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Database: UniProt
Entry: A0A1B6BGF3_9FIRM
LinkDB: A0A1B6BGF3_9FIRM
Original site: A0A1B6BGF3_9FIRM 
ID   A0A1B6BGF3_9FIRM        Unreviewed;       159 AA.
AC   A0A1B6BGF3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=F3D3_3391 {ECO:0000313|EMBL:GAU78756.1};
OS   Fusibacter sp. 3D3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XII. Incertae Sedis; Fusibacter.
OX   NCBI_TaxID=1048380 {ECO:0000313|EMBL:GAU78756.1, ECO:0000313|Proteomes:UP000095197};
RN   [1] {ECO:0000313|EMBL:GAU78756.1, ECO:0000313|Proteomes:UP000095197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D3 {ECO:0000313|EMBL:GAU78756.1,
RC   ECO:0000313|Proteomes:UP000095197};
RA   Serrano A.E., Escudero L.V., Encalada O., Tebes C.J., Fernandez S.,
RA   Demergasso C.S.;
RT   "Draft genome sequence of Fusibacter ascotence 3D3 isolated from the high
RT   arsenic level Ascotan salt flat in northern Chile.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:GAU78756.1}.
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DR   EMBL; BDHH01000015; GAU78756.1; -; Genomic_DNA.
DR   RefSeq; WP_069875543.1; NZ_BDHH01000015.1.
DR   AlphaFoldDB; A0A1B6BGF3; -.
DR   STRING; 1048380.F3D3_3391; -.
DR   OrthoDB; 9806661at2; -.
DR   UniPathway; UPA00241; UER00355.
DR   Proteomes; UP000095197; 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:UP000095197};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000313|EMBL:GAU78756.1}.
FT   DOMAIN          5..133
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   BINDING         9..10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         88..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         123..129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   SITE            17
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
SQ   SEQUENCE   159 AA;  17855 MW;  73B01C2C60638DF8 CRC64;
     MKIAVYPGSF DPVTKGHLDI IERASKLFDH VIVTVMFNQS KAPMFSPDER IALLEKTTSH
     LSNVSVDKHM GLLIDYLKLK EARILVKGLR AISDFEAEFQ MASVNQKLCK EIETVFIMTR
     TDYMYLSSSI VKEVASFGGD ISDFVTEEVK NAIFKKIGG
//
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