NANM_BRUME
ID NANM_BRUME Reviewed; 388 AA.
AC Q8YBP3; Q9XDD2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 102.
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=BMEII0856;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 45-388.
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11598046; DOI=10.1128/iai.69.11.6738-6748.2001;
RA Vizcaino N., Cloeckaert A., Zygmunt M.S., Fernandez-Lago L.;
RT "Characterization of a Brucella species 25-kilobase DNA fragment deleted
RT from Brucella abortus reveals a large gene cluster related to the synthesis
RT of a polysaccharide.";
RL Infect. Immun. 69:6738-6748(2001).
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=AAL54098.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008918; AAL54098.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF076290; AAD43845.1; -; Genomic_DNA.
DR PIR; AG3616; AG3616.
DR RefSeq; WP_004681742.1; NZ_GG703779.1.
DR AlphaFoldDB; Q8YBP3; -.
DR SMR; Q8YBP3; -.
DR STRING; 224914.BMEII0856; -.
DR EnsemblBacteria; AAL54098; AAL54098; BMEII0856.
DR GeneID; 29595352; -.
DR KEGG; bme:BMEII0856; -.
DR PATRIC; fig|224914.52.peg.2507; -.
DR eggNOG; COG3055; Bacteria.
DR PhylomeDB; Q8YBP3; -.
DR Proteomes; UP000000419; 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_0000333050"
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; 40726 MW; 926CBB71CF7D1413 CRC64;
MFSLIRAKRL 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
