ID   A0A2K6D0Z4_MACNE        Unreviewed;       717 AA.
AC   A0A2K6D0Z4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase {ECO:0000313|Ensembl:ENSMNEP00000029584.1};
GN   Name=GNE {ECO:0000313|Ensembl:ENSMNEP00000029584.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000029584.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000029584.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A2K6D0Z4; -.
DR   Ensembl; ENSMNET00000053990.1; ENSMNEP00000029584.1; ENSMNEG00000038236.1.
DR   GeneTree; ENSGT00390000017246; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000038236; Expressed in liver and 12 other cell types or tissues.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:InterPro.
DR   CDD; cd03786; GTB_UDP-GlcNAc_2-Epimerase; 1.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000600; ROK.
DR   InterPro; IPR020004; UDP-GlcNAc_Epase.
DR   InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR   NCBIfam; TIGR03568; NeuC_NnaA; 1.
DR   PANTHER; PTHR18964:SF149; BIFUNCTIONAL UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE_N-ACETYLMANNOSAMINE KINASE; 1.
DR   PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1.
DR   Pfam; PF02350; Epimerase_2; 1.
DR   Pfam; PF00480; ROK; 1.
DR   PRINTS; PR00475; HEXOKINASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120}.
FT   DOMAIN          38..370
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
FT   ACT_SITE        512
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-1"
FT   BINDING         472
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT   BINDING         484
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT   BINDING         512
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT   BINDING         561
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT   BINDING         564
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT   BINDING         564
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT   BINDING         574
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT   BINDING         576
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT   BINDING         581
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT   BINDING         583
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
SQ   SEQUENCE   717 AA;  78613 MW;  1562A90A7C783B6D CRC64;
     MPIGDCSVAA KPREQLLCSL FHTTPGYRAC ALGWKPMVIR RGSHAFKDLI NTYRMIEQDD
     FDINTRLHTI VRGEDEAAMV ESVGLALVKL PDVLNRLKPD IMIVHGDRFD ALALATSAAL
     MNIRILHIEG GEVSGTIDDS IRHAITKLAH YHVCCTRSAE QHLISMCEDH DRILLAGCPS
     YDKLLSAKNK DYMSIIRMWL GDDVKSKDYI VALQHPVTTD IKHSIKMFEL TLDALISFNK
     RTLVLFPNID AGSKEMVRVM RKKGIEHHPN FRAVKHVPFD QFIQLVAHAG CMIGNSSCGV
     REVGAFGTPV INLGTRQIGR ETGENVLHVR DADTQDKILQ ALHLQFGKQY PCSKIYGDGN
     AVPRILKFLK SIDLQEPLQK KFCFPPVKEN ISQDIDHILE TLSALAVDLG GTNLRVAIVS
     MKGEIVKKYT QFNPKTYEER INLILQMCVE AAAEAVKLNC RILGVGISTG GRVNPREGIV
     LHSTKLIQEW NSVDLRTPLS DTLHLPVWVD NDGNCAALAE RKFGQGKGLE NFVTLITGTG
     IGGGIIHQHE LIHGSSFCAA ELGHLVVSLD GPDCSCGSHG CIEAYASGMA LQREAKKLHD
     EDLLLVEGMS VPKDEAVGAL HLIQAAKLGN AKAQSILRTA GTALGLGVVN ILHTMNPSLV
     ILSGVLASHY IHIVKDIIRQ QALSSVQDVD VVVSDLVDPA LLGAASMVLD YTTRRIY
//