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Database: UniProt
Entry: A0A2G2CPY8_9HELI
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ID   A0A2G2CPY8_9HELI        Unreviewed;       169 AA.
AC   A0A2G2CPY8;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   08-MAY-2019, entry version 9.
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=COA39_05730 {ECO:0000313|EMBL:PHR14560.1};
OS   Sulfurimonas sp.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Sulfurimonas.
OX   NCBI_TaxID=2022749 {ECO:0000313|EMBL:PHR14560.1, ECO:0000313|Proteomes:UP000226052};
RN   [1] {ECO:0000313|Proteomes:UP000226052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy
RT   inhabits the cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) 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       ECO:0000256|SAAS:SAAS00395140}.
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, ECO:0000256|SAAS:SAAS01126069};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00151, ECO:0000256|SAAS:SAAS00834013};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC       (R)-pantothenate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00151,
CC       ECO:0000256|SAAS:SAAS00108991}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00151,
CC       ECO:0000256|SAAS:SAAS00109038}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00151,
CC       ECO:0000256|SAAS:SAAS00108990}.
CC   -!- SIMILARITY: Belongs to the bacterial CoaD family.
CC       {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS00580827}.
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:PHR14560.1}.
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DR   EMBL; NVXO01000004; PHR14560.1; -; Genomic_DNA.
DR   UniPathway; UPA00241; UER00355.
DR   Proteomes; UP000226052; 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; -; 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 {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00109018};
KW   Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00109017};
KW   Complete proteome {ECO:0000313|Proteomes:UP000226052};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00109028};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00834014};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00109023};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00109019, ECO:0000313|EMBL:PHR14560.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00108989, ECO:0000313|EMBL:PHR14560.1}.
FT   DOMAIN       12    140       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
FT   NP_BIND      16     17       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   NP_BIND      95     97       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   NP_BIND     130    136       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   BINDING      16     16       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00151}.
FT   BINDING      24     24       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   BINDING      48     48       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00151}.
FT   BINDING      80     80       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   BINDING      94     94       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00151}.
FT   BINDING     105    105       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   SITE         24     24       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00151}.
SQ   SEQUENCE   169 AA;  18805 MW;  CA4B3907BE8432C1 CRC64;
     MEIEMNSKKT ALYPGTFDPV TNGHIDIIQR ASKLFDELVV AVAASVDKKP MFSLTERIEM
     TKAAVIDLKN VRVVGFDNLT IDLAHEYEAG VLIRGLRAVS DFEYELQLGY LNNSLDTSIE
     TVYLMPTLQN AFISSSIVRN LLKFNGKTEH IIPAPVQKII GNMTTCTSH
//
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