Identification |
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Name | Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase |
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Synonyms | - 1-AGP acyltransferase
- 1-AGPAT
- Lysophosphatidic acid acyltransferase
- LPAAT
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Gene Name | SLC1 |
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Enzyme Class | |
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Biological Properties |
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General Function | Involved in acyltransferase activity |
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Specific Function | May be an acyltransferase with an altered substrate specificity that enables it to use a C-26-CoA in place of the C-16 or C-18-CoAs used by the wild-type protein |
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Cellular Location | Membrane; Single-pass membrane protein (Potential) |
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SMPDB Pathways | Cardiolipin Biosynthesis CL(10:0/12:0/18:1(9Z)/22:1(11Z)) | PW003884 | | Cardiolipin Biosynthesis CL(10:0/12:0/18:1(9Z)/22:1(9Z)) | PW003885 | | Cardiolipin Biosynthesis CL(10:0/12:0/18:1(9Z)/24:0) | PW003886 | | Cardiolipin Biosynthesis CL(10:0/12:0/18:1(9Z)/24:1(11Z)) | PW003887 | | Cardiolipin Biosynthesis CL(10:0/12:0/18:1(9Z)/24:1(9Z)) | PW003888 | |
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KEGG Pathways | |
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SMPDB Reactions | LPA(10:0/0:0)
+
long-chain fatty acyl-CoA
→
Coenzyme A
+
PA(10:0/20:0)
| LPA(10:0/0:0)
+
long-chain fatty acyl-CoA
→
Coenzyme A
+
PA(10:0/15:0)
| LPA(12:0/0:0)
+
long-chain fatty acyl-CoA
→
Coenzyme A
+
PA(12:0/16:0)
| LPA(10:0/0:0)
+
long-chain fatty acyl-CoA
→
Coenzyme A
+
PA(10:0/20:1(13Z))
| LPA(10:0/0:0)
+
long-chain fatty acyl-CoA
→
Coenzyme A
+
PA(10:0/15:1(9Z))
|
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KEGG Reactions | |
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Metabolites | YMDB ID | Name | View |
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YMDB00045 | Coenzyme A | Show | YMDB00069 | Palmitic acid | Show | YMDB00301 | Palmityl-CoA | Show | YMDB00539 | oleoyl-CoA | Show | YMDB00862 | hydron | Show | YMDB01127 | DG(16:0/16:0/0:0) | Show | YMDB01160 | PA(16:0/0:0) | Show | YMDB01161 | PA(16:0/16:0) | Show | YMDB16302 | 1-oleyl-2-lyso-phosphatidate | Show |
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GO Classification | Component |
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cell part | membrane | Function |
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acyltransferase activity | O-acyltransferase activity | acylglycerol O-acyltransferase activity | 1-acylglycerol-3-phosphate O-acyltransferase activity | catalytic activity | transferase activity | transferase activity, transferring acyl groups | transferase activity, transferring acyl groups other than amino-acyl groups | Process |
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organophosphate metabolic process | phospholipid metabolic process | phospholipid biosynthetic process | metabolic process |
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Gene Properties |
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Chromosome Location | chromosome 4 |
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Locus | YDL052C |
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Gene Sequence | >912 bp
ATGAGTGTGATAGGTAGGTTCTTGTATTACTTGAGGTCCGTGTTGGTCGTACTGGCGCTT
GCAGGCTGTGGCTTTTACGGTGTAATCGCCTCTATCCTTTGCACGTTAATCGGTAAGCAA
CATTTGGCTCAGTGGATTACTGCGCGTTGTTTTTACCATGTCATGAAATTGATGCTTGGC
CTTGACGTCAAGGTCGTTGGCGAGGAGAATTTGGCCAAGAAGCCATATATTATGATTGCC
AATCACCAATCCACCTTGGATATCTTCATGTTAGGTAGGATTTTCCCCCCTGGTTGCACA
GTTACTGCCAAGAAGTCTTTGAAATACGTCCCCTTTCTGGGTTGGTTCATGGCTTTGAGT
GGTACATATTTCTTAGACAGATCTAAAAGGCAAGAAGCCATTGACACCTTGAATAAAGGT
TTAGAAAATGTTAAGAAAAACAAGCGTGCTCTATGGGTTTTTCCTGAGGGTACCAGGTCT
TACACGAGTGAGCTGACAATGTTGCCTTTCAAGAAGGGTGCTTTCCATTTGGCACAACAG
GGTAAGATCCCCATTGTTCCAGTGGTTGTTTCCAATACCAGTACTTTAGTAAGTCCTAAA
TATGGGGTCTTCAACAGAGGCTGTATGATTGTTAGAATTTTAAAACCTATTTCAACCGAG
AACTTAACAAAGGACAAAATTGGTGAATTTGCTGAAAAAGTTAGAGATCAAATGGTTGAC
ACTTTGAAGGAGATTGGCTACTCTCCCGCCATCAACGATACAACCCTCCCACCACAAGCT
ATTGAGTATGCCGCTCTTCAACATGACAAGAAAGTGAACAAGAAAATCAAGAATGAGCCT
GTGCCTTCTGTCAGCATTAGCAACGATGTCAATACCCATAACGAAGGTTCATCTGTAAAA
AAGATGCATTAA |
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Protein Properties |
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Pfam Domain Function | |
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Protein Residues | 303 |
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Protein Molecular Weight | 33886.69922 |
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Protein Theoretical pI | 10.15 |
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Signalling Regions | |
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Transmembrane Regions | |
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Protein Sequence | >Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase
MSVIGRFLYYLRSVLVVLALAGCGFYGVIASILCTLIGKQHLAQWITARCFYHVMKLMLG
LDVKVVGEENLAKKPYIMIANHQSTLDIFMLGRIFPPGCTVTAKKSLKYVPFLGWFMALS
GTYFLDRSKRQEAIDTLNKGLENVKKNKRALWVFPEGTRSYTSELTMLPFKKGAFHLAQQ
GKIPIVPVVVSNTSTLVSPKYGVFNRGCMIVRILKPISTENLTKDKIGEFAEKVRDQMVD
TLKEIGYSPAINDTTLPPQAIEYAALQHDKKVNKKIKNEPVPSVSISNDVNTHNEGSSVK
KMH |
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References |
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External Links | |
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General Reference | - Nagiec, M. M., Wells, G. B., Lester, R. L., Dickson, R. C. (1993). "A suppressor gene that enables Saccharomyces cerevisiae to grow without making sphingolipids encodes a protein that resembles an Escherichia coli fatty acyltransferase." J Biol Chem 268:22156-22163.8408076
- Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, M., Buitrago, M. J., Coster, F., Delaveau, T., del Rey, F., Dujon, B., Eide, L. G., Garcia-Cantalejo, J. M., Goffeau, A., Gomez-Peris, A., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
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