PPTA_EMENI
ID PPTA_EMENI Reviewed; 344 AA.
AC G5EB87; A0A1U8QGT1; C8V2B5; Q5AZZ0; Q9UVK7;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=4'-phosphopantetheinyl transferase NpgA;
DE Short=PPTase;
DE EC=2.7.8.7 {ECO:0000269|PubMed:12127488, ECO:0000269|PubMed:18805498, ECO:0000269|PubMed:25557478};
GN Name=npgA; Synonyms=cfwA; ORFNames=ANIA_06140;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=25557478; DOI=10.1007/s12275-015-4657-8;
RA Kim J.M., Song H.Y., Choi H.J., So K.K., Kim D.H., Chae K.S., Han D.M.,
RA Jahng K.Y.;
RT "Characterization of NpgA, a 4'-phosphopantetheinyl transferase of
RT Aspergillus nidulans, and evidence of its involvement in fungal growth and
RT formation of conidia and cleistothecia for development.";
RL J. Microbiol. 53:21-31(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP CATALYTIC ACTIVITY.
RX PubMed=12127488; DOI=10.1111/j.1574-6968.2002.tb11285.x;
RA Mootz H.D., Schoergendorfer K., Marahiel M.A.;
RT "Functional characterization of 4'-phosphopantetheinyl transferase genes of
RT bacterial and fungal origin by complementation of Saccharomyces cerevisiae
RT lys5.";
RL FEMS Microbiol. Lett. 213:51-57(2002).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF ASP-20 AND LEU-217.
RX PubMed=12664133; DOI=10.1007/s00294-003-0382-7;
RA Keszenman-Pereyra D., Lawrence S., Twfieg M.E., Price J., Turner G.;
RT "The npgA/cfwA gene encodes a putative 4'-phosphopantetheinyl transferase
RT which is essential for penicillin biosynthesis in Aspergillus nidulans.";
RL Curr. Genet. 43:186-190(2003).
RN [6]
RP FUNCTION.
RX PubMed=14508603; DOI=10.1007/s00294-003-0434-z;
RA Oberegger H., Eisendle M., Schrettl M., Graessle S., Haas H.;
RT "4'-phosphopantetheinyl transferase-encoding npgA is essential for
RT siderophore biosynthesis in Aspergillus nidulans.";
RL Curr. Genet. 44:211-215(2003).
RN [7]
RP FUNCTION.
RX PubMed=17277172; DOI=10.1128/ec.00362-06;
RA Marquez-Fernandez O., Trigos A., Ramos-Balderas J.L., Viniegra-Gonzalez G.,
RA Deising H.B., Aguirre J.;
RT "Phosphopantetheinyl transferase CfwA/NpgA is required for Aspergillus
RT nidulans secondary metabolism and asexual development.";
RL Eukaryot. Cell 6:710-720(2007).
RN [8]
RP CATALYTIC ACTIVITY.
RX PubMed=18805498; DOI=10.1016/j.fgb.2008.08.009;
RA Schneider P., Bouhired S., Hoffmeister D.;
RT "Characterization of the atromentin biosynthesis genes and enzymes in the
RT homobasidiomycete Tapinella panuoides.";
RL Fungal Genet. Biol. 45:1487-1496(2008).
CC -!- FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to
CC a Ser of an acyl-carrier-protein. The enzyme is able to transfer the
CC cofactor to a broad range of enzymes with acyl- or peptidyl-carrier
CC protein domains. Required for primary biological processes such as
CC growth and asexual/sexual development, and activates target enzymes
CC involved in the synthesis of metabolites such as fatty acids,
CC polyketides and nonribosomal peptides, lysine, siderophore, penicillin,
CC sterigmatocystin, shamixantone, dehydroaustinol, and pigments.
CC {ECO:0000269|PubMed:12664133, ECO:0000269|PubMed:14508603,
CC ECO:0000269|PubMed:17277172, ECO:0000269|PubMed:25557478}.
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:12127488, ECO:0000269|PubMed:18805498,
CC ECO:0000269|PubMed:25557478};
CC -!- DISRUPTION PHENOTYPE: Essential for growth.
CC {ECO:0000269|PubMed:25557478}.
CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily.
CC {ECO:0000305}.
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DR EMBL; AF198117; AAF12814.1; -; Genomic_DNA.
DR EMBL; AACD01000105; EAA57926.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF70101.1; -; Genomic_DNA.
DR RefSeq; XP_663744.1; XM_658652.1.
DR AlphaFoldDB; G5EB87; -.
DR SMR; G5EB87; -.
DR STRING; 162425.CADANIAP00006870; -.
DR EnsemblFungi; CBF70101; CBF70101; ANIA_06140.
DR EnsemblFungi; EAA57926; EAA57926; AN6140.2.
DR GeneID; 2870872; -.
DR KEGG; ani:AN6140.2; -.
DR eggNOG; ENOG502SA2B; Eukaryota.
DR HOGENOM; CLU_031126_1_1_1; -.
DR InParanoid; G5EB87; -.
DR OMA; RWYIDTR; -.
DR OrthoDB; 960416at2759; -.
DR BRENDA; 2.7.8.7; 517.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
DR Gene3D; 3.90.470.20; -; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR Pfam; PF01648; ACPS; 1.
DR SUPFAM; SSF56214; SSF56214; 2.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..344
FT /note="4'-phosphopantetheinyl transferase NpgA"
FT /id="PRO_0000442635"
FT MUTAGEN 20
FT /note="D->G: In cfwA2; abolishes penicillin biosynthesis;
FT when associated with R-217."
FT MUTAGEN 217
FT /note="L->R: In cfwA2; abolishes penicillin biosynthesis;
FT when associated with G-20."
SQ SEQUENCE 344 AA; 37711 MW; F96E0F662CDE9C20 CRC64;
MVQDTSSAST SPILTRWYID TRPLTASTAA LPLLETLQPA DQISVQKYYH LKDKHMSLAS
NLLKYLFVHR NCRIPWSSIV ISRTPDPHRR PCYIPPSGSQ EDSFKDGYTG INVEFNVSHQ
ASMVAIAGTA FTPNSGGDSK LKPEVGIDIT CVNERQGRNG EERSLESLRQ YIDIFSEVFS
TAEMANIRRL DGVSSSSLSA DRLVDYGYRL FYTYWALKEA YIKMTGEALL APWLRELEFS
NVVAPAAVAE SGDSAGDFGE PYTGVRTTLY KNLVEDVRIE VAALGGDYLF ATAARGGGIG
ASSRPGGGPD GSGIRSQDPW RPFKKLDIER DIQPCATGVC NCLS
