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The map label for this gene is aas [C]

Identifier: 195952811

GI number: 195952811

Start: 378686

End: 379327

Strand: Direct

Name: aas [C]

Synonym: HY04AAS1_0433

Alternate gene names: 195952811

Gene position: 378686-379327 (Clockwise)

Preceding gene: 195952810

Following gene: 195952814

Centisome position: 24.28

GC content: 36.29

Gene sequence:

>642_bases
ATGGAATGCCCAGATACAACGCTTGGGAAATATGTGATAAAACCTCTTTGGTTTGGTATAAGAGGTATTTTTAGAAGTGT
ATTTAAGATTAGGGCTTTTAACATAGAAAATATAGAAGGGCTTGAAGGGGTTATTTTTGCATCAAACCACAGATCTCATT
TAGATCCACCAGTGTTAAACGCTTTGGTAAAAGAACCTCTTTATTTTATCGCCAAGAAGGAGCTTTTTGAAGCACCTGTC
ATAGGATTTTTATACAACCATATGAGGGCTATACCAGTCCAAAGAGGTTCTGGAGATTTTGGAGCTATTGAAAAGGCTAT
AGAGCTTTTAAATATCGGTTGTAATGTTTGCATATTTCCAGAGGGAAGAAGAGCGCCAGCTGGGGAGTTTTTAAAACCAA
AAACTGGTGTTGGTATAATGGTTGTAAAAACCAAAAAACCAGTGATACCAATATACATTGAAAATACGGATGTAAATTTT
CCTATAGGAGCAAAGTATCCAGTGCCAAAAGAGCCTATAAACGTATACTTTGGAAAGCCCATTCATTTTGGAGATTTAGA
AGATAACATTCAAAGCTACAAACTTGTGGCAAACACCATAATGGAGCACATCAAAGAACTTGCCTACAATAAACCTACTT
GA

Upstream 100 bases:

>100_bases
TGGCTTATCTCAAAATGCCTTTTTGTTTTCACAATCTTATTCCAAATCTTATTTTTGCGGGAAATATAAAAATATCATTA
CTATGCTATAATACTCTAAG

Downstream 100 bases:

>100_bases
ATTTAGGAAGTTTCCATTTTAACATTATAGCCAACATCCTTATTGAAAAAACCGATATTACACAAAAAGATGCCGCAAGC
GTTATGTTTTTGAAAAACAT

Product: phospholipid/glycerol acyltransferase

Products: AMP; diphosphate; acyl-[acyl-carrier protein]

Alternate protein names: Phospholipid/Glycerol Acyltransferase; Acyltransferase; 1-Acylglycerol-3-Phosphate O-Acyltransferase; 2-Acylglycerophosphoethanolamine Acyltransferase; Acyltransferase Domain Protein; Transferase; 1-Acyl-Sn-Glycerol-3-Phosphate Acyltransferases; Long-Chain-Fatty-Acid CoA Ligase; 1-Acyl-Sn-Glycerol-3-Phosphateacyltransferase-Like Protein; Glycerol-3-Phosphate Acyltransferase; 1-Acylglycerol-3-Phosphate O-Acyltransferase Putayive; [Acyl-]Glycerolphosphate Acyltransferase; Glycerol-3-P Acyltransferase; AMP-Dependent Synthetase And Ligase; 1-Acyl-Sn-Glycerol-3-Phosphate Acetyltransferase; Acyltransferase PlsC; L-Acyl-Sn-Glycerol-3-Phosphate Acetyltransferase; Cytidylate Kinase

Number of amino acids: Translated: 213; Mature: 213

Protein sequence:

>213_residues
MECPDTTLGKYVIKPLWFGIRGIFRSVFKIRAFNIENIEGLEGVIFASNHRSHLDPPVLNALVKEPLYFIAKKELFEAPV
IGFLYNHMRAIPVQRGSGDFGAIEKAIELLNIGCNVCIFPEGRRAPAGEFLKPKTGVGIMVVKTKKPVIPIYIENTDVNF
PIGAKYPVPKEPINVYFGKPIHFGDLEDNIQSYKLVANTIMEHIKELAYNKPT

Sequences:

