MULTISPECIES: N-acetylmannosamine-6-phosphate 2-epimerase

LOCUS       WP_002918463             234 aa            linear   BCT 06-NOV-2024
            [Klebsiella].
ACCESSION   WP_002918463
VERSION     WP_002918463.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 234)
  AUTHORS   Arif,T., Currie,M.J., Dobson,R.C.J., Newson,H.L., Poonthiyil,V.,
            Fairbanks,A.J., North,R.A. and Rendle,P.M.
  TITLE     Synthesis of N-acetylmannosamine-6-phosphate derivatives to
            investigate the mechanism of N-acetylmannosamine-6-phosphate
            2-epimerase
  JOURNAL   Carbohydr Res 510, 108445 (2021)
   PUBMED   34607125
REFERENCE   2  (residues 1 to 234)
  AUTHORS   Currie,M.J., Manjunath,L., Horne,C.R., Rendle,P.M., Subramanian,R.,
            Friemann,R., Fairbanks,A.J., Muscroft-Taylor,A.C., North,R.A. and
            Dobson,R.C.J.
  TITLE     N-acetylmannosamine-6-phosphate 2-epimerase uses a novel
            substrate-assisted mechanism to catalyze amino sugar epimerization
  JOURNAL   J Biol Chem 297 (4), 101113 (2021)
   PUBMED   34437902
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.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10011628
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..234
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..234
                     /product="N-acetylmannosamine-6-phosphate 2-epimerase"
                     /EC_number="5.1.3.9"
                     /GO_function="GO:0047465 - N-acylglucosamine-6-phosphate
                     2-epimerase activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /GO_process="GO:0006051 - N-acetylmannosamine metabolic
                     process [Evidence IEA]"
                     /GO_process="GO:0019262 - N-acetylneuraminate catabolic
                     process [Evidence IEA]"
                     /calculated_mol_wt=24356
     Region          14..226
                     /region_name="PRK01130"
                     /note="putative N-acetylmannosamine-6-phosphate
                     2-epimerase"
                     /db_xref="CDD:234907"
     Site            order(20,22,51,72,74,105,132,153,157,184..186,207)
                     /site_type="active"
                     /note="putative active site cavity [active]"
                     /db_xref="CDD:240080"
ORIGIN      
        1 msllaqldqr irhhgglivs cqpvpgspld npaivaamal aaeqagaval rieglanlqa
       61 vrplvtvpvi glikrdlpds pvritpwled idalaqggad iiaidgtqrq rpasvsalla
      121 eihqlgkvam adcsslddal ecwqlgaeiv gttlsgytae etpdepdlal vqclsaagcr
      181 viaegryntp aqaaeamrcg awavtvgsai trlehicgwy ntalkaavcp aneq