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Database: UniProt
Entry: A0A1H9A1W1_9EURY
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ID   A0A1H9A1W1_9EURY        Unreviewed;       155 AA.
AC   A0A1H9A1W1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00647};
DE            EC=2.7.7.3 {ECO:0000256|HAMAP-Rule:MF_00647};
DE   AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00647};
DE   AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00647};
DE            Short=PPAT {ECO:0000256|HAMAP-Rule:MF_00647};
GN   Name=coaD {ECO:0000256|HAMAP-Rule:MF_00647};
GN   ORFNames=SAMN04489841_0327 {ECO:0000313|EMBL:SEP70649.1};
OS   Natrinema salaciae.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=1186196 {ECO:0000313|EMBL:SEP70649.1, ECO:0000313|Proteomes:UP000199114};
RN   [1] {ECO:0000313|Proteomes:UP000199114}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25055 {ECO:0000313|Proteomes:UP000199114};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC       phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
CC       {ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_00647};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00647}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00647}.
CC   -!- SIMILARITY: Belongs to the eukaryotic CoaD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00647}.
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DR   EMBL; FOFD01000001; SEP70649.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9A1W1; -.
DR   STRING; 1186196.SAMN04489841_0327; -.
DR   OrthoDB; 53228at2157; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000199114; Unassembled WGS sequence.
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; HUPs; 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   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00647};
KW   Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00647};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00647};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00647};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00647,
KW   ECO:0000313|EMBL:SEP70649.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00647}.
FT   DOMAIN          5..142
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
SQ   SEQUENCE   155 AA;  17202 MW;  39C28A17F87A2A86 CRC64;
     MDVALGGTFD PVHDGHRRLF ERAFELGDVT VGLTSDELAP KTRDVDRRVR SYDERKADLE
     TELESIAADH GRAFEIRILE APTGIATEPQ YDYLVVSPET REGGDRINEI RTERGHDPLE
     VVVVPHVLAD DGDIISSTRI VKGEIDEHGT VLDGD
//
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