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Database: UniProt
Entry: A0A3Q7SXW6_VULVU
LinkDB: A0A3Q7SXW6_VULVU
Original site: A0A3Q7SXW6_VULVU 
ID   A0A3Q7SXW6_VULVU        Unreviewed;       722 AA.
AC   A0A3Q7SXW6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase {ECO:0000313|RefSeq:XP_025868949.1};
GN   Name=GNE {ECO:0000313|RefSeq:XP_025868949.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025868949.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025868949.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025868949.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025868949.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_025868949.1; XM_026013164.1.
DR   AlphaFoldDB; A0A3Q7SXW6; -.
DR   STRING; 9627.ENSVVUP00000027308; -.
DR   Ensembl; ENSVVUT00000036323; ENSVVUP00000027308; ENSVVUG00000020053.
DR   KEGG; vvp:112930761; -.
DR   OMA; HELYFKK; -.
DR   OrthoDB; 5489121at2759; -.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0009384; F:N-acylmannosamine kinase activity; IEA:Ensembl.
DR   GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:Ensembl.
DR   GO; GO:0046380; P:N-acetylneuraminate biosynthetic process; IEA:Ensembl.
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   Kinase {ECO:0000313|RefSeq:XP_025868949.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW   Transferase {ECO:0000313|RefSeq:XP_025868949.1}.
FT   DOMAIN          38..375
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
FT   ACT_SITE        517
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-1"
FT   BINDING         477
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT   BINDING         489
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT   BINDING         517
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT   BINDING         566
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT   BINDING         569
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT   BINDING         569
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT   BINDING         579
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         586
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT   BINDING         588
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
SQ   SEQUENCE   722 AA;  79228 MW;  F363F92BBAD488E4 CRC64;
     MEKNGDNRKL RVCVATCNRA DYSKLAPIMF GIKMEPEFFE LDVVVLGSHL IDDYGNTYRM
     IEQDDFDINT RLHTIVRGED EAAMVESVGL ALVKLPDVLN RLKPDIMIVH GDRFDALALA
     TSAALMNIRI LHIEGGEVSG TIDDSIRHAI TKLAHYHVCC TRSAEQHLIS MCEDHDRILL
     AGCPSYDKLL SAKNKDYMSI IRMWLGDDVK SKDYIVALQH PVTTDIKHSI KMFELTLDAL
     ISFNKRTLVL FPNIDAGSKE MVRVMRKKGI EHHPNFRAVK HVPFDQFIQL VAHAGCMIGN
     SSCGVREVGA FGTPVINLGT RQIGRETGEN VLHVRDADTQ DKILQALHLQ FGKQYPCSKI
     YGDGNAVPRI LKFLKSIDLQ EPLQKKFCFP PVKENISQDI DHILETLSAL AVDLGGTNLR
     VAIVSMKGEI VKKYTQFNPK TYEERINLIL QMCVEAAAEA VKLNCRILGV GISTGGRVNP
     REGVVLHSTK LIQEWNSVDL RTPLSDTLHL PVWVDNDGNC AALAERKFGQ GKGLENFVTL
     ITGTGIGGGI IHQHELIHGS SFCAAELGHL VVSLDGPDCS CGSHGCIEAY ASGMALQREA
     KKLHDEDLLL VEGMSVPKDE AVSAVHLIQA AKLGNVKAQS ILRTAGTALG LGVVNILHTI
     NPSLVILSGV LAGHYIHIVK DVIRQQALSS VQDVDVVVSD LVDPALLGAA SMVLDYTTRR
     IC
//
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