ID   NANM_YERPS              Reviewed;         392 AA.
AC   Q66BP2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
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}; OrderedLocusNames=YPTB1729;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH20968.1; -; Genomic_DNA.
DR   RefSeq; WP_002211169.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66BP2; -.
DR   SMR; Q66BP2; -.
DR   EnsemblBacteria; CAH20968; CAH20968; YPTB1729.
DR   GeneID; 66841836; -.
DR   KEGG; ypo:BZ17_771; -.
DR   KEGG; yps:YPTB1729; -.
DR   PATRIC; fig|273123.14.peg.816; -.
DR   OMA; PSTNKWR; -.
DR   Proteomes; UP000001011; Chromosome.
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; -; 1.
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..35
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
FT   CHAIN           36..392
FT                   /note="N-acetylneuraminate epimerase"
FT                   /id="PRO_5000098674"
FT   REPEAT          56..100
FT                   /note="Kelch 1"
FT   REPEAT          102..155
FT                   /note="Kelch 2"
FT   REPEAT          157..192
FT                   /note="Kelch 3"
FT   REPEAT          193..238
FT                   /note="Kelch 4"
FT   REPEAT          241..290
FT                   /note="Kelch 5"
FT   REPEAT          312..361
FT                   /note="Kelch 6"
FT   REPEAT          363..392
FT                   /note="Kelch 7"
FT   ACT_SITE        247
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
SQ   SEQUENCE   392 AA;  42294 MW;  9A3643D1520C8540 CRC64;
     MTQLYPQYKK QLTTKIVLFS ALSLLMMASL PNTYAEQYPD VPVPFKNGTG GKVENSLYVG
     LGSAGVSWFR LDTDKTGAGW QKVANFPGQP REQAVTVVLA GKLYVFGGVG KTNANDTQVR
     ALDDAYRFDP QTNQWQQLAT RAPRGLVGTV ATTLDGSQAV LLGGVNKAIF DGYFTDLASA
     GSDEVRKSAV INAYFNQAPA DYFYNRDVLI YDPQKNQWKS GGLLPFLGTA GSAISRMDNR
     LILINGEIKP GLRTAAVWQG LMQGNVLEWQ PQPDLIGAET GSAQEGLAGA FSGISHKTVL
     VAGGANFPGA WKQFNRGHLY AHQGLEKQWH QQVYALVDNQ WRIAGKLPQP LGYGVSIQGP
     DKVILIGGET TGGTATSAVT QLSWQGGKLH IE