ID NANM_ECOLI Reviewed; 368 AA.
AC P39371; Q2M603;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 27-MAR-2024, entry version 154.
DE RecName: Full=N-acetylneuraminate epimerase;
DE EC=5.1.3.24 {ECO:0000269|PubMed:33895133};
DE AltName: Full=N-acetylneuraminate anomerase NanM {ECO:0000303|PubMed:33895133};
DE AltName: Full=N-acetylneuraminate mutarotase;
DE Short=Neu5Ac mutarotase;
DE AltName: Full=Sialic acid epimerase;
DE Flags: Precursor;
GN Name=nanM; Synonyms=yjhT; OrderedLocusNames=b4310, JW5777;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP INDUCTION BY SIALIC ACID.
RX PubMed=15743943; DOI=10.1128/jb.187.6.1959-1965.2005;
RA Condemine G., Berrier C., Plumbridge J., Ghazi A.;
RT "Function and expression of an N-acetylneuraminic acid-inducible outer
RT membrane channel in Escherichia coli.";
RL J. Bacteriol. 187:1959-1965(2005).
RN [5]
RP INDUCTION.
RX PubMed=23935044; DOI=10.1128/jb.00692-13;
RA Kalivoda K.A., Steenbergen S.M., Vimr E.R.;
RT "Control of the Escherichia coli sialoregulon by transcriptional repressor
RT NanR.";
RL J. Bacteriol. 195:4689-4701(2013).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RC STRAIN=K12;
RX PubMed=33895133; DOI=10.1016/j.jbc.2021.100699;
RA Kentache T., Thabault L., Deumer G., Haufroid V., Frederick R.,
RA Linster C.L., Peracchi A., Veiga-da-Cunha M., Bommer G.T.,
RA Van Schaftingen E.;
RT "The metalloprotein YhcH is an anomerase providing N-acetylneuraminate
RT aldolase with the open form of its substrate.";
RL J. Biol. Chem. 296:100699-100699(2021).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), NMR, MASS SPECTROMETRY, FUNCTION,
RP SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF LYS-30; GLU-228; ARG-234;
RP HIS-297; LYS-302; TYR-328 AND GLU-344.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=18063573; DOI=10.1074/jbc.m707822200;
RA Severi E., Mueller A., Potts J.R., Leech A., Williamson D., Wilson K.S.,
RA Thomas G.H.;
RT "Sialic acid mutarotation is catalyzed by the Escherichia coli beta-
RT propeller protein YjhT.";
RL J. Biol. Chem. 283:4841-4849(2008).
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 (PubMed:18063573). Forms linear aceneuramate
CC during interconversion of Neu5Ac anomers (PubMed:33895133).
CC {ECO:0000269|PubMed:18063573, ECO:0000269|PubMed:33895133}.
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:0000269|PubMed:33895133};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25234;
CC Evidence={ECO:0000269|PubMed:33895133};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25235;
CC Evidence={ECO:0000269|PubMed:33895133};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18063573}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:18063573}.
CC -!- INDUCTION: Induced by N-acetylneuraminate and modulated by N-
CC acetylglucosamine, via the NanR and NagC regulators.
CC {ECO:0000269|PubMed:15743943, ECO:0000269|PubMed:23935044}.
CC -!- MASS SPECTROMETRY: Mass=38685; Mass_error=4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:18063573};
CC -!- SIMILARITY: Belongs to the NanM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97206.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97206.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77266.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78303.1; -; Genomic_DNA.
DR PIR; S56535; S56535.
DR RefSeq; NP_418730.4; NC_000913.3.
DR RefSeq; WP_001309184.1; NZ_SSUV01000012.1.
DR PDB; 2UVK; X-ray; 1.50 A; A/B=20-368.
DR PDBsum; 2UVK; -.
DR AlphaFoldDB; P39371; -.
DR SMR; P39371; -.
DR BioGRID; 4259377; 10.
DR DIP; DIP-12628N; -.
DR IntAct; P39371; 6.
DR STRING; 511145.b4310; -.
DR jPOST; P39371; -.
DR PaxDb; 511145-b4310; -.
DR EnsemblBacteria; AAC77266; AAC77266; b4310.
DR GeneID; 949106; -.
DR KEGG; ecj:JW5777; -.
DR KEGG; eco:b4310; -.
DR PATRIC; fig|1411691.4.peg.2383; -.
DR EchoBASE; EB2450; -.
DR eggNOG; COG3055; Bacteria.
DR HOGENOM; CLU_061535_0_0_6; -.
DR InParanoid; P39371; -.
DR OMA; FNGFFQD; -.
DR OrthoDB; 198899at2; -.
DR PhylomeDB; P39371; -.
DR BioCyc; EcoCyc:G7920-MONOMER; -.
DR BioCyc; MetaCyc:G7920-MONOMER; -.
DR BRENDA; 5.1.3.24; 2026.
DR EvolutionaryTrace; P39371; -.
DR PRO; PR:P39371; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IDA:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IMP:EcoCyc.
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; 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; PF13418; Kelch_4; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Isomerase; Kelch repeat; Periplasm;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..19
FT CHAIN 20..368
FT /note="N-acetylneuraminate epimerase"
FT /id="PRO_0000016655"
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"
FT MUTAGEN 30
FT /note="K->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:18063573"
FT MUTAGEN 228
FT /note="E->A: Great decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:18063573"
FT MUTAGEN 234
FT /note="R->A: Decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:18063573"
FT MUTAGEN 297
FT /note="H->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:18063573"
FT MUTAGEN 302
FT /note="K->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:18063573"
FT MUTAGEN 328
FT /note="Y->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:18063573"
FT MUTAGEN 344
FT /note="E->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:18063573"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:2UVK"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:2UVK"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:2UVK"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:2UVK"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:2UVK"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:2UVK"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:2UVK"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 266..270
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:2UVK"
FT HELIX 285..290
FT /evidence="ECO:0007829|PDB:2UVK"
FT TURN 296..299
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 337..344
FT /evidence="ECO:0007829|PDB:2UVK"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 350..358
FT /evidence="ECO:0007829|PDB:2UVK"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:2UVK"
SQ SEQUENCE 368 AA; 39572 MW; 1194F392C51EA204 CRC64;
MNKTITALAI MMASFAANAS VLPETPVPFK SGTGAIDNDT VYIGLGSAGT AWYKLDTQAK
DKKWTALAAF PGGPRDQATS AFIDGNLYVF GGIGKNSEGL TQVFNDVHKY NPKTNSWVKL
MSHAPMGMAG HVTFVHNGKA YVTGGVNQNI FNGYFEDLNE AGKDSTAIDK INAHYFDKKA
EDYFFNKFLL SFDPSTQQWS YAGESPWYGT AGAAVVNKGD KTWLINGEAK PGLRTDAVFE
LDFTGNNLKW NKLAPVSSPD GVAGGFAGIS NDSLIFAGGA GFKGSRENYQ NGKNYAHEGL
KKSYSTDIHL WHNGKWDKSG ELSQGRAYGV SLPWNNSLLI IGGETAGGKA VTDSVLITVK
DNKVTVQN
//
