence={ECO:0000269|PubMed:27322068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68337;
CC Evidence={ECO:0000305|PubMed:27322068};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:27322068};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:27322068};
CC Note=Phosphatase activity is strongly promoted by several divalent
CC cation ions but is it suggested that Mn(2+) and possibly Ni(2+)
CC represent biologically relevant metal ion cofactors for damage-control
CC phosphatases. {ECO:0000269|PubMed:27322068};
CC -!- ACTIVITY REGULATION: Activity is strongly promoted by Co(2+), Ni(2+)
CC and Mn(2+) (PubMed:27322068). Activity is inhibited by EDTA
CC (PubMed:27322068). {ECO:0000269|PubMed:27322068}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=640 uM for p-nitrophenylphosphate {ECO:0000269|PubMed:27322068};
CC KM=18.9 uM for phosphopantetheine {ECO:0000269|PubMed:27322068};
CC KM=2.91 uM for 4'-phosphopantotheine-S-sulfonate
CC {ECO:0000269|PubMed:27322068};
CC KM=0.28 uM for 4'-phosphopantothenate {ECO:0000269|PubMed:27322068};
CC Note=kcat is 1.99 sec(-1) with p-nitrophenylphosphate as substrate.
CC kcat is 0.26 sec(-1) with phosphopantetheine as substrate. kcat is
CC 0.94 sec(-1) with 4'-phosphopantotheine-S-sulfonate as substrate.
CC kcat is 0.52 sec(-1) with 4'-phosphopantothenate as substrate.
CC {ECO:0000269|PubMed:27322068};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5. {ECO:0000269|PubMed:16897480}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q8L5Y9-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves and developing seeds.
CC Expressed in roots, stems and flowers. {ECO:0000269|PubMed:16897480}.
CC -!- DOMAIN: Subfamily II proteins have an EGMGR motif about 50 residues
CC from the C-terminus (Probable). This motif lies near the metal-binding
CC residues in the putative substrate-binding cleft 2 (Probable).
CC Subfamily II proteins occur only in eukaryotes, in two forms: as a
CC stand-alone unit in plants, and as a C-terminal domain of pantothenate
CC kinases in plants, animals, and chytrid fungi (Probable).
CC {ECO:0000305|PubMed:27322068}.
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: In the N-terminal section; belongs to the type II
CC pantothenate kinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the damage-control
CC phosphatase family. Phosphopantetheine phosphatase II subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16571.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA16972.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79936.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021636; CAA16571.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL021811; CAA16972.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161580; CAB79936.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86015.1; -; Genomic_DNA.
DR EMBL; AY099839; AAM20690.1; -; mRNA.
DR RefSeq; NP_194945.3; NM_119370.5. [Q8L5Y9-1]
DR AlphaFoldDB; Q8L5Y9; -.
DR SMR; Q8L5Y9; -.
DR BioGRID; 14637; 3.
DR IntAct; Q8L5Y9; 1.
DR STRING; 3702.AT4G32180.1; -.
DR iPTMnet; Q8L5Y9; -.
DR PaxDb; Q8L5Y9; -.
DR PRIDE; Q8L5Y9; -.
DR ProteomicsDB; 226054; -. [Q8L5Y9-1]
DR EnsemblPlants; AT4G32180.1; AT4G32180.1; AT4G32180. [Q8L5Y9-1]
DR GeneID; 829351; -.
DR Gramene; AT4G32180.1; AT4G32180.1; AT4G32180. [Q8L5Y9-1]
DR KEGG; ath:AT4G32180; -.
DR Araport; AT4G32180; -.
DR TAIR; locus:2116490; AT4G32180.
DR eggNOG; KOG2201; Eukaryota.
DR eggNOG; KOG4584; Eukaryota.
DR InParanoid; Q8L5Y9; -.
DR BioCyc; ARA:AT4G32180-MON; -.
DR BioCyc; MetaCyc:AT4G32180-MON; -.
