ID Q4W392_TAKRU Unreviewed; 695 AA.
AC Q4W392; H2USH4;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Putative UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase {ECO:0000313|EMBL:CAG33857.1};
DE Flags: Fragment;
GN Name=glcne {ECO:0000313|EMBL:CAG33857.1};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|EMBL:CAG33857.1};
RN [1] {ECO:0000313|EMBL:CAG33857.1}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann F.;
RT "Evolution of sialic acids.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AJ745719; CAG33857.1; -; mRNA.
DR RefSeq; XP_011611361.1; XM_011613059.1.
DR RefSeq; XP_011611362.1; XM_011613060.1.
DR RefSeq; XP_011611363.1; XM_011613061.1.
DR AlphaFoldDB; Q4W392; -.
DR STRING; 31033.ENSTRUP00000078238; -.
DR GeneID; 778010; -.
DR CTD; 10020; -.
DR HOGENOM; CLU_023411_0_0_1; -.
DR OrthoDB; 5489121at2759; -.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 2: Evidence at transcript level;
KW Kinase {ECO:0000313|EMBL:CAG33857.1};
KW Transferase {ECO:0000313|EMBL:CAG33857.1}.
FT DOMAIN 9..347
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
FT ACT_SITE 490
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-1"
FT BINDING 450
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 462
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 490
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 539
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 542
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 552
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 559
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 561
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAG33857.1"
SQ SEQUENCE 695 AA; 76179 MW; 8B977A3981B19B19 CRC64;
MFGLKSHPDE FELEVVVLGS HLIDDYGNTF RMIEQDDFDI GSKLHTIVRG EDEAAMVESV
GLALVKLPDV IQRLHPDILV VHGDRFDALA LATAAALMNI RILHVEGGEV SGTIDDSIRH
AISKLAHYHA CCTRMAEQHL IAMCEDHSRI LLAGCPSYDK LLLSHQKEDY MDIIKSWLGD
NVKEHDYIVA LQHPVTTDIK NSIKIYGLML DALLSFNKTT LILFPNIDAG SKEMVRVMRK
KGIEQHPNFR AVKHIPFEQF IQLVNHAGCM IGNSSCGVRE AGAFGTPVIN LGTRQTGRET
GENVLHVRDA DTHNKIYHAL ELQFGKRYPC SKIYGDGNAV PRILKFLSSI DLDEPLQKTF
CFPPVKDPIS QDIDHILETQ SALAVDLGGT NLRVAIICMR GNIVRKYTQA NPKTFEARMQ
LILKMCSDAM RDAVFLNCRI LGVGVSTGGR VNPQEGVVLH STKLIQEWSA VDLRTPISDA
LHLPVWVDND GNCAALAEKK FGHGKGVENF VTVITGTGIG GGIIHQNELV HGSTFCAAEL
GHIMVSFDGP ECSCGSRGCI ESIASGMALQ REAKRLHDED LLKVDGLDMK ISDPITAAHL
INAARLGNSK ANIVLNKAST ALGMGIINIL HIMNPSLVIL SGVLGSYYQA PVQRTIMERA
LFSAQSVKVV ISDLEEPALL GAASMVLDYA TRRIY
//
