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Database: UniProt
Entry: X7EMV8_9RHOB
LinkDB: X7EMV8_9RHOB
Original site: X7EMV8_9RHOB 
ID   X7EMV8_9RHOB            Unreviewed;       166 AA.
AC   X7EMV8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   08-MAY-2019, entry version 29.
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=OCH239_01170 {ECO:0000313|EMBL:ETX16478.1};
OS   Roseivivax halodurans JCM 10272.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Roseivivax.
OX   NCBI_TaxID=1449350 {ECO:0000313|EMBL:ETX16478.1, ECO:0000313|Proteomes:UP000022447};
RN   [1] {ECO:0000313|EMBL:ETX16478.1, ECO:0000313|Proteomes:UP000022447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10272 {ECO:0000313|EMBL:ETX16478.1,
RC   ECO:0000313|Proteomes:UP000022447};
RA   Lai Q., Li G., Shao Z.;
RT   "Roseivivax halodurans JCM 10272 Genome Sequencing.";
RL   Submitted (JAN-2014) 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:ETX16478.1}.
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DR   EMBL; JALZ01000001; ETX16478.1; -; Genomic_DNA.
DR   RefSeq; WP_037257443.1; NZ_JALZ01000001.1.
DR   STRING; 1449350.OCH239_01170; -.
DR   EnsemblBacteria; ETX16478; ETX16478; OCH239_01170.
DR   PATRIC; fig|1449350.3.peg.237; -.
DR   OrthoDB; 1846503at2; -.
DR   UniPathway; UPA00241; UER00355.
DR   Proteomes; UP000022447; 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:UP000022447};
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:ETX16478.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000022447};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00108989, ECO:0000313|EMBL:ETX16478.1}.
FT   DOMAIN        5    138       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
FT   NP_BIND       9     10       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   NP_BIND      93     95       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   NP_BIND     128    134       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   BINDING       9      9       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00151}.
FT   BINDING      17     17       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   BINDING      41     41       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00151}.
FT   BINDING      78     78       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   BINDING      92     92       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00151}.
FT   BINDING     103    103       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   SITE         17     17       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00151}.
SQ   SEQUENCE   166 AA;  18152 MW;  608CFD3D4A3E3965 CRC64;
     MPTGLYPGTF DPITLGHIDI IRRATVMVDR LVIGVAINGD KGPLFDLGTR VSMIEAECAK
     LQSETGTEIV VHPFENLLID CARDVGAQVI IRGLRAVADF EYEFQMVGMN RALDQSIETV
     FLMAEARHQA IASKLVKEIA RLGGDVSKFV TPPVRDALQA RFASQP
//
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