ORENZA : a database of ORphan ENZyme Activities

ORphan ENZyme ActivitiesSorted by :
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EC used by the NC-IUBMBSorted by :
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EC 2.7.8.9 is Orphan !
Common name :Phosphomannan mannosephosphotransferase

Systematic name :GDP-mannose:phosphomannan mannose phosphotransferase

Other names :CDP-diacylglycerol--L-serine O-phosphatidyltransferase
CDP-diglyceride:serine phosphatidyltransferase
CDP-diglyceride--L-serine phosphatidyltransferase
CDPdiacylglycerol--serine O-phosphatidyltransferase
CDPdiglyceride--serine O-phosphatidyltransferase
PS synthase
Cytidine 5''-diphospho-1,2-diacyl-sn-glycerol (CDPdiglyceride):L-serine O-phosphatidyltransferase
Cytidine 5''-diphospho-1,2-diacyl-sn-glycerol:L-serine O-phosphatidyltransferase
Cytidine diphosphoglyceride--serine O-phosphatidyltransferase
Phosphatidylserine synthase
Phosphatidylserine synthetase
CDP-diglycerine-serine O-phosphatidyltransferase
CDP-diacylglycerol:L-serine 3-O-phosphatidyltransferase
Comments :Requires Mg(2+). All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. The inactive apo-proteins are converted into their active holo-forms by transfer of the 4''''-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain (3). The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes (6). Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14, (acyl-carrier-protein) phosphodiesterase. All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. The inactive apo-proteins are converted into their active holo-forms by transfer of the 4''''-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain. The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes. Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14.

Created :EC 2.7.8.9 created 1972

BRENDA organisms :Nakazawaea holstii

Swiss-ProtNo protein sequences are associated with EC 2.7.8.9 in Swiss-Prot

TrEMBLNo protein sequences are associated with EC 2.7.8.9 in TrEMBL

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for EC 2.7.8.9.

Links to other databases
NC-IUBMB, INTENZ, ENZYME, PDB, BRENDA, KEGG, BIOCYC, PubMed,NCBI-Entrez

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