ID NANM_SHIFL Reviewed; 368 AA.
AC Q83IN1; Q7UAQ6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 3.
DT 27-MAR-2024, entry version 122.
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=SF4212, S4469;
OS Shigella flexneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN45632.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP19418.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN45632.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP19418.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_709925.2; NC_004337.2.
DR RefSeq; WP_005048917.1; NZ_WPGW01000210.1.
DR AlphaFoldDB; Q83IN1; -.
DR SMR; Q83IN1; -.
DR STRING; 198214.SF4212; -.
DR PaxDb; 198214-SF4212; -.
DR GeneID; 1025399; -.
DR KEGG; sfl:SF4212; -.
DR KEGG; sfx:S4469; -.
DR PATRIC; fig|198214.7.peg.4968; -.
DR HOGENOM; CLU_061535_0_0_6; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Kelch-type beta propeller; 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 NCBIfam; TIGR03547; muta_rot_YjhT; 1.
DR PANTHER; PTHR23244; KELCH REPEAT DOMAIN; 1.
DR PANTHER; PTHR23244:SF471; KELCH REPEAT-CONTAINING PROTEIN 1-RELATED; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Isomerase; Kelch repeat; Periplasm;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
FT CHAIN 20..368
FT /note="N-acetylneuraminate epimerase"
FT /id="PRO_0000333070"
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 /evidence="ECO:0000255|HAMAP-Rule:MF_01195"
SQ SEQUENCE 368 AA; 39646 MW; 1E663ED153E90DAF CRC64;
MNKTIMALAI MMASFAANAS VLPETPVPFK SGTGAIDNDT VYIGLGSAGT AWYKLDTQAK
DKKWTALAAF PGGPREQATS AFIDGNLYVF GGIGKNSEGL TQVFNDVHKY NPKTNSWVKL
MSHAPMGMAG HVTFVHNGKA YVTGGVNQNI FNGYFEDLNE AGKDSTAIDK INAHYFDKKA
EDYFFNKFLL SFDPSTQQWS YAGESPWYGT AGAAVVNKGD KTWLINGEAK PGLRTDAVFE
LDFTGNNLKW NKLDPVSSPD GVAGGFAGIS NDSLIFAGGA GFKGSRENYQ NGKNYAHEGL
KKSYSTDIHL WHNGKWDKSG ELSQGRAYGV SLPWNNSLLI IGGETAGGKA VTDSVLISVK
DNKVTVQN
//
