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PPT2_CANGA
ID   PPT2_CANGA              Reviewed;         152 AA.
AC   Q6FJZ5;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Mitochondrial holo-[acyl-carrier-protein] synthase;
DE            Short=Mitochondrial holo-ACP synthase;
DE            EC=2.7.8.7;
DE   AltName: Full=4'-phosphopantetheinyl transferase PPT2;
DE            Short=PPTase;
GN   Name=PPT2; OrderedLocusNames=CAGL0M02365g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to
CC       a Ser of mitochondrial acyl-carrier-protein. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-
CC         [ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC         COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.
CC       {ECO:0000305}.
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DR   EMBL; CR380959; CAG62425.1; -; Genomic_DNA.
DR   RefSeq; XP_449449.1; XM_449449.1.
DR   AlphaFoldDB; Q6FJZ5; -.
DR   SMR; Q6FJZ5; -.
DR   STRING; 5478.XP_449449.1; -.
DR   EnsemblFungi; CAG62425; CAG62425; CAGL0M02365g.
DR   GeneID; 2891457; -.
DR   KEGG; cgr:CAGL0M02365g; -.
DR   CGD; CAL0136693; CAGL0M02365g.
DR   VEuPathDB; FungiDB:CAGL0M02365g; -.
DR   eggNOG; ENOG502S43T; Eukaryota.
DR   HOGENOM; CLU_089696_4_1_1; -.
DR   InParanoid; Q6FJZ5; -.
DR   OMA; IVYLPRF; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0031108; P:holo-[acyl-carrier-protein] biosynthetic process; IEA:EnsemblFungi.
DR   Gene3D; 3.90.470.20; -; 1.
DR   InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR   InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR   InterPro; IPR016614; PPTase_2.
DR   Pfam; PF01648; ACPS; 1.
DR   PIRSF; PIRSF013370; ACPS_fun; 1.
DR   SUPFAM; SSF56214; SSF56214; 1.
PE   3: Inferred from homology;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Mitochondrion; Reference proteome; Transferase.
FT   CHAIN           1..152
FT                   /note="Mitochondrial holo-[acyl-carrier-protein] synthase"
FT                   /id="PRO_0000175744"
SQ   SEQUENCE   152 AA;  17018 MW;  22DA302618D2AE01 CRC64;
     MSVLGVGCDV VHLPRMHRLL TKYDAGSRGF QRVVSKFMHP TERIALGVDG ASLSAGQIRY
     IAGTWALKEA ALKALHCAAP LHTVLPPAMF IYTKLLYRQR RSNGVPQLLL DNEALRLDQL
     QFLRQAKFLS TLSHDNEYLV AYTTLIDTKN LV
 
 
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