ID I6C7G1_SHIFL Unreviewed; 368 AA.
AC I6C7G1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=N-acetylneuraminate epimerase {ECO:0000256|HAMAP-Rule:MF_01195};
DE EC=5.1.3.24 {ECO:0000256|HAMAP-Rule:MF_01195};
DE AltName: Full=N-acetylneuraminate mutarotase {ECO:0000256|HAMAP-Rule:MF_01195};
DE Short=Neu5Ac mutarotase {ECO:0000256|HAMAP-Rule:MF_01195};
DE AltName: Full=Sialic acid epimerase {ECO:0000256|HAMAP-Rule:MF_01195};
DE Flags: Precursor;
GN Name=nanM {ECO:0000256|HAMAP-Rule:MF_01195,
GN ECO:0000313|EMBL:EIQ15453.1};
GN ORFNames=SFK315_5054 {ECO:0000313|EMBL:EIQ15453.1};
OS Shigella flexneri K-315.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=766150 {ECO:0000313|EMBL:EIQ15453.1, ECO:0000313|Proteomes:UP000005407};
RN [1] {ECO:0000313|EMBL:EIQ15453.1, ECO:0000313|Proteomes:UP000005407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K-315 {ECO:0000313|EMBL:EIQ15453.1,
RC ECO:0000313|Proteomes:UP000005407};
RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., Jones K.,
RA Santana-Cruz I., Liu X.;
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01195};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01195}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_01195}.
CC -!- SIMILARITY: Belongs to the NanM family. {ECO:0000256|HAMAP-
CC Rule:MF_01195}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIQ15453.1}.
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DR EMBL; AKMY01000077; EIQ15453.1; -; Genomic_DNA.
DR AlphaFoldDB; I6C7G1; -.
DR PATRIC; fig|766150.3.peg.4871; -.
DR Proteomes; UP000005407; Unassembled WGS sequence.
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; PTHR24412; KELCH PROTEIN; 1.
DR PANTHER; PTHR24412:SF272; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01195};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01195};
KW Kelch repeat {ECO:0000256|HAMAP-Rule:MF_01195};
KW Periplasm {ECO:0000256|HAMAP-Rule:MF_01195};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_01195};
KW Signal {ECO:0000256|HAMAP-Rule:MF_01195}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01195"
FT CHAIN 20..368
FT /note="N-acetylneuraminate epimerase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01195"
FT /id="PRO_5009014783"
FT REPEAT 40..84
FT /note="Kelch 1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01195"
FT REPEAT 86..137
FT /note="Kelch 2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01195"
FT REPEAT 139..173
FT /note="Kelch 3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01195"
FT REPEAT 174..219
FT /note="Kelch 4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01195"
FT REPEAT 222..265
FT /note="Kelch 5"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01195"
FT REPEAT 287..336
FT /note="Kelch 6"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01195"
FT REPEAT 338..367
FT /note="Kelch 7"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01195"
FT ACT_SITE 228
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01195"
SQ SEQUENCE 368 AA; 39749 MW; AD8AD5E5A1570C5D CRC64;
MNKTITVLAI MMASFAANAS VLPETPVPFK SGTGAIDNDT VYIGLGSAGT AWYKLDTQAK
DKKWTALAAF PGGPRDQATS AFIDGNLYVF GGIGKNREGL TQVFNDVHKY NPKTNSWVKL
MSHAPMGMAG HVTFVHNGKA YVTGGVNQNI FNGYFEDLNE AGKDSTAVDK INVYYFDKKA
EDYFFNKFLL SFDPSTQQWS YAGESPWYGM AGAAVVNKGD KTWLINGEAK PGLRTDAVFE
LDFTGNNLKW NKLAPVSSPD GVAGGFAGIS NDSLIFAGGA GFKGSRENYQ HGKNYAHEGL
KKSYSTDIHL WHNGKWDKSG ELSQGRAYGV SLPWNNSLLI IGGETAGGKA VTDSVLISVK
DNKVTVQN
//