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Database: UniProt
Entry: A0A0P4R1A2_9ACTN
LinkDB: A0A0P4R1A2_9ACTN
Original site: A0A0P4R1A2_9ACTN 
ID   A0A0P4R1A2_9ACTN        Unreviewed;       170 AA.
AC   A0A0P4R1A2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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   ECO:0000313|EMBL:GAO06630.1};
GN   ORFNames=TPA0598_01_10010 {ECO:0000313|EMBL:GAO06630.1};
OS   Streptomyces lydicamycinicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1546107 {ECO:0000313|EMBL:GAO06630.1, ECO:0000313|Proteomes:UP000048965};
RN   [1] {ECO:0000313|Proteomes:UP000048965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110027 {ECO:0000313|Proteomes:UP000048965};
RA   Komaki H., Ichikawa N., Katano-Makiyama Y., Hosoyama A., Hashimoto M.,
RA   Uohara A., Kitahashi Y., Ohji S., Kimura A., Yamazoe A., Igarashi Y.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Streptomyces sp. NBRC 110027.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAO06630.1, ECO:0000313|Proteomes:UP000048965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110027 {ECO:0000313|EMBL:GAO06630.1,
RC   ECO:0000313|Proteomes:UP000048965};
RX   PubMed=26380643; DOI=10.1186/s40793-015-0046-5;
RA   Komaki H., Ichikawa N., Hosoyama A., Fujita N., Igarashi Y.;
RT   "Draft genome sequence of marine-derived Streptomyces sp. TP-A0598, a
RT   producer of anti-MRSA antibiotic lydicamycins.";
RL   Stand. Genomic Sci. 10:58-58(2015).
CC   -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'-
CC       phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
CC       {ECO:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00029346, ECO:0000256|HAMAP-
CC         Rule:MF_00151};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00151};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       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. {ECO:0000256|HAMAP-
CC       Rule:MF_00151}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAO06630.1}.
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DR   EMBL; BBNO01000001; GAO06630.1; -; Genomic_DNA.
DR   RefSeq; WP_042149286.1; NZ_CP098437.1.
DR   AlphaFoldDB; A0A0P4R1A2; -.
DR   OrthoDB; 9806661at2; -.
DR   UniPathway; UPA00241; UER00355.
DR   Proteomes; UP000048965; 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   CDD; cd02163; PPAT; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR01510; coaD_prev_kdtB; 1.
DR   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   PANTHER; PTHR21342; PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR21342:SF1; PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   PRINTS; PR01020; LPSBIOSNTHSS.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00151};
KW   Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993, ECO:0000256|HAMAP-
KW   Rule:MF_00151};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00151};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00151};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00151};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00151}; Reference proteome {ECO:0000313|Proteomes:UP000048965};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000313|EMBL:GAO06630.1}.
FT   DOMAIN          15..142
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   BINDING         19..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         98..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         132..138
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   SITE            27
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
SQ   SEQUENCE   170 AA;  18784 MW;  1CF691849B88F309 CRC64;
     MTGSESEETE LRRAVCPGSF DPITNGHLDI IARASKLYDV VHVAVMINQS KQGLFTVDER
     IDLIRRATAE YGNVEVEAFH GLLVDFCKQR DIPAIVKGLR AVSDFDYELQ MAQMNNGLSG
     VETLFVPTNP TYSFLSSSLV KEVAAWGGDV SHLVPPFVLE ALTERLRKKG
//
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