COAD_THEMA
ID COAD_THEMA Reviewed; 161 AA.
AC Q9WZK0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
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}; Synonyms=kdtB;
GN OrderedLocusNames=TM_0741;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH PHOSPHOPANTETHEINE,
RP AND SUBUNIT.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of phosphopantetheine adenylyltransferase (TM0741) from
RT Thermotoga maritima at 2.20 A resolution.";
RL Submitted (JUL-2004) to the PDB data bank.
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 ECO:0000269|Ref.2}.
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; AE000512; AAD35822.1; -; Genomic_DNA.
DR PIR; H72339; H72339.
DR RefSeq; NP_228550.1; NC_000853.1.
DR RefSeq; WP_004080981.1; NZ_CP011107.1.
DR PDB; 1VLH; X-ray; 2.20 A; A/B/C/D/E/F=1-161.
DR PDBsum; 1VLH; -.
DR AlphaFoldDB; Q9WZK0; -.
DR SMR; Q9WZK0; -.
DR STRING; 243274.THEMA_00950; -.
DR DrugBank; DB03912; D-pantetheine 4'-phosphate.
DR EnsemblBacteria; AAD35822; AAD35822; TM_0741.
DR KEGG; tma:TM0741; -.
DR eggNOG; COG0669; Bacteria.
DR InParanoid; Q9WZK0; -.
DR OMA; EFQMALM; -.
DR OrthoDB; 1846503at2; -.
DR UniPathway; UPA00241; UER00355.
DR EvolutionaryTrace; Q9WZK0; -.
DR Proteomes; UP000008183; 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..161
FT /note="Phosphopantetheine adenylyltransferase"
FT /id="PRO_0000156296"
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|Ref.2, ECO:0007744|PDB:1VLH"
FT BINDING 16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 36..40
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:1VLH"
FT BINDING 72
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|Ref.2, ECO:0007744|PDB:1VLH"
FT BINDING 86
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|Ref.2, ECO:0007744|PDB:1VLH"
FT BINDING 87..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 122..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00151"
FT BINDING 132
FT /ligand="substrate"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:1VLH"
FT SITE 16
FT /note="Transition state stabilizer"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1VLH"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:1VLH"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:1VLH"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:1VLH"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:1VLH"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1VLH"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:1VLH"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:1VLH"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:1VLH"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:1VLH"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1VLH"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:1VLH"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1VLH"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:1VLH"
SQ SEQUENCE 161 AA; 18249 MW; 4A0F62B9D368496F CRC64;
MKAVYPGSFD PITLGHVDII KRALSIFDEL VVLVTENPRK KCMFTLEERK KLIEEVLSDL
DGVKVDVHHG LLVDYLKKHG IKVLVRGLRA VTDYEYELQM ALANKKLYSD LETVFLIASE
KFSFISSSLV KEVALYGGDV TEWVPPEVAR ALNEKLKEGK R
