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Database: UniProt
Entry: A0A2I3TKD1_PANTR
LinkDB: A0A2I3TKD1_PANTR
Original site: A0A2I3TKD1_PANTR 
ID   A0A2I3TKD1_PANTR        Unreviewed;       717 AA.
AC   A0A2I3TKD1; A0A2J8QRP2;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase {ECO:0000313|Ensembl:ENSPTRP00000089687.1};
GN   Name=GNE {ECO:0000313|Ensembl:ENSPTRP00000089687.1,
GN   ECO:0000313|VGNC:VGNC:8890};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000089687.1, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000089687.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000089687.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AACZ04033385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003312123.1; XM_003312075.3.
DR   AlphaFoldDB; A0A2I3TKD1; -.
DR   Ensembl; ENSPTRT00000108279.1; ENSPTRP00000089687.1; ENSPTRG00000020931.6.
DR   VGNC; VGNC:8890; GNE.
DR   GeneTree; ENSGT00390000017246; -.
DR   OrthoDB; 5489121at2759; -.
DR   Proteomes; UP000002277; Chromosome 9.
DR   Bgee; ENSPTRG00000020931; Expressed in liver and 21 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:UP000002277}.
FT   DOMAIN          35..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;  78579 MW;  6CCF484FC092DAF4 CRC64;
     MPIGDCSVAA KPRKQLLCSL FQTTLGYRAC ASGWKPMVIR 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 IHIVKDVIRQ QALSSVQDVD VVVSDLVDPA LLGAASMVLD YTTRRIY
//
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