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