PPTB_ASPFU
ID PPTB_ASPFU Reviewed; 153 AA.
AC Q4W9R0; E9QQI6; Q4FCS6;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=4'-phosphopantetheinyl transferase B, mitochondrial {ECO:0000303|PubMed:21195204};
DE Short=PPTase B {ECO:0000303|PubMed:21195204};
DE EC=2.7.8.7 {ECO:0000269|PubMed:21195204};
DE AltName: Full=Acyl-carrier-protein synthase pptB {ECO:0000303|PubMed:21195204};
DE AltName: Full=Phosphopantetheine:protein transferase pptB {ECO:0000303|PubMed:21195204};
GN Name=pptB {ECO:0000303|PubMed:21195204}; ORFNames=AFUA_4G04040;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=21195204; DOI=10.1016/j.fgb.2010.12.006;
RA Allen G., Bromley M., Kaye S.J., Keszenman-Pereyra D., Zucchi T.D.,
RA Price J., Birch M., Oliver J.D., Turner G.;
RT "Functional analysis of a mitochondrial phosphopantetheinyl transferase
RT (PPTase) gene pptB in Aspergillus fumigatus.";
RL Fungal Genet. Biol. 48:456-464(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Acyl-carrier-protein synthase transfers the 4'-
CC phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier-
CC protein (PubMed:21195204). The 4'-phosphopantetheine (4'-PPT) portion
CC of CoA provides the essential prosthetic group for a number of carrier
CC proteins and multi-domain enzymes, priming them for the acceptance of
CC acyl building blocks in fatty acid synthesis and many aspects of
CC secondary metabolism mediated by polyketide synthases (PKSs) and non-
CC ribosomal peptide synthetases (NRPSs) (PubMed:21195204). PptB is
CC specific for the mitochondrial acyl carrier protein acpA
CC (PubMed:21195204). {ECO:0000269|PubMed:21195204}.
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 Evidence={ECO:0000269|PubMed:21195204};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21195204}.
CC -!- DISRUPTION PHENOTYPE: Essential for viability (PubMed:21195204). Leads
CC to swollen spores in heterokaryons with a low germination rate and
CC arrest at this stage (PubMed:21195204). {ECO:0000269|PubMed:21195204}.
CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily.
CC {ECO:0000305}.
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DR EMBL; DQ092863; AAY99390.1; -; Genomic_DNA.
DR EMBL; AAHF01000016; EAL84553.1; -; Genomic_DNA.
DR RefSeq; XP_746591.1; XM_741498.1.
DR AlphaFoldDB; Q4W9R0; -.
DR SMR; Q4W9R0; -.
DR STRING; 746128.CADAFUBP00009617; -.
DR EnsemblFungi; EAL84553; EAL84553; AFUA_4G04040.
DR GeneID; 3503902; -.
DR KEGG; afm:AFUA_4G04040; -.
DR VEuPathDB; FungiDB:Afu4g04040; -.
DR eggNOG; ENOG502SDWS; Eukaryota.
DR HOGENOM; CLU_089696_4_2_1; -.
DR InParanoid; Q4W9R0; -.
DR OMA; FTRRILC; -.
DR OrthoDB; 1595195at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0005739; C:mitochondrion; IDA:AspGD.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IDA:AspGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.90.470.20; -; 1.
DR HAMAP; MF_00101; AcpS; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR002582; ACPS.
DR Pfam; PF01648; ACPS; 1.
DR SUPFAM; SSF56214; SSF56214; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; Reference proteome; Transferase.
FT CHAIN 1..153
FT /note="4'-phosphopantetheinyl transferase B, mitochondrial"
FT /id="PRO_0000444448"
SQ SEQUENCE 153 AA; 16789 MW; 8CF12548E8D54B1D CRC64;
MKLIPFPYPL NIGTDVVHLP RILRLINRPD YFHRFTRRIL HEQEQRDFRT RFSLPPPSSG
AEKTGLNPIT PDMARWLAGR FAAKEAARKA APAGASSLGW KDVIVRVGEA DKGRPEIVYL
DPMGCGETGG GRVGKLSISH DGDYVVATVL AAG
