NANM_HAEIN
ID NANM_HAEIN Reviewed; 375 AA.
AC P44544;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=N-acetylneuraminate epimerase;
DE EC=5.1.3.24;
DE AltName: Full=N-acetylneuraminate mutarotase;
DE Short=Neu5Ac mutarotase;
DE AltName: Full=Sialic acid epimerase;
DE Flags: Precursor;
GN Name=nanM; OrderedLocusNames=HI_0148;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP PROTEIN SEQUENCE OF 23-32, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INVOLVEMENT IN SIALIC ACID
RP CATABOLISM.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=15121896; DOI=10.1093/nar/gkh555;
RA Kolker E., Makarova K.S., Shabalina S., Picone A.F., Purvine S.,
RA Holzman T., Cherny T., Armbruster D., Munson R.S. Jr., Kolesov G.,
RA Frishman D., Galperin M.Y.;
RT "Identification and functional analysis of 'hypothetical' genes expressed
RT in Haemophilus influenzae.";
RL Nucleic Acids Res. 32:2353-2361(2004).
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 (By similarity). {ECO:0000250}.
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;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10675023}.
CC -!- SIMILARITY: Belongs to the NanM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC21820.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L42023; AAC21820.1; ALT_INIT; Genomic_DNA.
DR PIR; A64144; A64144.
DR RefSeq; NP_438317.1; NC_000907.1.
DR RefSeq; WP_032828455.1; NC_000907.1.
DR AlphaFoldDB; P44544; -.
DR SMR; P44544; -.
DR STRING; 71421.HI_0148; -.
DR EnsemblBacteria; AAC21820; AAC21820; HI_0148.
DR KEGG; hin:HI_0148; -.
DR PATRIC; fig|71421.8.peg.150; -.
DR eggNOG; COG3055; Bacteria.
DR HOGENOM; CLU_061535_0_0_6; -.
DR Proteomes; UP000000579; 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; -; 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 Pfam; PF01344; Kelch_1; 1.
DR SUPFAM; SSF117281; SSF117281; 1.
DR TIGRFAMs; TIGR03547; muta_rot_YjhT; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Direct protein sequencing; Isomerase;
KW Kelch repeat; Periplasm; Reference proteome; Repeat; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:10675023"
FT CHAIN 23..375
FT /note="N-acetylneuraminate epimerase"
FT /id="PRO_0000016656"
FT REPEAT 43..87
FT /note="Kelch 1"
FT REPEAT 89..140
FT /note="Kelch 2"
FT REPEAT 142..176
FT /note="Kelch 3"
FT REPEAT 177..222
FT /note="Kelch 4"
FT REPEAT 225..273
FT /note="Kelch 5"
FT REPEAT 295..344
FT /note="Kelch 6"
FT REPEAT 346..375
FT /note="Kelch 7"
SQ SEQUENCE 375 AA; 40343 MW; 05EC99114EAC27BE CRC64;
MKLTKTALCT ALFATFTFSA NAQTYPDLPV GIKGGTGALI GDTVYVGLGS GGDKFYTLDL
KDPSAQWKEI ATFPGGERNQ PVAAAVDGKL YVFGGLQKNE KGELQLVNDA YRYNPSDNTW
MKLPTRSPRG LVGSSGASHG DKVYILGGSN LSIFNGFFQD TVAAGEDKAK KDEIAAAYFD
QRPEDYFFTT ELLSYEPSTN KWRNEGRIPF SGRAGAAFTI QGNELVVVNG EIKPGLRTAE
THQGKFTAKG VQWKNLPDLP APKGKSQDGL AGALSGYSNG HYLVTGGANF PGSIKQFKEG
KLHAHKGLSK AWHNEVYTLN NGKWRIVGEL PMNIGYGFSV SYNNKVLLIG GETDGGKALT
SVKAISYDGK KLTIE
