COAD_BACVZ
ID COAD_BACVZ Reviewed; 160 AA.
AC A7Z4C5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151};
DE EC=2.7.7.3 {ECO:0000255|HAMAP-Rule:MF_00151};
DE AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00151};
DE AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151};
DE Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00151};
GN Name=coaD {ECO:0000255|HAMAP-Rule:MF_00151}; OrderedLocusNames=RBAM_014880;
OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS (Bacillus amyloliquefaciens subsp. plantarum).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=326423;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX PubMed=17704766; DOI=10.1038/nbt1325;
RA Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA Strittmatter A., Gottschalk G., Borriss R.;
RT "Comparative analysis of the complete genome sequence of the plant growth-
RT promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL Nat. Biotechnol. 25:1007-1014(2007).
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_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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00151};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00151};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00151}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00151}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00151}.
CC -!- SIMILARITY: Belongs to the bacterial CoaD family. {ECO:0000255|HAMAP-
CC Rule:MF_00151}.
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DR EMBL; CP000560; ABS73851.1; -; Genomic_DNA.
DR RefSeq; WP_007409694.1; NC_009725.2.
DR AlphaFoldDB; A7Z4C5; -.
DR SMR; A7Z4C5; -.
DR STRING; 326423.RBAM_014880; -.
DR EnsemblBacteria; ABS73851; ABS73851; RBAM_014880.
DR KEGG; bay:RBAM_014880; -.
DR HOGENOM; CLU_100149_0_1_9; -.
DR OMA; EFQMALM; -.
DR UniPathway; UPA00241; UER00355.
DR Proteomes; UP000001120; 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; -; 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 PANTHER; PTHR21342:SF1; PTHR21342:SF1; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR PRINTS; PR01020; LPSBIOSNTHSS.
DR TIGRFAMs; TIGR01510; coaD_prev_kdtB; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Magnesium;
KW Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT CHAIN 1..160
FT /note="Phosphopantetheine adenylyltransferase"
FT /id="PRO_1000011091"
FT BINDING 10..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 89..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 124..130
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT SITE 18
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
SQ SEQUENCE 160 AA; 18028 MW; 06A3C829FFE90E0F CRC64;
MASIAVCPGS FDPVTYGHLD IIRRGANVFE QVYVCVLNNS SKQPLFTVEE RCELLREVTK
DIPNVTVETS QGLLIDYAKK KRAKAIIRGL RAVSDFEYEM QGTSVNRVLD ESIETFFMMT
NNQYSFLSSS IVKEVAKYNG PVSEFVPPEV EQALMQKFKG
