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Database: UniProt
Entry: A0A0D6AM68_9CHRO
LinkDB: A0A0D6AM68_9CHRO
Original site: A0A0D6AM68_9CHRO 
ID   A0A0D6AM68_9CHRO        Unreviewed;       159 AA.
AC   A0A0D6AM68;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=GM3709_520 {ECO:0000313|EMBL:BAQ63755.1};
OS   Geminocystis sp. NIES-3709.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Geminocystaceae; Geminocystis.
OX   NCBI_TaxID=1617448 {ECO:0000313|EMBL:BAQ63755.1, ECO:0000313|Proteomes:UP000064126};
RN   [1] {ECO:0000313|EMBL:BAQ63755.1, ECO:0000313|Proteomes:UP000064126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3709 {ECO:0000313|EMBL:BAQ63755.1,
RC   ECO:0000313|Proteomes:UP000064126};
RA   Hirose Y.;
RT   "Geminocystis sp. NIES-3709 complete genome sequence.";
RL   Submitted (MAR-2015) 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}.
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DR   EMBL; AP014821; BAQ63755.1; -; Genomic_DNA.
DR   RefSeq; WP_066115971.1; NZ_AP014821.1.
DR   AlphaFoldDB; A0A0D6AM68; -.
DR   STRING; 1617448.GM3709_520; -.
DR   KEGG; gen:GM3709_520; -.
DR   PATRIC; fig|1617448.3.peg.531; -.
DR   OrthoDB; 9806661at2; -.
DR   UniPathway; UPA00241; UER00355.
DR   Proteomes; UP000064126; 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; 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};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000313|EMBL:BAQ63755.1}.
FT   DOMAIN          4..132
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
FT   BINDING         8..9
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         8
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         87..89
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   BINDING         122..128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
FT   SITE            16
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00151"
SQ   SEQUENCE   159 AA;  17846 MW;  28BEFDC8AB053D40 CRC64;
     MIAIYPGSFD PITLGHLDLI QRSSILFEKV IVAVLKNPNK TPFFTIEKRV QQIQECTANI
     KNIEVDSFSG LTVEYAQKKQ AGVLLRGLRV MSDFEQELQM AHINKTLENK IETVFLATNT
     ELSFISSSVV KEIAKFGGSI DHLVTSNIAQ DLYSNIRNK
//
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