ID   A0A3P8N8P2_ASTCA        Unreviewed;       763 AA.
AC   A0A3P8N8P2;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-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:ENSACLP00000001114.1};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000001114.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000001114.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000001114.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3P8N8P2; -.
DR   STRING; 8154.ENSACLP00000001114; -.
DR   Ensembl; ENSACLT00000001140.1; ENSACLP00000001114.1; ENSACLG00000000785.1.
DR   GeneTree; ENSGT00390000017246; -.
DR   OMA; HELYFKK; -.
DR   OrthoDB; 5489121at2759; -.
DR   Proteomes; UP000265100; Chromosome 6.
DR   Bgee; ENSACLG00000000785; Expressed in liver and 7 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   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   4: Predicted;
FT   DOMAIN          77..415
FT                   /note="UDP-N-acetylglucosamine 2-epimerase"
FT                   /evidence="ECO:0000259|Pfam:PF02350"
FT   ACT_SITE        558
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-1"
FT   BINDING         518
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT   BINDING         530
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT   BINDING         558
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT   BINDING         607
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT   BINDING         610
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT   BINDING         610
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
FT   BINDING         620
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT   BINDING         622
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT   BINDING         627
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-3"
FT   BINDING         629
FT                   /ligand="an N-acyl-D-mannosamine"
FT                   /ligand_id="ChEBI:CHEBI:16062"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620004-2"
SQ   SEQUENCE   763 AA;  84109 MW;  5ED421617A8BF9A8 CRC64;
     MDMHLGSVQI SPHPLNIWKA QEQYFLRMQR NKEKKSMEKM GESNQCKRKL RVCVATCNRA
     DYSKLAPIMS GIKSHPEDFE LEVVVLGSHL IDDYGNTFRM IEQDDFDIGS KLHTIVRGED
     EAAMVESVGL ALVKLPDVIQ RLKPDILVVH GDRFDALALA TAAALMNIRI LHLEGGEVSG
     TIDDSIRHAI SKLAHYHACC TRMAEQHLIA MCEDHSRILL AGCPSYDKLL LSHHREDYMD
     IIKSWLDDKV QEGDYIVALQ HPVTTNIQHS IKIYGLMLDA LISFNKKTLI LFPNIDAGSK
     EMVRVMRRKG IEQHPNFRAV KHIPFEQFIQ LVSHAGCMIG NSSCGVREAG AFGTPVINLG
     TRQTGRETGE NVLHVRDADT HNKIYHALEL QFGKRYPCSK IYGDGNAVPR ILKFLRSIDL
     DEPLQKTFCF PPVKDPISQD IDHILETQSA LAVDLGGTNL RVAIVCMRGT IVKKYSQPNP
     KTFEARMELI LKMCNDAMRD AVGLNCRILG VGVSTGGRVN PQDGVVLHST KLIQEWSSVD
     LRTPISDALH LPVWVDNDGN CAALAERKFG HGKGVENFVT VITGTGIGGG IIHHNELVHG
     STFCAAELGH IMVSLEGPEC MCGSRGCIEA YASGMALQRE AKKLHDEDLL KVEGMDMKLS
     EPITAAHLIS AAKMGNSKAD AVLTKAATAL GVGIINILHI VNPSQVILSG VLASYYQAPV
     QHVISQRALF SVQNIKVVTS DLEEPALLGA ASMVLDYATR RIY
//