ID   NANM_BRUO2              Reviewed;         388 AA.
AC   A5VU94;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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=BOV_A0355;
OS   Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=444178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX   PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA   Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA   de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA   Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA   Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT   "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT   range and tissue tropism.";
RL   PLoS ONE 4:E5519-E5519(2009).
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; CP000709; ABQ62413.1; -; Genomic_DNA.
DR   RefSeq; WP_004688930.1; NC_009504.1.
DR   AlphaFoldDB; A5VU94; -.
DR   SMR; A5VU94; -.
DR   EnsemblBacteria; ABQ62413; ABQ62413; BOV_A0355.
DR   GeneID; 45125762; -.
DR   KEGG; bov:BOV_A0355; -.
DR   HOGENOM; CLU_061535_0_0_5; -.
DR   OMA; PSTNKWR; -.
DR   Proteomes; UP000006383; Chromosome II.
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; IPR019936; Mutatrotase_YjhT-like.
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..26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
FT   CHAIN           27..388
FT                   /note="N-acetylneuraminate epimerase"
FT                   /id="PRO_0000333051"
FT   REPEAT          48..92
FT                   /note="Kelch 1"
FT   REPEAT          94..147
FT                   /note="Kelch 2"
FT   REPEAT          149..186
FT                   /note="Kelch 3"
FT   REPEAT          187..232
FT                   /note="Kelch 4"
FT   REPEAT          236..285
FT                   /note="Kelch 5"
FT   REPEAT          307..356
FT                   /note="Kelch 6"
FT   REPEAT          358..387
FT                   /note="Kelch 7"
FT   ACT_SITE        242
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
SQ   SEQUENCE   388 AA;  40627 MW;  6B1DBC00747DA663 CRC64;
     MFSLIGAKRL AIGIAALAWS TGAVMASEHW PDLPVGIKNG AAARIGNMAY VGLGSAGTDF
     YALDLNNPSK GWVKRANFIG PATNGAAMAA AGGKIFAFSG NGKATPDAKS PIIFDTAYVY
     DPGSDGWSKL DTQTPVGLSG AKAVGLADGR IAIFGGYNKE LFDKYLADVG AIDKDKEPEA
     YRKLVDSYMG MKPEAYRWND EVLVYDPAGN NWGSLGANPF LPNCDPAMAT MGEGDFLLVS
     GEIKPGLRTP EAKLVKIRDG AAHWQKVSDL PPLSGSEPQE GVAGAYAGKA GDDVLVAGGA
     NFKGAQANAA AGKWFAHDGL AKSWRDDVYA FDGKDWKVAG KLPRGLAYGA AFDAPGGLLV
     VGGEDRDGKA RKEVFLLKWD GKALSVEN