PANK4_MACFA
ID PANK4_MACFA Reviewed; 773 AA.
AC Q4R4U1; Q2PFY2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=4'-phosphopantetheine phosphatase {ECO:0000250|UniProtKB:Q9NVE7};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q9NVE7};
DE AltName: Full=Inactive pantothenic acid kinase 4 {ECO:0000250|UniProtKB:Q9NVE7};
GN Name=PANK4; ORFNames=QccE-17245;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphatase which shows a preference for 4'-
CC phosphopantetheine and its oxidatively damaged forms (sulfonate or S-
CC sulfonate), providing strong indirect evidence that the phosphatase
CC activity pre-empts damage in the coenzyme A (CoA) pathway. Hydrolyzing
CC excess 4'-phosphopantetheine could constitute a directed overflow
CC mechanism to prevent its oxidation to the S-sulfonate, sulfonate, or
CC other forms. Hydrolyzing 4'-phosphopantetheine sulfonate or S-sulfonate
CC would forestall their conversion to inactive forms of CoA and acyl
CC carrier protein. May play a role in the physiological regulation of CoA
CC intracellular levels. {ECO:0000250|UniProtKB:Q9NVE7}.
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:Q9NVE7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68329;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
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:Q9NVE7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68337;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phospho-S-sulfopantetheine + H2O = (R)-S-
CC sulfopantetheine + phosphate; Xref=Rhea:RHEA:68340,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:177302,
CC ChEBI:CHEBI:177303; Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68341;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250|UniProtKB:Q9NVE7};
CC -!- ACTIVITY REGULATION: Activity is strongly promoted by Co(2+), Ni(2+),
CC Mg(2+) and Mn(2+). Activity is inhibited by EDTA.
CC {ECO:0000250|UniProtKB:Q9NVE7}.
CC -!- SUBUNIT: Homodimer. Interacts with PKM. {ECO:0000250|UniProtKB:Q923S8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q923S8}.
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:Q8K4K6}.
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 -!- CAUTION: Despite belonging to the type II pantothenate kinase family,
CC the pantothenate kinase domain contains a Val residue at position 147
CC and a Trp residue at position 211 instead of the two conserved active
CC site residues, Glu and Arg. Lacks pantothenate kinase activity.
CC {ECO:0000250|UniProtKB:Q9NVE7}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE72988.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB169803; BAE01884.1; -; mRNA.
DR EMBL; AB220455; BAE72988.1; ALT_INIT; mRNA.
DR RefSeq; NP_001270249.1; NM_001283320.1.
DR AlphaFoldDB; Q4R4U1; -.
DR SMR; Q4R4U1; -.
DR STRING; 9541.XP_005545066.1; -.
DR PRIDE; Q4R4U1; -.
DR GeneID; 101865764; -.
DR CTD; 55229; -.
DR eggNOG; KOG2201; Eukaryota.
DR eggNOG; KOG4584; Eukaryota.
DR OrthoDB; 865329at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; 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; 2.
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 Acetylation; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Hydrolase;
KW Manganese; Metal-binding; Nickel; Nitration; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT CHAIN 2..773
FT /note="4'-phosphopantetheine phosphatase"
FT /id="PRO_0000249247"
FT REGION 2..402
FT /note="Pantothenate kinase"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT REGION 403..773
FT /note="4'-phosphopantetheine phosphatase"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT MOTIF 724..728
FT /note="Subfamily II EGMGR motif"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT BINDING 196
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250"
FT BINDING 623
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 624
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 659
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic; for phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT MOD_RES 320
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80YV4"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVE7"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80YV4"
FT CONFLICT 176
FT /note="E -> G (in Ref. 1; BAE01884)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="D -> G (in Ref. 1; BAE01884)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 773 AA; 86011 MW; 2B8DD62B83A9B502 CRC64;
MAECGASGSG SSGDSLDKSI TLPPDEIFRN LENAKRFAID IGGSLTKLAY YSTVQHKVAK
VRSFDHSGKD TERDHEPPYE ISVQEEITAR LHFVKFENTY IEACLDFIKD HLVNTETKVI
QATGGGAYKF KDLIEEKLRL KVDKEDVMTC LIKGCNFVLK NIPHEAFVYQ KDSDPEFRFQ
TNHPHIFPYL LVNIGSGVSI VKVETEDRFE WVGGSSIGGG TFWGLGALLT KTKKFDELLH
LASRGQHSNV DMLVRDVYGG AHQTLGLSGN LIASSFGKSA TADQEFSKED MAKSLLHMIS
NDIGQLACLH ARLHSLDRVY FGGFFIRGHP VTMRTITYSI NFFSKGEVQA LFLRHEGYLG
AIGAFLKGAE QDNPNQYSWG ENYAGSSGLM STSPELGPAQ RARSGTFDLL EMDRLERPLV
NLPLLLDPPS YVPDTVDLTD DALARKYWLT CFEEALDGVV KRAVASQPDS VDAAERAEKF
RQKYWNKLQT LRQQPFAYGT LTVRSLLDTR EHCLNEFNFP DPYSKVKQRE NGVALRCFPG
VVRSLDTLGW EERQLALVKG LLAGNVFDWG AKAVSDVLES DPYFGFEEAK RKLQERPWLV
DSYSEWLQRL KGPPHKCALI FADNSGIDII LGVFPFVREL LLRGTEVILA CNSGPALNDV
THGESLIVAE RIAGMDPVVH SALREERLLL VQTGSSSPCL DLSRLDKGLA ALVRERGADL
VVIEGMGRAV HTNYHAALCC ESLKLAVIKN AWLAERLGGR LFSVIFKYEV PAE
