ACL_RS01115
  | Uniprot: A9NES3
Description: phosphate acyltransferase EC number: 2.3.1.n2 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + phosphate = acyl-phosphate + [acyl-carrier-protein]. {ECO:0000255|HAMAP-Rule:MF_00019}. Cofactor: Enzyme regulation: Function [CC]: FUNCTION: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00019}. Pathway: PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000255|HAMAP-Rule:MF_00019}. Active site: Binding site: Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: Gene names (primary): plsX Gene names (synonym): Mass: 36,477 Subunit structure [CC]: SUBUNIT: Homodimer. Probably interacts with PlsY. {ECO:0000255|HAMAP-Rule:MF_00019}. Gene ontology (GO): cytoplasm [GO:0005737]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]; transferase activity, transferring acyl groups other than amino-acyl groups [GO:0016747]; fatty acid biosynthetic process [GO:0006633]; phospholipid biosynthetic process [GO:0008654] Gene ontology IDs: GO:0005737; GO:0006633; GO:0008654; GO:0016616; GO:0016747 Chain: CHAIN 1 334 Phosphate acyltransferase. /FTId=PRO_1000201885. Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the PlsX family. {ECO:0000255|HAMAP-Rule:MF_00019}. Protein families: PlsX family Coiled coil: Domain [FT]: Motif: Region: EMBL: CP000896 ProteinModelPortal: A9NES3 MEROPS: EnsemblBacteria KO: ABX80853 UniPathway: K03621 CDD: Gene3D: HAMAP: 3.40.718.10 InterPro: MF_00019 PANTHER: IPR003664;IPR024084;IPR012281 PIRSF: PRINTS: PIRSF002465 PROSITE: Pfam: ProDom: PF02504 SMART: SUPFAM: TIGRFAMs: |
219414-220419(+) >nucleotide sequence GGCTCTATTTTAGCTTTAAAGCAGTTTGATGACATTGAACTTACTATTTTTGGTGATGTT GATAAAATGAAACCATATTTAATTGAACATCCAAGATTAAAGGTAGTTCATACACCGAAA TATTTTGAAATGGGTGTAAAAGATATTGGAAGACACACCTTAAGAGATGATAAAGATACA TCGATGTTAATGGCGATTAATCATGTAAAAGAAGGTTTAGCGGATGGTGTAGTGTCCAGT GGTCCTACACAAGCACTTATTTTTGCATCATTTTTTATGATTCGTCCGATGAAAGAAATG AAACGTGTAGCGATTGCACCCATGGTACCAACCGTGATTGGAAAACCTACAATCTTACTT GATGCAGGTGGAAATATTGATGCAAAAGCTGAGCATCTTTTAGACTTTGCAATATTTTCA ACAATTGCCTTAAAAGAAGTTTATGGTGTTAAATCCCCTAAAGTTGGATTAATTAATATT GGTACAGAACCCGGAAAAGGTAGAGATATTGATAAAGAAACTTTTGAGTTATTAAGTAAG CATCCATTAATTGATTTTTACGGCAACTTAGAACCAAAAGAAATTTTAACATCTGATGCA CAGATCTTACTTTCTGACGGATTTACTGCAAATATCGTCATGAAAACCATGGAAGGTACA GCAAGTGCCTTAGGTAAAATTCTAAAAAGAGAAATTAAAGCAAGCTTCTGGGGTAAACTC GCAGCAGTTTTATTCTTGAAAAAACCATTAAAGAGATTTAAACAATCCATGTCTGCTGAT GAAGTAGGTGGAGCATTAATTGCAGGGCTTGATAAAGTTGTAGTTAAAGCACACGGTTCT AGCGAGGCTTACGCATTTATGAATGCTATTAGACAAGCTAAAACAATGGTTTCACATGAC GTGATTGGTAAAGTAAAAAATGTATTGAGGGGTCAAGATGAATGA >protein sequence YFEMGVKDIGRHTLRDDKDTSMLMAINHVKEGLADGVVSSGPTQALIFASFFMIRPMKEM KRVAIAPMVPTVIGKPTILLDAGGNIDAKAEHLLDFAIFSTIALKEVYGVKSPKVGLINI GTEPGKGRDIDKETFELLSKHPLIDFYGNLEPKEILTSDAQILLSDGFTANIVMKTMEGT ASALGKILKREIKASFWGKLAAVLFLKKPLKRFKQSMSADEVGGALIAGLDKVVVKAHGS SEAYAFMNAIRQAKTMVSHDVIGKVKNVLRGQDEW |
© Fisunov Lab of Proteomics, 2016.