ID A0A3Q3A578_CHICK Unreviewed; 685 AA.
AC A0A3Q3A578;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase {ECO:0000313|Ensembl:ENSGALP00010018601.1};
GN Name=GNE {ECO:0000313|Ensembl:ENSGALP00010018601.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00010018601.1, ECO:0000313|Proteomes:UP000000539};
RN [1] {ECO:0000313|Ensembl:ENSGALP00010018601.1}
RP IDENTIFICATION.
RC STRAIN=broiler {ECO:0000313|Ensembl:ENSGALP00010018601.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_015135910.1; XM_015280424.1.
DR AlphaFoldDB; A0A3Q3A578; -.
DR Ensembl; ENSGALT00010031777.1; ENSGALP00010018601.1; ENSGALG00010013225.1.
DR GeneID; 427285; -.
DR CTD; 10020; -.
DR VEuPathDB; HostDB:geneid_427285; -.
DR GeneTree; ENSGT00390000017246; -.
DR Proteomes; UP000000539; Chromosome Z.
DR Bgee; ENSGALG00000015331; Expressed in colon and 12 other cell types or tissues.
DR ExpressionAtlas; A0A3Q3A578; baseline and differential.
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 1: Evidence at protein level;
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A3Q3A578};
KW Reference proteome {ECO:0000313|Proteomes:UP000000539}.
FT DOMAIN 21..338
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
FT ACT_SITE 480
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-1"
FT BINDING 440
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 452
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 480
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 529
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 532
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 532
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 542
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 544
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 549
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 551
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
SQ SEQUENCE 685 AA; 75003 MW; 699F7B81D99EEBA5 CRC64;
MECLVPDPFL CKNFLYPSNT YRMIEQDDFD IHTRLHTIVR GEDEAAMVES VGLALVKLPD
VLNRLKPDIM IVHGDRFDAL ALATSAALMN IRILHIEGGE VSGTIDDSIR HAITKLAHYH
VCCTRSAEQH LIAMCEDHDR ILLAGCPSYD KLLSAKNKDY MSVIRMWLGE DVKPRDYIVA
LQHPVTTDIK HSIKMFELTL DALISFNKRT LVLFPNVDAG SKEMVRVMRK KGIEHHPNFR
AVKHVPFDQF IQLVAHAGCM IGNSSCGVRE VGAFGTPVIN LGTRQTGRET GENVLHVRDA
DTQDKILHAL QLQFGKQYPC SKIYGDGNAV PRILKFLKSI DLKEPLQKKF CFPPVKDNIS
QDIDHILETQ SALAVDLGGT NLRVAIVSMK GEIVKKYTQL NPKTYEDRLG LILKMCVEAA
SEAVNLNCRI LGVGISTGGR VNPREGIVLH STKLIQEWSS VDLRTPISDA LHLPVWVDND
GNCAALAERK FGHGKGIENF VTLITGTGIG GGIIHQHELI HGSSFCAAEL GHIVVSLDGP
ECLCGSQGCI EAYASGIALQ REAKKLHDED LLLVEGMSMK NEEVVSAAHL IQAAKLGNAK
AESILRTAGT ALGLGVVNIL HTMNPSLVIL SGVLASHYVN AVKDVIHRQA LSSVKTVDVV
VSNLADPALL GAASLVLDYT TRRIY
//