DR UniPathway; UPA00241; UER00352.
DR PRO; PR:Q8L5Y9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L5Y9; baseline and differential.
DR Genevisible; Q8L5Y9; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004594; F:pantothenate kinase activity; IGI:TAIR.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1700.10; -; 1.
DR InterPro; IPR036075; ARMT-1-like_metal-bd_sf.
DR InterPro; IPR002791; ARMT1-like_metal-bd.
DR InterPro; IPR035073; At2g17340_3_helix_bundle.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR015844; PanK_long.
DR InterPro; IPR004567; Type_II_PanK.
DR PANTHER; PTHR12280; PTHR12280; 1.
DR Pfam; PF01937; ARMT1-like_dom; 1.
DR Pfam; PF03630; Fumble; 1.
DR PIRSF; PIRSF036939; PanK_long; 1.
DR SUPFAM; SSF111321; SSF111321; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00555; panK_eukar; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coenzyme A biosynthesis; Hydrolase;
KW Kinase; Manganese; Metal-binding; Nickel; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..901
FT /note="Pantothenate kinase 2"
FT /id="PRO_0000161809"
FT REGION 1..466
FT /note="Pantothenate kinase"
FT /evidence="ECO:0000305|PubMed:27322068"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..901
FT /note="4'-phosphopantetheine phosphatase"
FT /evidence="ECO:0000305|PubMed:27322068"
FT MOTIF 851..855
FT /note="Subfamily II EGMGR motif"
FT /evidence="ECO:0000305|PubMed:27322068"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 731
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic; for phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 732
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic; for phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 767
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic; for phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
SQ SEQUENCE 901 AA; 99640 MW; BF5176A4B06B8108 CRC64;
MAGQEDEYDP ILDNKREAEA KSQVSVAADK NMAPSTSGTP IHRSGSRPQL DLSKAEIQGN
LEERDPTILL PNQSDDISHL ALDIGGSLIK LLYFSRHEDY SNDDDKRKRT IKERLGITNG
NLRSYPVLGG RLHFVKFETH KINECLDFIH SKQLHRRDPY PWSSKTLPLG TGVIKVTGGG
AFKFADLFKE RLGVSIEKED EMHCLVSGAN FLLKAIRHEA FTHMEGEKEF VQIDPNDLYP
YLLVNVGSGV SIIKVDGEGK FERVSGTNVG GGTYWGLGRL LTKCKSFDEL LELSQKGDNS
AIDMLVGDIY GGMDYSKIGL SASTIASSFG KAISENKELD DYRPEDISLS LLRMISYNIG
QISYLNALRF GLKRIFFGGF FIRGHAYTMD TISFAVHFWS KGEMQAMFLR HEGFLGALGA
FMSYEKHGLD DLMSHQLVER FPMGAPYTGG NIHGPPLGDL DEKISWMEKF VRRGTEITAP
VPMTPSKTTG LGGFEVPSSR GSALRSDASA LNVGVLHLVP TLEVFPLLAD PKTYEPNTID
LSDQGEREYW LKVLSEHLPD LVDTAVASEG GTEDAKRRGD AFARAFSAHL ARLMEEPAAY
GKLGLANLLE LREECLREFQ FVDAYRSIKQ RENEASLAVL PDLLEELDSM SEEARLLTLI
EGVLAANIFD WGSRACVDLY HKGTIIEIYR MSRNKMQRPW RVDDFDAFKE RMLGSGGKQP
HRHKRALLFV DNSGADVILG MLPLAREFLR RGTEVVLVAN SLPALNDVTA MELPDIVAGA
AKHCDILRRA AEMGGLLVDA MVNPGDGSKK DSTSAPLMVV ENGCGSPCID LRQVSSELAA
AAKDADLVVL EGMGRALHTN FNAQFQCEAL KLAMVKNQRL AEKLIKGNIY DCVCRYEPPS
L
