ID H3A1P0_LATCH Unreviewed; 720 AA.
AC H3A1P0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase {ECO:0000313|Ensembl:ENSLACP00000003561.1};
GN Name=GNE {ECO:0000313|Ensembl:ENSLACP00000003561.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000003561.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000003561.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AFYH01192786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01192787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01192788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01192789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01192790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01192791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006008242.1; XM_006008180.2.
DR RefSeq; XP_006008244.1; XM_006008182.2.
DR RefSeq; XP_014351401.1; XM_014495915.1.
DR Ensembl; ENSLACT00000003593.1; ENSLACP00000003561.1; ENSLACG00000003172.2.
DR Ensembl; ENSLACT00000025766.1; ENSLACP00000022946.1; ENSLACG00000003172.2.
DR GeneID; 102354276; -.
DR KEGG; lcm:102354276; -.
DR CTD; 10020; -.
DR GeneTree; ENSGT00390000017246; -.
DR HOGENOM; CLU_023411_0_0_1; -.
DR OrthoDB; 5489121at2759; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000003172; Expressed in pectoral fin and 6 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:UP000008672}.
FT DOMAIN 36..374
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT /evidence="ECO:0000259|Pfam:PF02350"
FT ACT_SITE 515
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-1"
FT BINDING 475
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 487
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 515
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="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT BINDING 567
FT /ligand="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT BINDING 577
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
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 584
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="an N-acyl-D-mannosamine"
FT /ligand_id="ChEBI:CHEBI:16062"
FT /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
SQ SEQUENCE 720 AA; 78676 MW; CAD860EFC49F9DB5 CRC64;
MEKKGNQRKL QICVATCNRA DYSKLAPIMS GIKAESDYFK LDVVVLGSHM IDDYGNTYRM
IEQDDFDIDT RLHTIVRGED EAAMVESVGL ALVKLPDVLI RLKPDIMIVH GDRFDALAVA
TSAALMNIRI LHVEGGEVSG TIDDSIRHAI TKLAHYHVCC TRSAEQHLIA MCEDHDTILL
AGCPSYDKLL SAKNQDYMSI LQVWLGDVKP NEYIVALQHP VTTDIKHSIK MFELTLEALL
SFNKKTLILF PNIDAGSKEM VRVMRKKGIE QHPNFRAVKH IPFDQFIQLV AHAGCVIGNS
SCGVREAGAF GTPVINLGTR QTGRETGENV LHVRDTDTKN KILHALEIQF GKQYPCSKIY
GDGNAVPRIL KFLKSIDITE PLQKKFCFPP VKNISQDIDH ILETRSALAV DLGGTNLRVA
IVSMKGEIIK LCKQPNPKTY EARIALILKM CVEAASEAVD MNCRILGVGV STGGRVNPND
GVILHSTKLI QEWTSVDLRT PISDALHLPV WVDNDGNCAT LAERKFGHGR GVENFVTVIT
GTGIGGGVLH RSELIHGTSF CAAEFGHIAV SVDGPECSCG NRGCIEAYAS GMALQREAKR
LNDEESLLME GMALKNEETV SAIDLIVASK FGNLKAEKVL RTAGTAVGLG ILNILHILNP
SLVILSGVLA SQYESTVKEI ISQRALPSAQ TVNVVISNLV EPALLGAASM VLDYSTRRTY
//
