PPT2_YEAST
ID PPT2_YEAST Reviewed; 173 AA.
AC Q12036; D6W3M1;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
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=YPL148C; ORFNames=P2604;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9712852; DOI=10.1074/jbc.273.35.22334;
RA Stuible H.-P., Meier S., Wagner C., Hannappel E., Schweizer E.;
RT "A novel phosphopantetheine:protein transferase activating yeast
RT mitochondrial acyl carrier protein.";
RL J. Biol. Chem. 273:22334-22339(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
CC -!- FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to
CC a Ser of mitochondrial acyl-carrier-protein.
CC {ECO:0000269|PubMed:9712852}.
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:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Present with 486 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS56460.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA65545.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA76138.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA97853.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y16253; CAA76138.1; ALT_INIT; Genomic_DNA.
DR EMBL; X96770; CAA65545.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z73504; CAA97853.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY558134; AAS56460.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006949; DAA11287.1; -; Genomic_DNA.
DR PIR; S65159; S65159.
DR RefSeq; NP_015177.2; NM_001183962.1.
DR AlphaFoldDB; Q12036; -.
DR SMR; Q12036; -.
DR BioGRID; 36035; 225.
DR IntAct; Q12036; 1.
DR STRING; 4932.YPL148C; -.
DR MaxQB; Q12036; -.
DR PaxDb; Q12036; -.
DR PRIDE; Q12036; -.
DR EnsemblFungi; YPL148C_mRNA; YPL148C; YPL148C.
DR GeneID; 855955; -.
DR KEGG; sce:YPL148C; -.
DR SGD; S000006069; PPT2.
DR VEuPathDB; FungiDB:YPL148C; -.
DR eggNOG; ENOG502S43T; Eukaryota.
DR HOGENOM; CLU_089696_4_1_1; -.
DR InParanoid; Q12036; -.
DR OMA; IVYLPRF; -.
DR BioCyc; YEAST:G3O-34045-MON; -.
DR BRENDA; 2.7.8.7; 984.
DR PRO; PR:Q12036; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12036; protein.
DR GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IDA:SGD.
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; IDA:SGD.
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 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Mitochondrion; Reference proteome; Transferase.
FT CHAIN 1..173
FT /note="Mitochondrial holo-[acyl-carrier-protein] synthase"
FT /id="PRO_0000175745"
SQ SEQUENCE 173 AA; 19973 MW; 21C96AAFE4F9D2EA CRC64;
MSFASRNIGR KIAGVGVDIV YLPRFAHILE KYSPFDPCGR STLNKITRKF MHEKERFHFS
NLLIEENCLT PRLHEYIAGV WALKECSLKA LCCCVSKHDL PPAQVLYAGM LYKTQTDTGV
PQLEFDKMFG KKYPKYQQLS KNYDSLFSTH EFLVSLSHDK DYLIAVTNLV ERE
