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Database: UniProt
Entry: A0A0K1R953_9CORY
LinkDB: A0A0K1R953_9CORY
Original site: A0A0K1R953_9CORY 
ID   A0A0K1R953_9CORY        Unreviewed;       387 AA.
AC   A0A0K1R953;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
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   ORFNames=AK829_00840 {ECO:0000313|EMBL:AKV57960.1};
OS   Corynebacterium riegelii.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=156976 {ECO:0000313|EMBL:AKV57960.1, ECO:0000313|Proteomes:UP000060016};
RN   [1] {ECO:0000313|EMBL:AKV57960.1, ECO:0000313|Proteomes:UP000060016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PUDD_83A45 {ECO:0000313|EMBL:AKV57960.1,
RC   ECO:0000313|Proteomes:UP000060016};
RA   Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA   Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M., Henderson B.A.,
RA   Jones I.B., McGettigan J.A., Micheletti S.J., Nasrallah M.E., Ortiz D.,
RA   Piller C.R., Privatt S.R., Schneider S.L., Sharp S., Smith T.C.,
RA   Stanton J.D., Ullery H.E., Wilson R.J., Serrano M.G., Buck G., Lee V.,
RA   Wang Y., Carvalho R., Voegtly L., Shi R., Duckworth R., Johnson A.,
RA   Loviza R., Walstead R., Shah Z., Kiflezghi M., Wade K., Ball S.L.,
RA   Bradley K.W., Asai D.J., Bowman C.A., Russell D.A., Pope W.H.,
RA   Jacobs-Sera D., Hendrix R.W., Hatfull G.F.;
RL   Submitted (AUG-2015) 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; CP012342; AKV57960.1; -; Genomic_DNA.
DR   RefSeq; WP_052203436.1; NZ_CP012342.1.
DR   AlphaFoldDB; A0A0K1R953; -.
DR   STRING; 156976.AK829_00840; -.
DR   PATRIC; fig|156976.3.peg.160; -.
DR   Proteomes; UP000060016; Chromosome.
DR   GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:InterPro.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000060016}.
FT   DOMAIN          26..367
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
SQ   SEQUENCE   387 AA;  42335 MW;  F405C59B6049461D CRC64;
     MSVKPKIMTV YGTRPEAIKV APVVSALQND DRFDSVVVST GQHKEMLEQV NKRFGITPDH
     DMALMKPGQT LNELVSRAIQ GLDPIIEAEK PDVIISQGDT STAMVAALAG FHRGVKIVHL
     EAGLRTGNIF SPFPEEANRK IIGQVASLHL APTSESRENL RRENFRSKDI VVTGNTVIDA
     LLAASEWDVE FDDSRLEELR NSDEKLVLVT THRRENLDAM KEIGGAVQDL AKSYPDHIFA
     LPLHLNPKVR DAVLPEVENL PNVIITDPLP YDQFTALMSR AYLVLTDSGG VQEEAPSLGK
     PVLVMRENTE RPEAVVAGTV KLVGTDRNRI VAEARNLLDQ DAAYEAMANA VNPYGDGQAA
     ERAVAAIAEL VGVGERIDEF EPEIVSK
//
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