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Database: UniProt
Entry: A0A1J5A3J2_9CHLR
LinkDB: A0A1J5A3J2_9CHLR
Original site: A0A1J5A3J2_9CHLR 
ID   A0A1J5A3J2_9CHLR        Unreviewed;       376 AA.
AC   A0A1J5A3J2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Dephospho-CoA kinase {ECO:0000256|HAMAP-Rule:MF_00376};
DE            EC=2.7.1.24 {ECO:0000256|HAMAP-Rule:MF_00376};
DE   AltName: Full=Dephosphocoenzyme A kinase {ECO:0000256|HAMAP-Rule:MF_00376};
GN   Name=coaE {ECO:0000256|HAMAP-Rule:MF_00376};
GN   ORFNames=AUK03_13830 {ECO:0000313|EMBL:OIO89862.1};
OS   Anaerolineae bacterium CG2_30_64_16.
OC   Bacteria; Chloroflexota; Anaerolineae.
OX   NCBI_TaxID=1805005 {ECO:0000313|EMBL:OIO89862.1, ECO:0000313|Proteomes:UP000182267};
RN   [1] {ECO:0000313|EMBL:OIO89862.1, ECO:0000313|Proteomes:UP000182267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG2_30_64_16 {ECO:0000313|EMBL:OIO89862.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of
CC       dephosphocoenzyme A to form coenzyme A. {ECO:0000256|HAMAP-
CC       Rule:MF_00376}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+);
CC         Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216;
CC         EC=2.7.1.24; Evidence={ECO:0000256|HAMAP-Rule:MF_00376};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 5/5. {ECO:0000256|HAMAP-Rule:MF_00376}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376}.
CC   -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000256|HAMAP-
CC       Rule:MF_00376}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OIO89862.1}.
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DR   EMBL; MNXL01000317; OIO89862.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J5A3J2; -.
DR   UniPathway; UPA00241; UER00356.
DR   Proteomes; UP000182267; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004140; F:dephospho-CoA kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd02022; DPCK; 1.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR001977; Depp_CoAkinase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00152; dephospho-CoA kinase; 1.
DR   PANTHER; PTHR10695:SF46; BIFUNCTIONAL COENZYME A SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR10695; DEPHOSPHO-COA KINASE-RELATED; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF01121; CoaE; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51219; DPCK; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00376}; Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00376};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00376, ECO:0000313|EMBL:OIO89862.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00376}; Transferase {ECO:0000256|HAMAP-Rule:MF_00376}.
FT   DOMAIN          214..372
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   BINDING         25..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ   SEQUENCE   376 AA;  39740 MW;  16B487C2F54C3A2F CRC64;
     MKGHPIQAVQ ERGRPIVIGL TGGIGTGKST VLQNLVALGA EGIDADQVAH QVIAPDGPAY
     AAVVAEFDPA IVGPDGRIDR GALGRCVFAD PAALARLEAI VHPAVGQVIA ARVAASSAPV
     VVIEAIKLLE AGLSRRLCDQ VWVTVCPEAT QIARLAAGRG MTEAEARRRL ANQMPQAQLL
     AQADRVIDTR GALAETAIQV SEAWAALGLP LPVPTIRVAT PDDAEAIAAV WRAVVAEGGQ
     TVVDRPFTPA QERAYLEQLP PRARVTVAVV GDLVAGFQSL DLYATFTGAM DHVGVLGTFV
     LAPWRGRGIG RRLSQATFSY ARQAGFAKFV ITVRADNLDA QAFYATLGFQ PCGRLARQAF
     VDGRYVDELL FEMFLA
//
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