GenomeNet

Database: UniProt
Entry: A0A291JQU2_9GAMM
LinkDB: A0A291JQU2_9GAMM
Original site: A0A291JQU2_9GAMM 
ID   A0A291JQU2_9GAMM        Unreviewed;       164 AA.
AC   A0A291JQU2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   08-MAY-2019, entry version 7.
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=CLM76_02675 {ECO:0000313|EMBL:ATH76581.1};
OS   Halomonas hydrothermalis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=115561 {ECO:0000313|EMBL:ATH76581.1, ECO:0000313|Proteomes:UP000217920};
RN   [1] {ECO:0000313|EMBL:ATH76581.1, ECO:0000313|Proteomes:UP000217920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y2 {ECO:0000313|EMBL:ATH76581.1,
RC   ECO:0000313|Proteomes:UP000217920};
RX   PubMed=27315164; DOI=10.1007/s00792-016-0852-8;
RA   Cui Y., Cheng B., Meng Y., Li C., Yin H., Xu P., Yang C.;
RT   "Expression and functional analysis of two NhaD type antiporters from
RT   the halotolerant and alkaliphilic Halomonas sp. Y2.";
RL   Extremophiles 20:631-639(2016).
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP023656; ATH76581.1; -; Genomic_DNA.
DR   RefSeq; WP_039182878.1; NZ_JTDR01000018.1.
DR   KEGG; hhh:CLM76_02675; -.
DR   KO; K00954; -.
DR   UniPathway; UPA00241; UER00355.
DR   Proteomes; UP000217920; 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; -; 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:UP000217920};
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:ATH76581.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00108989, ECO:0000313|EMBL:ATH76581.1}.
FT   DOMAIN       10    138       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
FT   NP_BIND      14     15       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      14     14       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00151}.
FT   BINDING      22     22       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   BINDING      46     46       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         22     22       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00151}.
SQ   SEQUENCE   164 AA;  17863 MW;  340CF7F985B2F994 CRC64;
     MSAPRRNIAV YPGTFDPITN GHFDLIERGA RMFDQVVIAV AASPGKRPAL ELPTRIALAQ
     QVCASLENVS VIGFSSLLTT MMHEQGATII LRGLRAVSDF EYELQLANMN RAQNPELESV
     FLTPAVENSY ISSTIVREIA KLGGDISALV HPQVAEALRK HYTG
//
DBGET integrated database retrieval system