| Definition | Akkermansia muciniphila ATCC BAA-835, complete genome. |
|---|---|
| Accession | NC_010655 |
| Length | 2,664,102 |
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The map label for this gene is aas [H]
Identifier: 187735101
GI number: 187735101
Start: 705068
End: 705679
Strand: Direct
Name: aas [H]
Synonym: Amuc_0595
Alternate gene names: 187735101
Gene position: 705068-705679 (Clockwise)
Preceding gene: 187735100
Following gene: 187735102
Centisome position: 26.47
GC content: 57.19
Gene sequence:
>612_bases ATGAACTCTTTCTACTGGGTTTTCTACACGCTCTTCAAAAGCATTTCCAAAGCCTTCTTCTCCTGGAAAGTCGTCAACCG GGAAAAACTCATCGAAGACGGCCCCGTGCTCATCGTCAGCAATCACCAGAGCTTTCTGGATCCGCCCATGCTGGGCATTT CCTATGAGGACGGCATCTATTTTTTCGCACGCAAGACACTGTTCCAGGGCATTTTCAAATGGGCCCTGCCCCTCTGCCAG GCTATCCCCATTGACCAGGAAAACCCGGATGCCGCCAGCCTCAAGCACGTGATACGCCTGCTGAAATCCGGCAAGCGCGT ACTCGTGTTTCCGGAAGGCTCCCGCACGCCGGATGGTGAAATCCATGACGGCATGGGCGGGATCGGCCTCATCCTGAGCA AAACGAAAGTTCCCGTGCAGCCCCTGCGCATCAGCGGTGCGTATGAAGCCTTTCCCATCGGCGCCCGGTTTCCCAGGCTC CGCCCCGTCACGGTCACGGTGGGAGACCCCATCCCCTTCACGCCGGCGGAACTCAACGCCAAAGGAAAAGATGCATACCA GCACCTGACGGACAAAATCATGGACGCCATCCGCTCCCTCCCTGCGGAATAA
Upstream 100 bases:
>100_bases CGCAGGCGCCTGACGCTCTTCTGGTGGATACGTCAGACATGACGATTGACCAGGTCGTCCGTTTCATCACCGACAACATC CAACAAAAACTCTCCTCCAG
Downstream 100 bases:
>100_bases CCCCTTTCCCGGCCCCATGATCTCCAGGCTGAAATTAATGGACTTCCGTTGCTACGGAAGCTTCTCCTGGCAGATTCCGC AGCAGGGGGCCATCATCCTG
Product: phospholipid/glycerol acyltransferase
Products: NA
Alternate protein names: 2-acylglycerophosphoethanolamine acyltransferase; 2-acyl-GPE acyltransferase; Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase; Acyl-[acyl-carrier-protein] synthetase; Acyl-ACP synthetase; Long-chain-fatty-acid--[acyl-carrier-protein] ligase [H]
Number of amino acids: Translated: 203; Mature: 203
Protein sequence:
>203_residues MNSFYWVFYTLFKSISKAFFSWKVVNREKLIEDGPVLIVSNHQSFLDPPMLGISYEDGIYFFARKTLFQGIFKWALPLCQ AIPIDQENPDAASLKHVIRLLKSGKRVLVFPEGSRTPDGEIHDGMGGIGLILSKTKVPVQPLRISGAYEAFPIGARFPRL RPVTVTVGDPIPFTPAELNAKGKDAYQHLTDKIMDAIRSLPAE
Sequences:
>Translated_203_residues MNSFYWVFYTLFKSISKAFFSWKVVNREKLIEDGPVLIVSNHQSFLDPPMLGISYEDGIYFFARKTLFQGIFKWALPLCQ AIPIDQENPDAASLKHVIRLLKSGKRVLVFPEGSRTPDGEIHDGMGGIGLILSKTKVPVQPLRISGAYEAFPIGARFPRL RPVTVTVGDPIPFTPAELNAKGKDAYQHLTDKIMDAIRSLPAE >Mature_203_residues MNSFYWVFYTLFKSISKAFFSWKVVNREKLIEDGPVLIVSNHQSFLDPPMLGISYEDGIYFFARKTLFQGIFKWALPLCQ AIPIDQENPDAASLKHVIRLLKSGKRVLVFPEGSRTPDGEIHDGMGGIGLILSKTKVPVQPLRISGAYEAFPIGARFPRL RPVTVTVGDPIPFTPAELNAKGKDAYQHLTDKIMDAIRSLPAE
