COAD_PYRHO
ID COAD_PYRHO Reviewed; 158 AA.
AC O58358;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2003, sequence version 2.
DT 25-MAY-2022, entry version 110.
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=PH0624;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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=BAA29713.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000001; BAA29713.1; ALT_INIT; Genomic_DNA.
DR PIR; G71106; G71106.
DR AlphaFoldDB; O58358; -.
DR SMR; O58358; -.
DR STRING; 70601.3257030; -.
DR EnsemblBacteria; BAA29713; BAA29713; BAA29713.
DR KEGG; pho:PH0624; -.
DR eggNOG; arCOG01223; Archaea.
DR OMA; FDTLHSG; -.
DR OrthoDB; 93412at2157; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000000752; 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; Transferase.
FT CHAIN 1..158
FT /note="Phosphopantetheine adenylyltransferase"
FT /id="PRO_0000156327"
SQ SEQUENCE 158 AA; 17898 MW; 4EAF3820AC278C48 CRC64;
MKRFKKVVVG GTFDRLHLGH KALLRKAFEV GKIVYIGLTS DEMVKEKPYA EKILPYERRL
KDLIEFLEVN NFKGYRIIKI NNAIGFTTEI RSLEAIVVSE ETYKGALIVN RAREEVGLKP
LEIIVIPIIK SKLGCKISSS LIRAGLIDPF GNPMKPRS
