MULTISPECIES: GDP-perosamine N-acetyltransferase [Escherichia].

LOCUS       WP_001055391             221 aa            linear   BCT 27-AUG-2021
ACCESSION   WP_001055391
VERSION     WP_001055391.1
KEYWORDS    RefSeq.
SOURCE      Escherichia
  ORGANISM  Escherichia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 221)
  AUTHORS   Albermann,C. and Beuttler,H.
  TITLE     Identification of the GDP-N-acetyl-d-perosamine producing enzymes
            from Escherichia coli O157:H7
  JOURNAL   FEBS Lett. 582 (4), 479-484 (2008)
   PUBMED   18201574
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            REFSEQ INFORMATION: The reference sequence is identical to
            AAC32350.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: BlastRule
            Evidence Accession :: NBR009554
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..221
                     /organism="Escherichia"
                     /db_xref="taxon:561"
     gene            1..221
                     /gene="perB"
     Protein         1..221
                     /product="GDP-perosamine N-acetyltransferase"
                     /EC_number="2.3.1.227"
                     /calculated_mol_wt=23611
     Region          6..210
                     /region_name="LbH_AT_putative"
                     /note="Putative Acyltransferase (AT), Left-handed parallel
                     beta-Helix (LbH) domain; This group is composed of mostly
                     uncharacterized proteins containing an N-terminal helical
                     subdomain followed by a LbH domain. The alignment contains
                     6 turns, each containing...; cd03360"
                     /db_xref="CDD:100050"
     Site            order(118,120,124,126,136,142,144,154,159..160,162,172,
                     176,183,185)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:100050"
     Site            order(154,156..157,162,174,185)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:100050"
ORIGIN      
        1 mnlygifgag sygretipil nqqikqecgs dyalvfvddv lagkkvngfe vlstncflka
       61 pylkkyfnva iandkirqrv sesillhgve pitikhpnsv vydhtmigsg aiispfvtis
      121 tnthigrffh aniysyvahd cqigdyvtfa pgakcngyvv iednayigsg avikqgvpnr
      181 pliigagaii gmgavvtksv pagitvcgnp aremkrspts i