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 magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-
COG id: COG0204
COG function: function code I; 1-acyl-sn-glycerol-3-phosphate acyltransferase
Gene ontology:
Cell location: Cell inner membrane; Multi-pass membrane protein [H]
Metaboloic importance: Non_Essential [C]
Operon status: Not Known
Operon components: None
Similarity: In the C-terminal section; belongs to the ATP- dependent AMP-binding enzyme family [H]
Homologues:
Organism=Escherichia coli, GI1789201, Length=142, Percent_Identity=28.169014084507, Blast_Score=71, Evalue=5e-14,
Paralogues:
None
Copy number: NA
Swissprot (AC and ID): NA
Other databases:
- InterPro: IPR002123 - InterPro: IPR020845 - InterPro: IPR000873 [H]
Pfam domain/function: PF01553 Acyltransferase; PF00501 AMP-binding [H]
EC number: =2.3.1.40; =6.2.1.20 [H]
Molecular weight: Translated: 22722; Mature: 22722
Theoretical pI: Translated: 9.58; Mature: 9.58
Prosite motif: NA
Important sites: NA
Signals:
None
Transmembrane regions:
None
Cys/Met content:
0.5 %Cys (Translated Protein) 2.0 %Met (Translated Protein) 2.5 %Cys+Met (Translated Protein) 0.5 %Cys (Mature Protein) 2.0 %Met (Mature Protein) 2.5 %Cys+Met (Mature Protein)
Secondary structure:
>Translated Secondary Structure MNSFYWVFYTLFKSISKAFFSWKVVNREKLIEDGPVLIVSNHQSFLDPPMLGISYEDGIY CCCEEHHHHHHHHHHHHHHHHEEEECHHHHHCCCCEEEEECCHHHCCCCCCCEEECCCCH FFARKTLFQGIFKWALPLCQAIPIDQENPDAASLKHVIRLLKSGKRVLVFPEGSRTPDGE HHHHHHHHHHHHHHHHHHHHHCCCCCCCCCHHHHHHHHHHHHCCCEEEEEECCCCCCCCC IHDGMGGIGLILSKTKVPVQPLRISGAYEAFPIGARFPRLRPVTVTVGDPIPFTPAELNA CCCCCCCEEEEEECCCCCCCCEEECCCCCCCCCCCCCCCCEEEEEEECCCCCCCCCCCCC KGKDAYQHLTDKIMDAIRSLPAE CCHHHHHHHHHHHHHHHHHCCCC >Mature Secondary Structure MNSFYWVFYTLFKSISKAFFSWKVVNREKLIEDGPVLIVSNHQSFLDPPMLGISYEDGIY CCCEEHHHHHHHHHHHHHHHHEEEECHHHHHCCCCEEEEECCHHHCCCCCCCEEECCCCH FFARKTLFQGIFKWALPLCQAIPIDQENPDAASLKHVIRLLKSGKRVLVFPEGSRTPDGE HHHHHHHHHHHHHHHHHHHHHCCCCCCCCCHHHHHHHHHHHHCCCEEEEEECCCCCCCCC IHDGMGGIGLILSKTKVPVQPLRISGAYEAFPIGARFPRLRPVTVTVGDPIPFTPAELNA CCCCCCCEEEEEECCCCCCCCEEECCCCCCCCCCCCCCCCEEEEEEECCCCCCCCCCCCC KGKDAYQHLTDKIMDAIRSLPAE CCHHHHHHHHHHHHHHHHHCCCC
PDB accession: NA
Resolution: NA
Structure class: Alpha Beta
Cofactors: NA
Metal ions: NA
Kcat value (1/min): NA
Specific activity: NA
Km value (mM): NA
Substrates: NA
Specific reaction: NA
General reaction: NA
Inhibitor: NA
Structure determination priority: 7.0
TargetDB status: NA
Availability: NA
References: NA