COAE_AQUAE
ID COAE_AQUAE Reviewed; 196 AA.
AC O67792;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Dephospho-CoA kinase {ECO:0000255|HAMAP-Rule:MF_00376};
DE EC=2.7.1.24 {ECO:0000255|HAMAP-Rule:MF_00376};
DE AltName: Full=Dephosphocoenzyme A kinase {ECO:0000255|HAMAP-Rule:MF_00376};
GN Name=coaE {ECO:0000255|HAMAP-Rule:MF_00376}; OrderedLocusNames=aq_1985;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of
CC dephosphocoenzyme A to form coenzyme A. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00376};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 5/5. {ECO:0000255|HAMAP-Rule:MF_00376}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00376}.
CC -!- SIMILARITY: Belongs to the CoaE family. {ECO:0000255|HAMAP-
CC Rule:MF_00376, ECO:0000305}.
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DR EMBL; AE000657; AAC07761.1; -; Genomic_DNA.
DR PIR; D70470; D70470.
DR RefSeq; NP_214361.1; NC_000918.1.
DR RefSeq; WP_010881297.1; NC_000918.1.
DR PDB; 2IF2; X-ray; 3.00 A; A/B/C=1-196.
DR PDBsum; 2IF2; -.
DR AlphaFoldDB; O67792; -.
DR SMR; O67792; -.
DR STRING; 224324.aq_1985; -.
DR EnsemblBacteria; AAC07761; AAC07761; aq_1985.
DR KEGG; aae:aq_1985; -.
DR PATRIC; fig|224324.8.peg.1534; -.
DR eggNOG; COG0237; Bacteria.
DR HOGENOM; CLU_057180_2_1_0; -.
DR InParanoid; O67792; -.
DR OMA; QMDIEQK; -.
DR OrthoDB; 1515383at2; -.
DR UniPathway; UPA00241; UER00356.
DR EvolutionaryTrace; O67792; -.
DR Proteomes; UP000000798; Chromosome.
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; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR InterPro; IPR001977; Depp_CoAkinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01121; CoaE; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00152; TIGR00152; 1.
DR PROSITE; PS51219; DPCK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..196
FT /note="Dephospho-CoA kinase"
FT /id="PRO_0000172900"
FT DOMAIN 3..196
FT /note="DPCK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT BINDING 11..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00376"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2IF2"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:2IF2"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:2IF2"
FT HELIX 31..36
FT /evidence="ECO:0007829|PDB:2IF2"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2IF2"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:2IF2"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:2IF2"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:2IF2"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:2IF2"
FT HELIX 77..91
FT /evidence="ECO:0007829|PDB:2IF2"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2IF2"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:2IF2"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:2IF2"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:2IF2"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2IF2"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:2IF2"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:2IF2"
FT HELIX 148..155
FT /evidence="ECO:0007829|PDB:2IF2"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:2IF2"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:2IF2"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:2IF2"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:2IF2"
SQ SEQUENCE 196 AA; 22930 MW; DD691CBCD7B1C0E2 CRC64;
MKRIGLTGNI GCGKSTVAQM FRELGAYVLD ADKLIHSFYR KGHPVYEEVV KTFGKGILDE
EGNIDRKKLA DIVFKDEEKL RKLEEITHRA LYKEIEKITK NLSEDTLFIL EASLLVEKGT
YKNYDKLIVV YAPYEVCKER AIKRGMSEED FERRWKKQMP IEEKVKYADY VIDNSGSIEE
TYKQVKKVYE ELTRDP
