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
TTACTTTATATTTTTCTTATAGATATTAAGTAATCCTTTTAATACAAGCTCTTTATCTTG
CTTAATATCTAACCTAATGTGTTCTAAGATTAAACTAGATAGGCCACCAGTGATGATTAC
ATCAAAATCTTCGCCTACCTCTTCTCTAATACGGCCAAACATACCTTCAATCATAACAAT
AGTCCCGTAGACAACACCTGATTGAATACAGTGAATCGTATTATTGCCTAAATATTTTTT
AGGTACTTTAATATCCACTTCATGTAAGAGTGCAGTATTTCCATCTAGCGCATGAATCGA
TAGTTGAAGACCTGGTGCAATAATAACACCAGTTATCATTTGGTTTTTTACATAGATTAA
TTTGTTGGCAGTACCTAAGTCTATAATCAGTGTTGGATGTGGGTTATCTAAACCTGCAGC
ATTTGCGATTAAGTCTGCACCAACTTCTCTAGGGTTATCTGCTTTGACAAAAATACCAGT
TTTTGTGCCTGGTTCAATAACGACTGGTTTTAGTTTTAAATATTTTTCAGTTAATGCAAT
TAAAGCTTGTGTAACAAGCGGTACGACTGAACCAATAATAACGCCAGTAATGACATTTGG
ATCAATAAAAGATTTTAATGTGACAAAATATTCATCCGGTGATTTATGGATATCGGTATT
CATTCTAAATGTCTCATCAATGTTTGTACCATTGGATAAACCTGTATAAATACTAGTATT
ACCTACATCAAATAATATAATCAT


>protein sequence
MIILFDVGNTSIYTGLSNGTNIDETFRMNTDIHKSPDEYFVTLKSFIDPNVITGVIIGSV
VPLVTQALIALTEKYLKLKPVVIEPGTKTGIFVKADNPREVGADLIANAAGLDNPHPTLI
IDLGTANKLIYVKNQMITGVIIAPGLQLSIHALDGNTALLHEVDIKVPKKYLGNNTIHCI
QSGVVYGTIVMIEGMFGRIREEVGEDFDVIITGGLSSLILEHIRLDIKQDKELVLKGLLN
IYKKNIK






















© Fisunov Lab of Proteomics, 2016.