ID G0AME1_BORBD Unreviewed; 163 AA.
AC G0AME1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
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:AEL18867.1};
GN OrderedLocusNames=BbiDN127_0712 {ECO:0000313|EMBL:AEL18867.1};
OS Borrelia bissettiae (strain DSM 17990 / CIP 109136 / DN127) (Borreliella
OS bissettiae).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=521010 {ECO:0000313|EMBL:AEL18867.1, ECO:0000313|Proteomes:UP000001634};
RN [1] {ECO:0000313|Proteomes:UP000001634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17990 / CIP 109136 / DN127
RC {ECO:0000313|Proteomes:UP000001634};
RA Mongodin E.F., Casjens S.R., Fraser-Liggett C.M., Qiu W.-G., Dunn J.J.,
RA Luft B.J., Schutzer S.E.;
RT "Complete genome sequence of Borrelia bissettii strain DN127.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DN127;
RA Mongodin E.F., Casjens S.R., Fraser-Liggett C.M., Qiu W.-G., Dunn J.J.,
RA Luft B.J., Schutzer S.E.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AEL18867.1, ECO:0000313|Proteomes:UP000001634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17990 / CIP 109136 / DN127
RC {ECO:0000313|Proteomes:UP000001634};
RX PubMed=22207749; DOI=10.1128/JB.06263-11;
RA Schutzer S.E., Fraser-Liggett C.M., Qiu W.G., Kraiczy P., Mongodin E.F.,
RA Dunn J.J., Luft B.J., Casjens S.R.;
RT "Whole-Genome Sequences of Borrelia bissettii, Borrelia valaisiana, and
RT Borrelia spielmanii.";
RL J. Bacteriol. 194:545-546(2012).
RN [4] {ECO:0000313|EMBL:AEL18867.1, ECO:0000313|Proteomes:UP000001634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17990 / CIP 109136 / DN127
RC {ECO:0000313|Proteomes:UP000001634};
RX PubMed=26813420; DOI=10.1099/ijsem.0.000897;
RA Margos G., Lane R.S., Fedorova N., Koloczek J., Piesman J., Hojgaard A.,
RA Sing A., Fingerle V.;
RT "Borrelia bissettiae sp. nov. and Borrelia californiensis sp. nov. prevail
RT in diverse enzootic transmission cycles.";
RL Int. J. Syst. Evol. Microbiol. 66:1447-1452(2016).
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}.
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DR EMBL; CP002746; AEL18867.1; -; Genomic_DNA.
DR RefSeq; WP_014023913.1; NC_015921.1.
DR AlphaFoldDB; G0AME1; -.
DR STRING; 521010.BbiDN127_0712; -.
DR KEGG; bbs:BbiDN127_0712; -.
DR eggNOG; COG0669; Bacteria.
DR HOGENOM; CLU_100149_1_1_12; -.
DR UniPathway; UPA00241; UER00355.
DR Proteomes; UP000001634; 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; 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:AEL18867.1}.
FT DOMAIN 5..121
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
FT BINDING 9..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT BINDING 17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT BINDING 90..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT BINDING 125..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT SITE 17
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
SQ SEQUENCE 163 AA; 18883 MW; 1AB87DD607AC7A96 CRC64;
MKVAVFPGSF DPITWGHIDL IKRSLAIFDK VVVLVAKNKS KKYLLSDVER FSLTKEVVAS
LNFSNVLVDR YSGFIVDYAL INSIKFIVRG IRAFNDFDIE FERYLVNNKL NFKIDTIFLP
SSAEHLYVRS DFVKELMSKK DVDLSNFVPE LVFNRLKSKF IDK
//
