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Literature summary extracted from

  • Bhatt, K.; Gurcha, S.S.; Bhatt, A.; Besra, G.S.; Jacobs, W.R.
    Two polyketide-synthase-associated acyltransferases are required for sulfolipid biosynthesis in Mycobacterium tuberculosis (2007), Microbiology, 153, 513-520 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.288 D170A catalytically inactive Mycobacterium tuberculosis
2.3.1.288 H166A catalytically inactive Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.283 Mycobacterium tuberculosis P9WIK9
-
-
2.3.1.283 Mycobacterium tuberculosis H37Rv P9WIK9
-
-
2.3.1.287 Mycobacterium tuberculosis
-
-
-
2.3.1.287 Mycobacterium tuberculosis H37Rv
-
-
-
2.3.1.288 Mycobacterium tuberculosis P9WIK7
-
-
2.3.1.288 Mycobacterium tuberculosis ATCC 25618 P9WIK7
-
-

Synonyms

EC Number Synonyms Comment Organism
2.3.1.283 Rv3824c
-
 Mycobacterium tuberculosis
2.3.1.283 SL659 acyltransferase PapA1
-
 Mycobacterium tuberculosis
2.3.1.287 Pks2
-
 Mycobacterium tuberculosis
2.3.1.287 polyketide synthase
-
 Mycobacterium tuberculosis
2.3.1.288 papA2
-
 Mycobacterium tuberculosis
2.3.1.288 Rv3820c
-
 Mycobacterium tuberculosis
2.3.1.288 trehalose-2-sulfate acyltransferase
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
2.3.1.283 physiological function deletion of the H37Rv PapA1 gene results in loss of sulfolipid-I Mycobacterium tuberculosis
2.3.1.287 metabolism the enzyme synthesizes the methyl-branched fatty acyl components of sulfolipid-I Mycobacterium tuberculosis
2.3.1.288 physiological function deletion of PapA2 gene abolishes sulfolipid-I production. Both acyltransferases PapA1 and PapA2 are required for all acylation steps of sulfolipid-I assembly Mycobacterium tuberculosis