GenomeNet

Database: UniProt
Entry: I6C7G1_SHIFL
LinkDB: I6C7G1_SHIFL
Original site: I6C7G1_SHIFL 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system