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Database: UniProt
Entry: E5Y609_BILWA
LinkDB: E5Y609_BILWA
Original site: E5Y609_BILWA 
ID   E5Y609_BILWA            Unreviewed;       168 AA.
AC   E5Y609;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 2.
DT   16-JAN-2019, entry version 41.
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   ORFNames=HMPREF0179_01622 {ECO:0000313|EMBL:EFV44556.2};
OS   Bilophila wadsworthia 3_1_6.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Bilophila.
OX   NCBI_TaxID=563192 {ECO:0000313|EMBL:EFV44556.2, ECO:0000313|Proteomes:UP000006034};
RN   [1] {ECO:0000313|EMBL:EFV44556.2, ECO:0000313|Proteomes:UP000006034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_6 {ECO:0000313|EMBL:EFV44556.2,
RC   ECO:0000313|Proteomes:UP000006034};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA   Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   White J., Yandava C., Allen-Vercoe E., Sibley C., Ambrose C.E.,
RA   Strauss J., Daigneault M., Haas B., Nusbaum C., Birren B.;
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFV44556.2, ECO:0000313|Proteomes:UP000006034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_6 {ECO:0000313|EMBL:EFV44556.2,
RC   ECO:0000313|Proteomes:UP000006034};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Sibley C., Strauss J.,
RA   Allen-Vercoe E., Walker B., Young S., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bilophila wadsworthia 3_1_6.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC       phosphopantetheine, yielding dephospho-CoA (dPCoA) and
CC       pyrophosphate. {ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_00151};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00151};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC       (R)-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.
CC       {ECO:0000256|HAMAP-Rule:MF_00151}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00151}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EFV44556.2}.
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DR   EMBL; ADCP02000003; EFV44556.2; -; Genomic_DNA.
DR   STRING; 563192.HMPREF0179_01622; -.
DR   EnsemblBacteria; EFV44556; EFV44556; HMPREF0179_01622.
DR   eggNOG; ENOG4108ZEF; Bacteria.
DR   eggNOG; COG0669; LUCA.
DR   UniPathway; UPA00241; UER00355.
DR   Proteomes; UP000006034; Unassembled WGS sequence.
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; -; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00151};
KW   Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00151};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00151};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00151};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00151};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000313|EMBL:EFV44556.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006034};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000313|EMBL:EFV44556.2}.
FT   DOMAIN        2    107       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
FT   NP_BIND      62     64       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   NP_BIND      97    103       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   BINDING      15     15       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00151}.
FT   BINDING      47     47       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   BINDING      61     61       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00151}.
FT   BINDING      72     72       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
SQ   SEQUENCE   168 AA;  18963 MW;  F4EFAB4A16B68460 CRC64;
     MFDNIIVAVA ADTGKSPLFS LEERVAMAEK VFAKEPNISV EPFQGLLVEY VARRNVHTVL
     RGLRAVSDFE YEFQIALMNR KLRPDIETLF LISDYRWLYI SSTIVKTVAS LGGDVRGLVP
     DHVLSCLRER FGFTHGEIEP VSLPPVPELS ELARLQELEA SLDRDTDK
//
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