COAD_THET8
ID COAD_THET8 Reviewed; 160 AA.
AC Q5SJS9; Q7SIA7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000303|PubMed:14684898};
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, ECO:0000303|PubMed:14684898};
GN Name=coaD {ECO:0000255|HAMAP-Rule:MF_00151}; OrderedLocusNames=TTHA0929;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH
RP 4'-PHOSPHOPANTETHEINE, AND SUBUNIT.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=14684898; DOI=10.1107/s0907444903025319;
RA Takahashi H., Inagaki E., Fujimoto Y., Kuroishi C., Nodake Y., Nakamura Y.,
RA Arisaka F., Yutani K., Kuramitsu S., Yokoyama S., Yamamoto M., Miyano M.,
RA Tahirov T.H.;
RT "Structure and implications for the thermal stability of phosphopantetheine
RT adenylyltransferase from Thermus thermophilus.";
RL Acta Crystallogr. D 60:97-104(2004).
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. All subunits in the hexamer bind substrate. Is in
CC equilibrium between two trimers and a hexamer, and the trimer may be a
CC physiologically important form in T.thermophilus. {ECO:0000255|HAMAP-
CC Rule:MF_00151, ECO:0000269|PubMed:14684898}.
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; AP008226; BAD70752.1; -; Genomic_DNA.
DR RefSeq; WP_011173005.1; NC_006461.1.
DR RefSeq; YP_144195.1; NC_006461.1.
DR PDB; 1OD6; X-ray; 1.50 A; A=1-160.
DR PDBsum; 1OD6; -.
DR AlphaFoldDB; Q5SJS9; -.
DR SMR; Q5SJS9; -.
DR STRING; 300852.55772311; -.
DR EnsemblBacteria; BAD70752; BAD70752; BAD70752.
DR GeneID; 3169134; -.
DR KEGG; ttj:TTHA0929; -.
DR PATRIC; fig|300852.9.peg.912; -.
DR eggNOG; COG0669; Bacteria.
DR HOGENOM; CLU_100149_0_1_0; -.
DR OMA; EFQMALM; -.
DR PhylomeDB; Q5SJS9; -.
DR UniPathway; UPA00241; UER00355.
DR EvolutionaryTrace; Q5SJS9; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Magnesium;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..160
FT /note="Phosphopantetheine adenylyltransferase"
FT /id="PRO_1000011271"
FT BINDING 8..9
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 8
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000269|PubMed:14684898, ECO:0007744|PDB:1OD6"
FT BINDING 16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 40
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 74
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151,
FT ECO:0000269|PubMed:14684898, ECO:0007744|PDB:1OD6"
FT BINDING 88
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
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 BINDING 134
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000269|PubMed:14684898,
FT ECO:0007744|PDB:1OD6"
FT SITE 16
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1OD6"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:1OD6"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:1OD6"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:1OD6"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1OD6"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:1OD6"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:1OD6"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1OD6"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:1OD6"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:1OD6"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1OD6"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1OD6"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:1OD6"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1OD6"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:1OD6"
SQ SEQUENCE 160 AA; 17707 MW; 4F680109F29D894E CRC64;
MHVVYPGSFD PLTNGHLDVI QRASRLFEKV TVAVLENPSK RGQYLFSAEE RLAIIREATA
HLANVEAATF SGLLVDFVRR VGAQAIVKGL RAVSDYEYEL QMAHLNRQLY PGLETLFILA
ATRYSFVSST MVKEIARYGG DVSKLVPPAT LRALKAKLGQ