>Translated_213_residues
MECPDTTLGKYVIKPLWFGIRGIFRSVFKIRAFNIENIEGLEGVIFASNHRSHLDPPVLNALVKEPLYFIAKKELFEAPV
IGFLYNHMRAIPVQRGSGDFGAIEKAIELLNIGCNVCIFPEGRRAPAGEFLKPKTGVGIMVVKTKKPVIPIYIENTDVNF
PIGAKYPVPKEPINVYFGKPIHFGDLEDNIQSYKLVANTIMEHIKELAYNKPT
>Mature_213_residues
MECPDTTLGKYVIKPLWFGIRGIFRSVFKIRAFNIENIEGLEGVIFASNHRSHLDPPVLNALVKEPLYFIAKKELFEAPV
IGFLYNHMRAIPVQRGSGDFGAIEKAIELLNIGCNVCIFPEGRRAPAGEFLKPKTGVGIMVVKTKKPVIPIYIENTDVNF
PIGAKYPVPKEPINVYFGKPIHFGDLEDNIQSYKLVANTIMEHIKELAYNKPT

Specific function: Plays A Role In Lysophospholipid Acylation. Transfers Fatty Acids To The 1-Position VIa An Enzyme-Bound Acyl-Acp Intermediate In The Presence Of ATP And Mg(2+). Its Physiological Function Is To Regenerate Ptdetn From 2-Acyl-Gpe Formed By Transacylation R

COG id: COG0204

COG function: function code I; 1-acyl-sn-glycerol-3-phosphate acyltransferase

Gene ontology:

Cell location: Integral Membrane Protein. Inner Membrane [C]

Metaboloic importance: Non_Essential [C]

Operon status: Not Known

Operon components: None

Similarity: NA

Homologues:

None

Paralogues:

None

Copy number: NA

Swissprot (AC and ID): NA

Other databases:

NA

Pfam domain/function: NA

EC number: 6.2.1.20

Molecular weight: Translated: 23927; Mature: 23927

Theoretical pI: Translated: 9.04; Mature: 9.04

Prosite motif: NA

Important sites: NA

Signals:

None

Transmembrane regions:

None

Cys/Met content:

1.4 %Cys     (Translated Protein)
1.9 %Met     (Translated Protein)
3.3 %Cys+Met (Translated Protein)
1.4 %Cys     (Mature Protein)
1.9 %Met     (Mature Protein)
3.3 %Cys+Met (Mature Protein)

Secondary structure:

>Translated Secondary Structure
MECPDTTLGKYVIKPLWFGIRGIFRSVFKIRAFNIENIEGLEGVIFASNHRSHLDPPVLN
CCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCEEEEECCCCCCCCHHHHH
ALVKEPLYFIAKKELFEAPVIGFLYNHMRAIPVQRGSGDFGAIEKAIELLNIGCNVCIFP
HHHHHHHHHHHHHHHHHCHHHHHHHHHHHCCCCCCCCCCHHHHHHHHHHHHCCCCEEECC
EGRRAPAGEFLKPKTGVGIMVVKTKKPVIPIYIENTDVNFPIGAKYPVPKEPINVYFGKP
CCCCCCCCCCCCCCCCCEEEEEECCCCEEEEEEECCCCCCCCCCCCCCCCCCCEEEECCC
IHFGDLEDNIQSYKLVANTIMEHIKELAYNKPT
EECCCCHHHHHHHHHHHHHHHHHHHHHHCCCCC
>Mature Secondary Structure
MECPDTTLGKYVIKPLWFGIRGIFRSVFKIRAFNIENIEGLEGVIFASNHRSHLDPPVLN
CCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCEEEEECCCCCCCCHHHHH
ALVKEPLYFIAKKELFEAPVIGFLYNHMRAIPVQRGSGDFGAIEKAIELLNIGCNVCIFP
HHHHHHHHHHHHHHHHHCHHHHHHHHHHHCCCCCCCCCCHHHHHHHHHHHHCCCCEEECC
EGRRAPAGEFLKPKTGVGIMVVKTKKPVIPIYIENTDVNFPIGAKYPVPKEPINVYFGKP
CCCCCCCCCCCCCCCCCEEEEEECCCCEEEEEEECCCCCCCCCCCCCCCCCCCEEEECCC
IHFGDLEDNIQSYKLVANTIMEHIKELAYNKPT
EECCCCHHHHHHHHHHHHHHHHHHHHHHCCCCC

PDB accession: NA

Resolution: NA

Structure class: Unstructured

Cofactors: NA

Metal ions: NA

Kcat value (1/min): NA

Specific activity: NA

Km value (mM): NA

Substrates: ATP; acid; [acyl-carrier protein]

Specific reaction: ATP + an acid + [acyl-carrier protein] = AMP + diphosphate + acyl-[acyl-carrier protein]

General reaction: NA

Inhibitor: NA

Structure determination priority: 7.0

TargetDB status: NA

Availability: NA

References: NA