PANK2_ORYSJ
ID PANK2_ORYSJ Reviewed; 904 AA.
AC Q0J035; Q69SH7;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Pantothenate kinase 2 {ECO:0000250|UniProtKB:Q8L5Y9};
DE AltName: Full=Pantothenic acid kinase 2 {ECO:0000250|UniProtKB:Q8L5Y9};
DE Includes:
DE RecName: Full=Pantothenate kinase {ECO:0000250|UniProtKB:Q8L5Y9};
DE EC=2.7.1.33 {ECO:0000250|UniProtKB:Q8L5Y9};
DE Includes:
DE RecName: Full=4'-phosphopantetheine phosphatase {ECO:0000250|UniProtKB:Q8L5Y9};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q8L5Y9};
GN OrderedLocusNames=Os09g0533100, LOC_Os09g36270;
GN ORFNames=OJ1112_E07.4, P0515E01.23;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 150-904.
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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 (By similarity). 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 (By similarity). Hydrolyzing excess 4'-
CC phosphopantetheine could constitute a directed overflow mechanism to
CC prevent its oxidation to the S-sulfonate, sulfonate, or other forms (By
CC similarity). Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate
CC would forestall their conversion to inactive forms of CoA and acyl
CC carrier protein (By similarity). {ECO:0000250|UniProtKB:Q8L5Y9}.
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:0000250|UniProtKB:Q8L5Y9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16374;
CC Evidence={ECO:0000250|UniProtKB:Q8L5Y9};
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:0000250|UniProtKB:Q8L5Y9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68333;
CC Evidence={ECO:0000250|UniProtKB:Q8L5Y9};
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:0000250|UniProtKB:Q8L5Y9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68329;
CC Evidence={ECO:0000250|UniProtKB:Q8L5Y9};
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:0000250|UniProtKB:Q8L5Y9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68337;
CC Evidence={ECO:0000250|UniProtKB:Q8L5Y9};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8L5Y9};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250|UniProtKB:Q8L5Y9};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5. {ECO:0000250|UniProtKB:Q8L5Y9}.
CC -!- DOMAIN: Subfamily II proteins have an EGMGR motif about 50 residues
CC from the C-terminus (By similarity). This motif lies near the metal-
CC binding residues in the putative substrate-binding cleft 2 (By
CC similarity). Subfamily II proteins occur only in eukaryotes, in two
CC forms: as a stand-alone unit in plants, and as a C-terminal domain of
CC pantothenate kinases in plants, animals, and chytrid fungi (By
CC similarity). {ECO:0000250|UniProtKB:Q8L5Y9}.
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=BAD33319.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD46028.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP005092; BAD33319.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP005314; BAD46028.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008215; BAF25680.1; -; Genomic_DNA.
DR EMBL; AP014965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK106530; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015612123.1; XM_015756637.1.
DR AlphaFoldDB; Q0J035; -.
DR SMR; Q0J035; -.
DR STRING; 4530.OS09T0533100-01; -.
DR PaxDb; Q0J035; -.
DR PRIDE; Q0J035; -.
DR GeneID; 4347680; -.
DR KEGG; osa:4347680; -.
DR eggNOG; KOG2201; Eukaryota.
DR eggNOG; KOG4584; Eukaryota.
DR HOGENOM; CLU_012496_0_0_1; -.
DR InParanoid; Q0J035; -.
DR OrthoDB; 865329at2759; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR Genevisible; Q0J035; OS.
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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Coenzyme A biosynthesis; Hydrolase; Kinase; Manganese;
KW Metal-binding; Nickel; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..904
FT /note="Pantothenate kinase 2"
FT /id="PRO_0000429407"
FT REGION 1..472
FT /note="Pantothenate kinase"
FT /evidence="ECO:0000250|UniProtKB:Q8L5Y9"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..904
FT /note="4'-phosphopantetheine phosphatase"
FT /evidence="ECO:0000250|UniProtKB:Q8L5Y9"
FT MOTIF 855..859
FT /note="Subfamily II EGMGR motif"
FT /evidence="ECO:0000250|UniProtKB:Q8L5Y9"
FT BINDING 735
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 736
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 771
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic; for phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT CONFLICT 301
FT /note="Q -> R (in Ref. 4; AK106530)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 904 AA; 98951 MW; 5A7D92BFE64206E8 CRC64;
MAANNNSDPI LDEGGGGGVK HEAVGEAGEG KGGGGGAAAT QAPAAMLPRS GSRPQLDLSG
AAIHGNLEDR NPTILLPNQS DDISHLALDI GGSLIKLVYF SRHAEHSSED KRKLSTKRRL
GMLNGGRRSY PVLGGRLHFV KFETGKLNEC LDFISSKQLH RGGVDSPSWR SGAQPDNIVI
KATGGGAFKY ADLFKERLGV SLEKEDEMDC LVAGANFLLK SIRHEAFTHM DGQKEYVQID
QNDLFPFLLV NVGSGVSIIK VDGHGKFQRV SGTNVGGGTY WGLGRLMTKC KSFDELLELS
QRGDNSTIDM LVGDIYGGLD YSKIGLSAST IASSFGKTIS DDKELSDYRP EDISLSLLRM
ISYNIGQISY LNALRYGLKR IFFGGFFIRG HAYTMDTISF AVNFWSKGEA KAMFLRHEGF
LGALGAFMSY EKHGLDDLRI HHLVERFPMG APYVGGKIHG PPLGDLNEKI SWMEKFVQKG
TQITAPVPVG FPVTTGMGGF ERPTAKGDIL RSDASAALNV GVLHLVPTLD VFPLLEDPKM
YEPNTIDLDL NEYKYWFKIL SDHLPDLVDK AVASEGGTDD AKRRGDAFAH AFSAHLARLM
EEPAAYGKFG LANLLELREE CLREFQFVDA YVSIKQRENE ASLAVLPDLL MELDSMNEEA
RLLALIEGVL AANIFDWGSR ACVDLYHKGT IIEIYRMSRK KMQRPWRIDD FDMFKKRMLA
DKKGQPYKRA LLFVDNSGAD VVLGMIPLAR ELLRNGTEVV LVANSLPALN DVTANELPGI
VAEAAKHCGI LRKAAEAGGL IFDAMAGIQD DLKDEPVSVP LMVVENGCGS PCIDFRQVSS
ELAAAAKDAD LLILEGMGRS LHTNLNARFK CDTLKLAMVK NQRLAEKLFN GNIYDCICKF
EPVP
