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Database: UniProt
Entry: A0A1E4ANV5_9FLAO
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ID   A0A1E4ANV5_9FLAO        Unreviewed;       153 AA.
AC   A0A1E4ANV5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   08-MAY-2019, entry version 12.
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=ABS44_04810 {ECO:0000313|EMBL:ODS89536.1};
OS   Chryseobacterium sp. SCN 40-13.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Chryseobacterium.
OX   NCBI_TaxID=1660093 {ECO:0000313|EMBL:ODS89536.1, ECO:0000313|Proteomes:UP000094247};
RN   [1] {ECO:0000313|EMBL:ODS89536.1, ECO:0000313|Proteomes:UP000094247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA   Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA   Banfield J.F.;
RT   "Bioreactor microbial ecosystems for thiocyanate and cyanide
RT   degradation unravelled with genome-resolved metagenomics.";
RL   Environ. Microbiol. 17:4929-4941(2015).
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:ODS89536.1}.
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DR   EMBL; MEDR01000027; ODS89536.1; -; Genomic_DNA.
DR   UniPathway; UPA00241; UER00355.
DR   Proteomes; UP000094247; 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:UP000094247};
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:ODS89536.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00151,
KW   ECO:0000256|SAAS:SAAS00108989, ECO:0000313|EMBL:ODS89536.1}.
FT   DOMAIN        5    135       CTP_transf_like. {ECO:0000259|Pfam:
FT                                PF01467}.
FT   NP_BIND       9     10       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   NP_BIND      88     90       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   NP_BIND     125    131       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      73     73       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   BINDING      87     87       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00151}.
FT   BINDING      98     98       ATP. {ECO:0000256|HAMAP-Rule:MF_00151}.
FT   SITE         17     17       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00151}.
SQ   SEQUENCE   153 AA;  17541 MW;  654ED5487EFC8169 CRC64;
     MRIAVFPGSF DPITLGHYDI VERAAPLFDK IIIAIGQNSQ KKYMFSLEQR KEFIQKTFKD
     FPNVEVDSFE GLTIDYCQSK KVNFILRGLR NPADFEFEKA IAQTNRTLTH DNKIETIFLL
     TSAGKSFISS SIVREIISFK GHYELLVPDS VRV
//
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