ID   COAD_METTH              Reviewed;         164 AA.
AC   O27918;
DT   06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2003, sequence version 2.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00647};
DE            EC=2.7.7.3 {ECO:0000255|HAMAP-Rule:MF_00647};
DE   AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00647};
DE   AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00647};
DE            Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00647};
GN   Name=coaD {ECO:0000255|HAMAP-Rule:MF_00647}; OrderedLocusNames=MTH_1896;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC       phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_00647}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA +
CC         diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328,
CC         ChEBI:CHEBI:61723; EC=2.7.7.3; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00647};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00647}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00647}.
CC   -!- SIMILARITY: Belongs to the eukaryotic CoaD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00647}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB86356.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000666; AAB86356.1; ALT_INIT; Genomic_DNA.
DR   PIR; A69120; A69120.
DR   RefSeq; WP_048061166.1; NC_000916.1.
DR   AlphaFoldDB; O27918; -.
DR   SMR; O27918; -.
DR   STRING; 187420.MTH_1896; -.
DR   EnsemblBacteria; AAB86356; AAB86356; MTH_1896.
DR   GeneID; 1470981; -.
DR   KEGG; mth:MTH_1896; -.
DR   PATRIC; fig|187420.15.peg.1847; -.
DR   HOGENOM; CLU_035272_5_0_2; -.
DR   OMA; FDTLHSG; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00647; PPAT_arch; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR023540; PPAT_arch.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..164
FT                   /note="Phosphopantetheine adenylyltransferase"
FT                   /id="PRO_0000156323"
SQ   SEQUENCE   164 AA;  18791 MW;  88A24D0F81C470F0 CRC64;
     MKRKYSLVAV GGTFDRFHKG HRRLLDEAFR VGETVMIGVT SDEFAAAKGE GIEPCSVRMK
     NLEEYLRDKD ADYHVMRLDD PYGTTVTDEA FEAIVVSRET EPVAREINAI RRNRGFRELD
     IITIDMVNAD DGIPISSTRI RRGEIDPMGH IIKRIRGALR RRRE