ID   SIAA_NEIMB              Reviewed;         377 AA.
AC   H2VFI5;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=UDP-N-acetylglucosamine 2-epimerase;
DE            EC=3.2.1.183;
GN   Name=siaA; Synonyms=synX; OrderedLocusNames=NMB0070;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP   MUTAGENESIS OF ASP-100; GLU-122 AND ASP-131.
RC   STRAIN=MC58;
RX   PubMed=15518580; DOI=10.1021/bi048606d;
RA   Murkin A.S., Chou W.K., Wakarchuk W.W., Tanner M.E.;
RT   "Identification and mechanism of a bacterial hydrolyzing UDP-N-
RT   acetylglucosamine 2-epimerase.";
RL   Biochemistry 43:14290-14298(2004).
CC   -!- FUNCTION: Catalyzes the conversion of UDP-N-acetylglucosamine (UDP-
CC       GlcNAc) to UDP and N-acetyl-D-mannosamine (ManNAc).
CC       {ECO:0000269|PubMed:15518580}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-acetyl-D-
CC         mannosamine + UDP; Xref=Rhea:RHEA:30683, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17122, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:58223; EC=3.2.1.183;
CC         Evidence={ECO:0000269|PubMed:15518580};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.49 mM for UDP-N-acetyl-alpha-D-glucosamine
CC         {ECO:0000269|PubMed:15518580};
CC         Note=kcat is 4.7 sec(-1).;
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:15518580}.
CC   -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; AE002098; AAF40537.1; -; Genomic_DNA.
DR   PIR; A53384; A53384.
DR   PIR; S60758; S60758.
DR   RefSeq; NP_273134.1; NC_003112.2.
DR   RefSeq; WP_002226892.1; NC_003112.2.
DR   AlphaFoldDB; H2VFI5; -.
DR   SMR; H2VFI5; -.
DR   STRING; 122586.NMB0070; -.
DR   PaxDb; H2VFI5; -.
DR   EnsemblBacteria; AAF40537; AAF40537; NMB0070.
DR   GeneID; 61282336; -.
DR   KEGG; nme:NMB0070; -.
DR   PATRIC; fig|122586.8.peg.104; -.
DR   HOGENOM; CLU_061127_0_0_4; -.
DR   OMA; VTYHPVT; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:InterPro.
DR   GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:InterPro.
DR   InterPro; IPR020004; UDP-GlcNAc_Epase.
DR   InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR   InterPro; IPR029767; WecB-like.
DR   PANTHER; PTHR43174; PTHR43174; 1.
DR   Pfam; PF02350; Epimerase_2; 1.
DR   TIGRFAMs; TIGR03568; NeuC_NnaA; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Isomerase; Reference proteome.
FT   CHAIN           1..377
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /id="PRO_0000421996"
FT   ACT_SITE        212
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         100
FT                   /note="D->N: Strongly decreased activity."
FT                   /evidence="ECO:0000269|PubMed:15518580"
FT   MUTAGEN         122
FT                   /note="E->Q: Strongly decreased activity."
FT                   /evidence="ECO:0000269|PubMed:15518580"
FT   MUTAGEN         131
FT                   /note="D->Q: Strongly decreased activity."
FT                   /evidence="ECO:0000269|PubMed:15518580"
SQ   SEQUENCE   377 AA;  42308 MW;  D4289B3FA04EBB2B CRC64;
     MKRILCITGT RADFGKLKPL LAYIENHPDL ELHLIVTGMH MMKTYGRTYK EVTRENYQHT
     YLFSNQIQGE PMGAVLGNTI TFISRLSDEI EPDMVMIHGD RLEALAGAAV GALSSRLVCH
     IEGGELSGTV DDSIRHSISK LSHIHLVANE QAVTRLVQMG EKRKHIHIIG SPDLDVMASS
     TLPSLEEVKE YYGLPYENYG ISMFHPVTTE AHLMPQYAAQ YFKALELSGQ NIISIYPNND
     TGTESILQEL LKYQSDKFIA FPSIRFEYFL VLLKHAKFMV GNSSAGIREA PLYGVPSIDV
     GTRQSNRHMG KSIIHTDYET KNIFDAIQQA CSLGKFEADD TFNGGDTRTS TERFAEVINN
     PETWNVSAQK RFIDLNL