AC MF_01195; DC Protein; auto TR HAMAP; MF_01195; -; 1; level=0 XX Names: NanM XX ID NANM DE RecName: Full=N-acetylneuraminate epimerase; DE EC=5.1.3.24; DE AltName: Full=N-acetylneuraminate mutarotase; DE Short=Neu5Ac mutarotase; DE AltName: Full=Sialic acid epimerase; DE Flags: Precursor; GN Name=nanM; XX CC -!- FUNCTION: Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta- CC anomer, accelerating the equilibrium between the alpha- and beta- CC anomers. Probably facilitates sialidase-negative bacteria to compete CC sucessfully for limited amounts of extracellular Neu5Ac, which is CC likely taken up in the beta-anomer. In addition, the rapid removal of CC sialic acid from solution might be advantageous to the bacterium to CC damp down host responses. CC -!- CATALYTIC ACTIVITY: CC Reaction=N-acetyl-alpha-neuraminate = N-acetyl-beta-neuraminate; CC Xref=Rhea:RHEA:25233, ChEBI:CHEBI:58705, ChEBI:CHEBI:58770; CC EC=5.1.3.24; CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- SIMILARITY: Belongs to the NanM family. XX DR Pfam; PF01344; Kelch_1; 1; trigger=no DR NCBIfam; TIGR03547; Muta_rot_YjhT; 1; trigger=no DR General; Signal; -; 1; trigger=yes XX KW Carbohydrate metabolism KW Isomerase KW Kelch repeat KW Periplasm KW Repeat KW Signal XX GO GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives GO GO:0042597; C:periplasmic space XX FT From: NANM_ECOLI (P39371) FT REPEAT 40..84 FT /note="Kelch 1" FT REPEAT 86..137 FT /note="Kelch 2" FT REPEAT 139..173 FT /note="Kelch 3" FT REPEAT 174..219 FT /note="Kelch 4" FT REPEAT 222..265 FT /note="Kelch 5" FT REPEAT 287..336 FT /note="Kelch 6" FT REPEAT 338..367 FT /note="Kelch 7" FT ACT_SITE 228 FT /note="Proton acceptor" FT Condition: E XX Size: 368-392; Related: None; Template: P39371; Scope: Bacteria; Pseudomonadota Fusion: Nter: None Cter: None Duplicate: in ECOL6 Plasmid: None Comments: None XX # Revision 1.17 2023/06/01 //