ID A0A3A9ETK2_9FIRM Unreviewed; 531 AA.
AC A0A3A9ETK2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=D7X94_03275 {ECO:0000313|EMBL:RKJ41324.1};
OS Acutalibacter sp. 1XD8-33.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acutalibacter.
OX NCBI_TaxID=2320081 {ECO:0000313|EMBL:RKJ41324.1, ECO:0000313|Proteomes:UP000270929};
RN [1] {ECO:0000313|EMBL:RKJ41324.1, ECO:0000313|Proteomes:UP000270929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1XD8-33 {ECO:0000313|EMBL:RKJ41324.1,
RC ECO:0000313|Proteomes:UP000270929};
RA Liu C.;
RT "Murine metabolic-syndrome-specific gut microbial biobank.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-
CC threonylcarbamoyladenylate; Xref=Rhea:RHEA:36407, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57926, ChEBI:CHEBI:73682; EC=2.7.7.87;
CC Evidence={ECO:0000256|ARBA:ARBA00001803};
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|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00376}.
CC -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000256|HAMAP-
CC Rule:MF_00376}.
CC -!- SIMILARITY: Belongs to the SUA5 family.
CC {ECO:0000256|ARBA:ARBA00007663}.
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:RKJ41324.1}.
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DR EMBL; RAZF01000003; RKJ41324.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9ETK2; -.
DR OrthoDB; 9814580at2; -.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000270929; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0061710; F:L-threonylcarbamoyladenylate synthase; IEA:RHEA.
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 Gene3D; 3.90.870.10; DHBP synthase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.11030; Threonylcarbamoyl-AMP synthase, C-terminal domain; 1.
DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR InterPro; IPR001977; Depp_CoAkinase.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006070; Sua5-like_dom.
DR InterPro; IPR038385; Sua5/YwlC_C.
DR InterPro; IPR005145; Sua5_C.
DR NCBIfam; TIGR00152; dephospho-CoA kinase; 1.
DR NCBIfam; TIGR00057; L-threonylcarbamoyladenylate synthase; 1.
DR PANTHER; PTHR17490; SUA5; 1.
DR PANTHER; PTHR17490:SF16; THREONYLCARBAMOYL-AMP SYNTHASE; 1.
DR Pfam; PF01121; CoaE; 1.
DR Pfam; PF03481; Sua5_C; 1.
DR Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF55821; YrdC/RibB; 1.
DR PROSITE; PS51219; DPCK; 1.
DR PROSITE; PS51163; YRDC; 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|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00376};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00376};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00376}; Reference proteome {ECO:0000313|Proteomes:UP000270929};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00376}.
FT DOMAIN 10..197
FT /note="YrdC-like"
FT /evidence="ECO:0000259|PROSITE:PS51163"
FT BINDING 352..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ SEQUENCE 531 AA; 56848 MW; B5C7C4C5FBF20E59 CRC64;
MNTEIIPPSS QGAARAGEIL RAGGLVAIPT ETVYGLAANA LDPAAVKKIY EAKGRPSDNP
LIVHISSVEQ WPELVRGKIP ENARKLAEAF WPGPLTVILE KSGIIPSVTS GGLDTVAVRC
PAHPLARAVI EAAGVPLAAP SANLSGRPSP TTFSHTLEDL QGRVDAVMDG GDCGVGVEST
VISLAGGRVR LLRPGGVTKE ALEQVAGPVE LDPAVTAMLA PGERAASPGM KYKHYAPRAE
VVILDGSPEA FAQYVNAQGP GADVLCFSET EPLLAVPALC LGSRYDGAEQ ARRLFWALHR
LDQIGARRVL AQRPNRRGIG LAVYNRLLRA AAFRIEKLPG PPWIVGLVGP SGAGKSTVAK
EMGRLGFSLV DCDRLTRSAE VYNQECLAAL GRAFGEEVIP GGVLDRRELA RRAFRDEASK
KLLEEITFPT IERAVRRALE QMEGPVLLDA PTLFESGLDV LCARILTVTA PEDLRLRRVM
ARDGLTEEQA RQRFRAQKPA EFYEARGDFV IEGTGDNSGR LEEAAQELKG R
//
