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Database: UniProt
Entry: COAD_HELMI
LinkDB: COAD_HELMI
Original site: COAD_HELMI 
ID   COAD_HELMI              Reviewed;         168 AA.
AC   B0TGU9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 73.
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};
GN   OrderedLocusNames=Helmi_20850; ORFNames=HM1_2154;
OS   Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Heliobacteriaceae;
OC   Heliobacterium.
OX   NCBI_TaxID=498761;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51547 / Ice1;
RX   PubMed=18441057; DOI=10.1128/JB.00299-08;
RA   Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA   Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA   Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L.,
RA   Wang Z.T., Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT   "The genome of Heliobacterium modesticaldum, a phototrophic
RT   representative of the Firmicutes containing the simplest
RT   photosynthetic apparatus.";
RL   J. Bacteriol. 190:4687-4696(2008).
CC   -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC       phosphopantetheine, yielding dephospho-CoA (dPCoA) and
CC       pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00151}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-pantetheine 4'-phosphate + H(+) = 3'-dephospho-
CC         CoA + 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
CC       (R)-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.
CC       {ECO:0000255|HAMAP-Rule:MF_00151}.
DR   EMBL; CP000930; ABZ84710.1; -; Genomic_DNA.
DR   RefSeq; WP_012283210.1; NC_010337.2.
DR   SMR; B0TGU9; -.
DR   STRING; 498761.HM1_2154; -.
DR   PRIDE; B0TGU9; -.
DR   EnsemblBacteria; ABZ84710; ABZ84710; HM1_2154.
DR   KEGG; hmo:HM1_2154; -.
DR   eggNOG; ENOG4108ZEF; Bacteria.
DR   eggNOG; COG0669; LUCA.
DR   HOGENOM; HOG000006518; -.
DR   KO; K00954; -.
DR   OMA; EFQMALM; -.
DR   OrthoDB; 1846503at2; -.
DR   BioCyc; HMOD498761:G1GB0-1965-MONOMER; -.
DR   UniPathway; UPA00241; UER00355.
DR   Proteomes; UP000008550; 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; Complete proteome; Cytoplasm;
KW   Magnesium; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN         1    168       Phosphopantetheine adenylyltransferase.
FT                                /FTId=PRO_1000096799.
FT   NP_BIND       9     10       ATP. {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   NP_BIND      88     90       ATP. {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   NP_BIND     123    129       ATP. {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   BINDING       9      9       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00151}.
FT   BINDING      17     17       ATP. {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   BINDING      41     41       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00151}.
FT   BINDING      73     73       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   BINDING      87     87       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00151}.
FT   BINDING      98     98       ATP. {ECO:0000255|HAMAP-Rule:MF_00151}.
FT   SITE         17     17       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00151}.
SQ   SEQUENCE   168 AA;  18761 MW;  038BFC2E9F0055A5 CRC64;
     MTVAVYPGSF DPITKGHMDI VERAAQIFHE VIVAVVINPN KKPLFTMDER VEMIRMAVSH
     ISNVRVESFS GLLVDFTRKQ GARAIVRGLR AVSDFEVEFQ MALMNKRLYP EVETVFMATH
     TDYAFLSSSM VKEVASFGGD VSDYLPPAVL ARMAEKYGDT VRGKAPVR
//
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