ID   NANM_HAEIE              Reviewed;         375 AA.
AC   A5UB03;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=N-acetylneuraminate epimerase {ECO:0000255|HAMAP-Rule:MF_01195};
DE            EC=5.1.3.24 {ECO:0000255|HAMAP-Rule:MF_01195};
DE   AltName: Full=N-acetylneuraminate mutarotase {ECO:0000255|HAMAP-Rule:MF_01195};
DE            Short=Neu5Ac mutarotase {ECO:0000255|HAMAP-Rule:MF_01195};
DE   AltName: Full=Sialic acid epimerase {ECO:0000255|HAMAP-Rule:MF_01195};
DE   Flags: Precursor;
GN   Name=nanM {ECO:0000255|HAMAP-Rule:MF_01195};
GN   OrderedLocusNames=CGSHiEE_02545;
OS   Haemophilus influenzae (strain PittEE).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374930;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittEE;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
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. {ECO:0000255|HAMAP-Rule:MF_01195}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_01195};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01195}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01195}.
CC   -!- SIMILARITY: Belongs to the NanM family. {ECO:0000255|HAMAP-
CC       Rule:MF_01195}.
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DR   EMBL; CP000671; ABQ97954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5UB03; -.
DR   SMR; A5UB03; -.
DR   KEGG; hip:CGSHiEE_02545; -.
DR   HOGENOM; CLU_061535_0_0_6; -.
DR   OMA; PSTNKWR; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.80; -; 2.
DR   HAMAP; MF_01195; NanM; 1.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR019936; Mutatrotase_YjhT-like.
DR   Pfam; PF01344; Kelch_1; 1.
DR   SUPFAM; SSF117281; SSF117281; 1.
DR   TIGRFAMs; TIGR03547; muta_rot_YjhT; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Isomerase; Kelch repeat; Periplasm; Repeat;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
FT   CHAIN           23..375
FT                   /note="N-acetylneuraminate epimerase"
FT                   /id="PRO_0000333062"
FT   REPEAT          43..87
FT                   /note="Kelch 1"
FT   REPEAT          89..140
FT                   /note="Kelch 2"
FT   REPEAT          142..176
FT                   /note="Kelch 3"
FT   REPEAT          177..222
FT                   /note="Kelch 4"
FT   REPEAT          225..273
FT                   /note="Kelch 5"
FT   REPEAT          295..344
FT                   /note="Kelch 6"
FT   REPEAT          346..375
FT                   /note="Kelch 7"
FT   ACT_SITE        231
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
SQ   SEQUENCE   375 AA;  40358 MW;  2C7B0262FFECF513 CRC64;
     MKLTKTALCT ALFATFTFSA NAQTYPDLPV GIKGGTGALI GDTVYVGLGS GGDKFYTLDL
     KDPSAQWKEI ATFPGGERNQ PVAAAVDGKL YVFGGLQKNE KGELQLVNDA YRYNPSDNTW
     MKLPTRSPRG LVGSSGASHG DKVYILGGSN LSIFNGFFQD NVAAGEDQAK KDEIAAAYFD
     QRPEDYFFTT ELLSYEPSTN KWRNEGRIPF SGRAGAAFTI QGNDLVVVNG EIKPGLRTAE
     THQGKFTAKG VQWKNLPDLP APKGKSQDGL AGALSGYSNG HYLVTGGANF PGSIKQYKEG
     KLHAHKGLSK AWHNEVYTLN NGKWRIVGEL PMNIGYGFSV SYNNKVLLIG GETDGGKALT
     SVKAISYDGK KLTIE