ID A0A0H4QYA7_9LACO Unreviewed; 169 AA.
AC A0A0H4QYA7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00151};
DE EC=2.7.7.3 {ECO:0000256|HAMAP-Rule:MF_00151};
DE AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00151};
DE AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00151};
DE Short=PPAT {ECO:0000256|HAMAP-Rule:MF_00151};
GN Name=coaD {ECO:0000256|HAMAP-Rule:MF_00151,
GN ECO:0000313|EMBL:AKP66445.1};
GN ORFNames=ABM34_02015 {ECO:0000313|EMBL:AKP66445.1};
OS Companilactobacillus ginsenosidimutans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Companilactobacillus.
OX NCBI_TaxID=1007676 {ECO:0000313|EMBL:AKP66445.1, ECO:0000313|Proteomes:UP000036106};
RN [1] {ECO:0000313|Proteomes:UP000036106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EMML 3041 {ECO:0000313|Proteomes:UP000036106};
RA Kim M.K., Im W.-T., Srinivasan S., Lee J.-J.;
RT "Lactobacillus ginsenosidimutans/EMML 3141/ whole genome sequencing.";
RL Submitted (JUL-2015) 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_00151}.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00029346, ECO:0000256|HAMAP-
CC Rule:MF_00151};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00151};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00151}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00151}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00151}.
CC -!- SIMILARITY: Belongs to the bacterial CoaD family. {ECO:0000256|HAMAP-
CC Rule:MF_00151}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00151}.
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DR EMBL; CP012034; AKP66445.1; -; Genomic_DNA.
DR RefSeq; WP_048702813.1; NZ_CP012034.1.
DR AlphaFoldDB; A0A0H4QYA7; -.
DR STRING; 1007676.ABM34_02015; -.
DR KEGG; lgn:ABM34_02015; -.
DR PATRIC; fig|1007676.4.peg.420; -.
DR OrthoDB; 9806661at2; -.
DR UniPathway; UPA00241; UER00355.
DR Proteomes; UP000036106; 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 CDD; cd02163; PPAT; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00151; PPAT_bact; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR001980; PPAT.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR01510; coaD_prev_kdtB; 1.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR PANTHER; PTHR21342; PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE; 1.
DR PANTHER; PTHR21342:SF1; PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR PRINTS; PR01020; LPSBIOSNTHSS.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00151};
KW Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993, ECO:0000256|HAMAP-
KW Rule:MF_00151};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00151};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00151};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00151};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00151};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000313|EMBL:AKP66445.1}.
FT DOMAIN 7..136
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
FT BINDING 11..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT BINDING 19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT BINDING 126..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT SITE 19
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
SQ SEQUENCE 169 AA; 19083 MW; 23872354FFFBBE2F CRC64;
MSEKIGLYAG SFDPITNGHV DIIRRASKLF DKLIVAPMTN TSKKYLFTYD EKKTFIEEEI
KDLPNVKVVN GKDELTIKLA KRYGATFLVR SMRNADDFGY ESGVSSINKA LDDDIETIFL
ISDTKYSTIS SSMIKEVAKF NGDITKFVPK HVATELTKRL QKGNRSLEI
//
