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
ATGATAAAACTAGCAATTGATGGTATGGGTGGCGACAACGCACCTAAAGAAATAGTAGAG
GGCTCTATTTTAGCTTTAAAGCAGTTTGATGACATTGAACTTACTATTTTTGGTGATGTT
GATAAAATGAAACCATATTTAATTGAACATCCAAGATTAAAGGTAGTTCATACACCGAAA
TATTTTGAAATGGGTGTAAAAGATATTGGAAGACACACCTTAAGAGATGATAAAGATACA
TCGATGTTAATGGCGATTAATCATGTAAAAGAAGGTTTAGCGGATGGTGTAGTGTCCAGT
GGTCCTACACAAGCACTTATTTTTGCATCATTTTTTATGATTCGTCCGATGAAAGAAATG
AAACGTGTAGCGATTGCACCCATGGTACCAACCGTGATTGGAAAACCTACAATCTTACTT
GATGCAGGTGGAAATATTGATGCAAAAGCTGAGCATCTTTTAGACTTTGCAATATTTTCA
ACAATTGCCTTAAAAGAAGTTTATGGTGTTAAATCCCCTAAAGTTGGATTAATTAATATT
GGTACAGAACCCGGAAAAGGTAGAGATATTGATAAAGAAACTTTTGAGTTATTAAGTAAG
CATCCATTAATTGATTTTTACGGCAACTTAGAACCAAAAGAAATTTTAACATCTGATGCA
CAGATCTTACTTTCTGACGGATTTACTGCAAATATCGTCATGAAAACCATGGAAGGTACA
GCAAGTGCCTTAGGTAAAATTCTAAAAAGAGAAATTAAAGCAAGCTTCTGGGGTAAACTC
GCAGCAGTTTTATTCTTGAAAAAACCATTAAAGAGATTTAAACAATCCATGTCTGCTGAT
GAAGTAGGTGGAGCATTAATTGCAGGGCTTGATAAAGTTGTAGTTAAAGCACACGGTTCT
AGCGAGGCTTACGCATTTATGAATGCTATTAGACAAGCTAAAACAATGGTTTCACATGAC
GTGATTGGTAAAGTAAAAAATGTATTGAGGGGTCAAGATGAATGA


>protein sequence
MIKLAIDGMGGDNAPKEIVEGSILALKQFDDIELTIFGDVDKMKPYLIEHPRLKVVHTPK
YFEMGVKDIGRHTLRDDKDTSMLMAINHVKEGLADGVVSSGPTQALIFASFFMIRPMKEM
KRVAIAPMVPTVIGKPTILLDAGGNIDAKAEHLLDFAIFSTIALKEVYGVKSPKVGLINI
GTEPGKGRDIDKETFELLSKHPLIDFYGNLEPKEILTSDAQILLSDGFTANIVMKTMEGT
ASALGKILKREIKASFWGKLAAVLFLKKPLKRFKQSMSADEVGGALIAGLDKVVVKAHGS
SEAYAFMNAIRQAKTMVSHDVIGKVKNVLRGQDEW






















© Fisunov Lab of Proteomics, 2016.