ID A0A3P3RK89_9EURY Unreviewed; 163 AA.
AC A0A3P3RK89;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=EIK79_01235 {ECO:0000313|EMBL:RRJ33832.1};
OS Halomarina oriensis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halomarina.
OX NCBI_TaxID=671145 {ECO:0000313|EMBL:RRJ33832.1, ECO:0000313|Proteomes:UP000282322};
RN [1] {ECO:0000313|EMBL:RRJ33832.1, ECO:0000313|Proteomes:UP000282322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP-AMP-1 {ECO:0000313|EMBL:RRJ33832.1,
RC ECO:0000313|Proteomes:UP000282322};
RA Pal Y., Srinivasana K., Verma A., Kumar P.;
RT "Taxonoimc description of Halomarina strain SPP-AMP-1.";
RL Submitted (NOV-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RRJ33832.1}.
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DR EMBL; RRCH01000003; RRJ33832.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P3RK89; -.
DR OrthoDB; 53228at2157; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000282322; 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:RRJ33832.1};
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"
FT REGION 142..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 163 AA; 18545 MW; 49125CD17C2DE2A3 CRC64;
MQVALGGTFD PVHDGHRELF DRAFQLGDVT VGLTSDELAP QTRNEQRHIR PFEERKRDLK
RELERIADRR GGQFEIRRLN EPTGIATDPG FEYLIVSPET RPTGKTINRI RTDRGLDPLE
IVVIDHLAAE DGDRISSTRI VKGEIDEHGT LTPERQGRPT SER
//
