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Database: UniProt
Entry: A1UCI6_MYCSK
LinkDB: A1UCI6_MYCSK
Original site: A1UCI6_MYCSK 
ID   A1UCI6_MYCSK            Unreviewed;       387 AA.
AC   A1UCI6;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=UDP-N-acetylglucosamine 2-epimerase (non-hydrolyzing) {ECO:0000256|ARBA:ARBA00038858};
DE            EC=5.1.3.14 {ECO:0000256|ARBA:ARBA00038858};
GN   OrderedLocusNames=Mkms_1332 {ECO:0000313|EMBL:ABL90544.1};
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL90544.1};
RN   [1] {ECO:0000313|EMBL:ABL90544.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL90544.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-
CC         mannosamine; Xref=Rhea:RHEA:17213, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:68623; EC=5.1.3.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00036080};
CC   -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.
CC       {ECO:0000256|ARBA:ARBA00038209, ECO:0000256|RuleBase:RU003513}.
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DR   EMBL; CP000518; ABL90544.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1UCI6; -.
DR   STRING; 189918.Mkms_1332; -.
DR   KEGG; mkm:Mkms_1332; -.
DR   HOGENOM; CLU_041674_1_0_11; -.
DR   OrthoDB; 9803238at2; -.
DR   GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-EC.
DR   CDD; cd03786; GTB_UDP-GlcNAc_2-Epimerase; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR   InterPro; IPR029767; WecB-like.
DR   NCBIfam; TIGR00236; wecB; 1.
DR   PANTHER; PTHR43174; UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE; 1.
DR   PANTHER; PTHR43174:SF2; UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE; 1.
DR   Pfam; PF02350; Epimerase_2; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU003513}.
FT   DOMAIN          29..371
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
SQ   SEQUENCE   387 AA;  40790 MW;  7E7B6D8EE2088882 CRC64;
     MGGVTEVHLV AGTRPEAIKL APLVPALRAQ GMTPVFVASG QHPTMVHQAL DAFGLEPDVT
     LSIDRGSGSQ AELMAALTMK LEKHWQQRTP AAVVVQGDTT TVLAAAMVAF WAKLPIAHLE
     AGLRSHDLAA PFPEEGNRKL VGQISRLHLA PTARARANLE REGTPSADIV VTGNTVIDAV
     LGIAARGGPV TDSRVAAFVE RARAGASRLV LVTAHRRESW GEPLDRVLNA VALLLEKYSD
     VEVVLPAHPN PAVAEQVRAV LGAHPRVLVT EPLAYPVLVG ALAASTLVLS DSGGIQEEAP
     SFGVPVIVLR EVTERMEAVD AGCAILVGTD RDAVLGNACR LLDDPDERTA MVSKGNPFGD
     GRAAERSAAA IAWMLGRTDG RPAEFRF
//
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