ACL_RS04205
  | Uniprot: A9NGI4
Description: type III pantothenate kinase EC number: 2.7.1.33 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate. {ECO:0000255|HAMAP-Rule:MF_01274}. Cofactor: COFACTOR: Name=NH4(+); Xref=ChEBI:CHEBI:28938; Evidence={ECO:0000255|HAMAP-Rule:MF_01274}; Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_01274}; ; Note=A monovalent cation. Ammonium or potassium. {ECO:0000255|HAMAP-Rule:MF_01274} Enzyme regulation: Function [CC]: FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01274}. Pathway: PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. {ECO:0000255|HAMAP-Rule:MF_01274}. Active site: ACT_SITE 104 104 Proton acceptor. {ECO:0000255|HAMAP-Rule:MF_01274}. Binding site: BINDING 125 125 ATP. {ECO:0000255|HAMAP-Rule:MF_01274}.; BINDING 176 176 Substrate. {ECO:0000255|HAMAP-Rule:MF_01274}. Calcium binding: DNA binding: Metal binding: METAL 122 122 Monovalent cation. {ECO:0000255|HAMAP-Rule:MF_01274}. Nucleotide binding: NP_BIND 6 13 ATP. {ECO:0000255|HAMAP-Rule:MF_01274}. Site: Gene names (primary): coaX Gene names (synonym): Mass: 26,972 Subunit structure [CC]: SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01274}. Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; pantothenate kinase activity [GO:0004594]; coenzyme A biosynthetic process [GO:0015937] Gene ontology IDs: GO:0004594; GO:0005524; GO:0005737; GO:0015937; GO:0046872 Chain: CHAIN 1 247 Type III pantothenate kinase. /FTId=PRO_1000085845. Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the type III pantothenate kinase family. {ECO:0000255|HAMAP-Rule:MF_01274}. Protein families: Type III pantothenate kinase family Coiled coil: Domain [FT]: Motif: Region: REGION 102 105 Substrate binding. {ECO:0000255|HAMAP-Rule:MF_01274}. EMBL: CP000896 ProteinModelPortal: A9NGI4 MEROPS: EnsemblBacteria KO: ABX81464 UniPathway: K03525 CDD: Gene3D: HAMAP: InterPro: MF_01274 PANTHER: IPR004619 PIRSF: PRINTS: PROSITE: Pfam: ProDom: PF03309 SMART: SUPFAM: TIGRFAMs: |
884246-884990(-) >nucleotide sequence CTTAATATCTAACCTAATGTGTTCTAAGATTAAACTAGATAGGCCACCAGTGATGATTAC ATCAAAATCTTCGCCTACCTCTTCTCTAATACGGCCAAACATACCTTCAATCATAACAAT AGTCCCGTAGACAACACCTGATTGAATACAGTGAATCGTATTATTGCCTAAATATTTTTT AGGTACTTTAATATCCACTTCATGTAAGAGTGCAGTATTTCCATCTAGCGCATGAATCGA TAGTTGAAGACCTGGTGCAATAATAACACCAGTTATCATTTGGTTTTTTACATAGATTAA TTTGTTGGCAGTACCTAAGTCTATAATCAGTGTTGGATGTGGGTTATCTAAACCTGCAGC ATTTGCGATTAAGTCTGCACCAACTTCTCTAGGGTTATCTGCTTTGACAAAAATACCAGT TTTTGTGCCTGGTTCAATAACGACTGGTTTTAGTTTTAAATATTTTTCAGTTAATGCAAT TAAAGCTTGTGTAACAAGCGGTACGACTGAACCAATAATAACGCCAGTAATGACATTTGG ATCAATAAAAGATTTTAATGTGACAAAATATTCATCCGGTGATTTATGGATATCGGTATT CATTCTAAATGTCTCATCAATGTTTGTACCATTGGATAAACCTGTATAAATACTAGTATT ACCTACATCAAATAATATAATCAT >protein sequence VPLVTQALIALTEKYLKLKPVVIEPGTKTGIFVKADNPREVGADLIANAAGLDNPHPTLI IDLGTANKLIYVKNQMITGVIIAPGLQLSIHALDGNTALLHEVDIKVPKKYLGNNTIHCI QSGVVYGTIVMIEGMFGRIREEVGEDFDVIITGGLSSLILEHIRLDIKQDKELVLKGLLN IYKKNIK |
© Fisunov Lab of Proteomics, 2016.