ID L8LPY9_9CHRO Unreviewed; 508 AA.
AC L8LPY9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=GLO73106DRAFT_00019030 {ECO:0000313|EMBL:ELR98081.1};
OS Gloeocapsa sp. PCC 73106.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Chroococcaceae; Gloeocapsa.
OX NCBI_TaxID=102232 {ECO:0000313|EMBL:ELR98081.1, ECO:0000313|Proteomes:UP000011180};
RN [1] {ECO:0000313|EMBL:ELR98081.1, ECO:0000313|Proteomes:UP000011180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 73106 {ECO:0000313|EMBL:ELR98081.1,
RC ECO:0000313|Proteomes:UP000011180};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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:ELR98081.1}.
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DR EMBL; ALVY01000193; ELR98081.1; -; Genomic_DNA.
DR AlphaFoldDB; L8LPY9; -.
DR STRING; 102232.GLO73106DRAFT_00019030; -.
DR PATRIC; fig|102232.3.peg.2121; -.
DR eggNOG; COG0237; Bacteria.
DR eggNOG; COG0614; Bacteria.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000011180; 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:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01144; BtuF; 1.
DR CDD; cd02022; DPCK; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR InterPro; IPR002491; ABC_transptr_periplasmic_BD.
DR InterPro; IPR001977; Depp_CoAkinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00152; dephospho-CoA kinase; 1.
DR PANTHER; PTHR42860; VITAMIN B12-BINDING PROTEIN; 1.
DR PANTHER; PTHR42860:SF1; VITAMIN B12-BINDING PROTEIN; 1.
DR Pfam; PF01121; CoaE; 1.
DR Pfam; PF01497; Peripla_BP_2; 1.
DR SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51219; DPCK; 1.
DR PROSITE; PS50983; FE_B12_PBP; 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:ELR98081.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00376}; Reference proteome {ECO:0000313|Proteomes:UP000011180};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00376}.
FT DOMAIN 196..484
FT /note="Fe/B12 periplasmic-binding"
FT /evidence="ECO:0000259|PROSITE:PS50983"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00376"
SQ SEQUENCE 508 AA; 56659 MW; 7934DEBD4120336C CRC64;
MKRIIGLTGG IATGKTTVSD YLAQKYQLRI FDADIYAREA VALGSPLLED IYQRYGDSLR
LADGSLNRQA LGEIIFAQPQ EKAWLESLIH PYVRAKLESA LAKESDSLIV LVIPLLFEAQ
MKDLVTEIWV VSSTEQLQRL QKRNNLSESE AIARIQSQLP LEVKIASADL VLSNDSTVEH
LYQQVDLAMS RGTSLKIVTL LPSATEIVAS LGLIESLVGR SHECDYPPGV EDLPVCTRAK
INSDRSSYQI DTDVKALFNN ALSIYDLDIE TLKQLQPTHI ITQDQCELCA VSFSLVESAV
KELLPSQPQV ISLQPDTLSQ VWQDIQRVGK ALSINAQPTL NSLKARVEVI SSYSQSLPSS
QIPQVLALEW IDPLMVGGNW IPELIELAGG KPLFAQTGQP SRYLNWQEVE DNQPDIIVVM
PCGFNLERNL VEIEVLKPNP AWQNLVAVQQ NRVFLVDGNA YFNRPGPRLV DSLEILAQIF
HPERFNFDLP HPLNKNGVHA DKIKRLLF
//
