SPM_003510
  | Uniprot: A0A037UMG6
Description: transcriptional regulator 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:0000256|HAMAP-Rule:MF_01274, ECO:0000256|SAAS:SAAS00088447}. Cofactor: COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|SAAS:SAAS00611758}; ; COFACTOR: Name=NH4(+); Xref=ChEBI:CHEBI:28938; Evidence={ECO:0000256|HAMAP-Rule:MF_01274}; Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP-Rule:MF_01274}; ; Note=A monovalent cation. Ammonium or potassium. {ECO:0000256|HAMAP-Rule:MF_01274} Enzyme regulation: Function [CC]: FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01274, ECO:0000256|SAAS:SAAS00088441}. Pathway: PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5. {ECO:0000256|HAMAP-Rule:MF_01274, ECO:0000256|SAAS:SAAS00088429}. Active site: ACT_SITE 110 110 Proton acceptor. {ECO:0000256|HAMAP-Rule:MF_01274}. Binding site: BINDING 134 134 ATP. {ECO:0000256|HAMAP-Rule:MF_01274}.; BINDING 185 185 Substrate. {ECO:0000256|HAMAP-Rule:MF_01274}. Calcium binding: DNA binding: Metal binding: Nucleotide binding: NP_BIND 6 13 ATP. {ECO:0000256|HAMAP-Rule:MF_01274}. Site: Gene names (primary): coaX Gene names (synonym): Mass: 28,171 Subunit structure [CC]: SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01274, ECO:0000256|SAAS:SAAS00088433}. Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; pantothenate kinase activity [GO:0004594]; coenzyme A biosynthetic process [GO:0015937] Gene ontology IDs: GO:0004594; GO:0005524; GO:0005737; GO:0015937 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the type III pantothenate kinase family. {ECO:0000256|HAMAP-Rule:MF_01274, ECO:0000256|SAAS:SAAS00571292}. Protein families: Type III pantothenate kinase family Coiled coil: Domain [FT]: Motif: Region: REGION 108 111 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_01274}. EMBL: AGBZ02000001 ProteinModelPortal: MEROPS: EnsemblBacteria KO: KAI93044 UniPathway: CDD: Gene3D: HAMAP: InterPro: MF_01274 PANTHER: IPR004619 PIRSF: PRINTS: PROSITE: Pfam: ProDom: PF03309 SMART: SUPFAM: TIGRFAMs: |
660573-661338(+) >nucleotide sequence AAAAAGATTATTGTTTTTTTAACAATGGCTAGTCGCGAATTAGTTGCTGAAAAAAATTTT CGACAAAAAATAATAGCTGGTTTAAGTACAATAAAATTAGTTCTAACAGATCTTACATTA TTAGCTTTATCTTCAGTTCGACCAATGTGAGATGATTTATTTTATCAGTTGGCTGTCGAT TTAAAAATTCCTTTTTATCAAGTTAAAAAAAATTTGGCCACTGATCGACTAAAAACAGAG ATTCCTAATCCTCGTAATCTTGGTGCTGATTTAATTGTTGGTTCATATGCAACATTAGCT TTATTCCCTAAACAAGATGTTATTTTAGTTAATATGGGGACGGCAACAACAATTTCATTA TTAAAACAAGACACCCTCTTAGGAACAATTATTATGCCAGGTTTAGAAACAGCAGCAGAA GCCTTATTTGAACGAGCACAATTATTACAAAAATTTGATTTTTCTTATGACAATGCTATT TTAGGAAAAAATACTAAGCAAGCAATCAATATTGGATTAGTTAATGGTCATTTATTAGCA ATTACTGCTTTTGTTAATCAACTCGCAACTGAAGTAATAAACCCACAAGTAATTTTAACG GGAGGTAATGCTACTTACATTAAAAAATTAGTTAATTACCATTATGATAAAGATTTACTT TTTAAAGGGTTAGTTACCATTTTACAAGATAATAAATTAATATAA >protein sequence LALSSVRPMWDDLFYQLAVDLKIPFYQVKKNLATDRLKTEIPNPRNLGADLIVGSYATLA LFPKQDVILVNMGTATTISLLKQDTLLGTIIMPGLETAAEALFERAQLLQKFDFSYDNAI LGKNTKQAINIGLVNGHLLAITAFVNQLATEVINPQVILTGGNATYIKKLVNYHYDKDLL FKGLVTILQDNKLI |
© Fisunov Lab of Proteomics, 2016.