ID GLCNE_MOUSE Reviewed; 722 AA. AC Q91WG8; Q8CC83; Q8CCB0; Q9Z0P6; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 156. DE RecName: Full=Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase {ECO:0000305}; DE AltName: Full=UDP-GlcNAc-2-epimerase/ManAc kinase; DE Includes: DE RecName: Full=UDP-N-acetylglucosamine 2-epimerase (hydrolyzing) {ECO:0000305|PubMed:10745088}; DE EC=3.2.1.183 {ECO:0000269|PubMed:10745088, ECO:0000269|PubMed:11929971}; DE AltName: Full=UDP-GlcNAc-2-epimerase; DE AltName: Full=Uridine diphosphate-N-acetylglucosamine-2-epimerase; DE Includes: DE RecName: Full=N-acetylmannosamine kinase {ECO:0000250|UniProtKB:Q9Y223}; DE EC=2.7.1.60 {ECO:0000250|UniProtKB:Q9Y223}; DE AltName: Full=ManAc kinase; GN Name=Gne {ECO:0000312|MGI:MGI:1354951}; Synonyms=Glcne, Uae1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=BALB/cJ; TISSUE=Liver; RX PubMed=10103025; DOI=10.1046/j.1432-1327.1999.00253.x; RA Horstkorte R., Noehring S., Wiechens N., Schwarzkopf M., Danker K., RA Reutter W., Lucka L.; RT "Tissue expression and amino acid sequence of murine UDP-N- RT acetylglucosamine-2-epimerase/N-acetylmannosamine kinase."; RL Eur. J. Biochem. 260:923-927(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 572-722. RC STRAIN=C57BL/6J; TISSUE=Colon; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PHOSPHORYLATION. RX PubMed=10745088; DOI=10.1016/s0014-5793(00)01331-4; RA Horstkorte R., Noehring S., Danker K., Effertz K., Reutter W., Lucka L.; RT "Protein kinase C phosphorylates and regulates UDP-N-acetylglucosamine-2- RT epimerase/N-acetylmannosamine kinase."; RL FEBS Lett. 470:315-318(2000). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE. RX PubMed=11929971; DOI=10.1073/pnas.072066199; RA Schwarzkopf M., Knobeloch K.-P., Rohde E., Hinderlich S., Wiechens N., RA Lucka L., Horak I., Reutter W., Horstkorte R.; RT "Sialylation is essential for early development in mice."; RL Proc. Natl. Acad. Sci. U.S.A. 99:5267-5270(2002). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney, Liver, Lung, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Bifunctional enzyme that possesses both UDP-N- CC acetylglucosamine 2-epimerase and N-acetylmannosamine kinase CC activities, and serves as the initiator of the biosynthetic pathway CC leading to the production of N-acetylneuraminic acid (NeuAc), a CC critical precursor in the synthesis of sialic acids. By catalyzing this CC pivotal and rate-limiting step in sialic acid biosynthesis, this enzyme CC assumes a pivotal role in governing the regulation of cell surface CC sialylation (PubMed:11929971). Sialic acids represent a category of CC negatively charged sugars that reside on the surface of cells as CC terminal components of glycoconjugates and mediate important functions CC in various cellular processes, including cell adhesion, signal CC transduction, and cellular recognition (By similarity). CC {ECO:0000250|UniProtKB:Q9Y223, ECO:0000269|PubMed:11929971}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-acetyl-D- CC mannosamine + UDP; Xref=Rhea:RHEA:30683, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17122, ChEBI:CHEBI:57705, CC ChEBI:CHEBI:58223; EC=3.2.1.183; CC Evidence={ECO:0000269|PubMed:10745088, ECO:0000269|PubMed:11929971}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30684; CC Evidence={ECO:0000269|PubMed:11929971}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acyl-D-mannosamine + ATP = ADP + an N-acyl-D-mannosamine CC 6-phosphate + H(+); Xref=Rhea:RHEA:23832, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16062, ChEBI:CHEBI:30616, ChEBI:CHEBI:57666, CC ChEBI:CHEBI:456216; EC=2.7.1.60; CC Evidence={ECO:0000250|UniProtKB:Q9Y223}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23833; CC Evidence={ECO:0000250|UniProtKB:Q9Y223}; CC -!- ACTIVITY REGULATION: The UDP-N-acetylglucosamine 2-epimerase activity, CC in contrast to the N-acetylmannosamine kinase activity, exhibits CC allosteric regulation by cytidine monophosphate-N-acetylneuraminic acid CC (CMP-Neu5Ac), the end product of neuraminic acid biosynthesis (By CC similarity). Moreover, the activity is contingent upon the oligomeric CC state of the enzyme. The monomeric form is inactive, while the dimeric CC form selectively catalyzes the phosphorylation of N-acetylmannosamine. CC The hexameric form, on the other hand, demonstrates full proficiency in CC both enzyme activities (By similarity). Furthermore, the UDP-N- CC acetylglucosamine 2-epimerase activity is increased by PKC-mediated CC phosphorylation (PubMed:10745088). {ECO:0000250|UniProtKB:O35826, CC ECO:0000250|UniProtKB:Q9Y223, ECO:0000269|PubMed:10745088}. CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate biosynthesis. CC {ECO:0000269|PubMed:11929971}. CC -!- SUBUNIT: Homodimer. Homotetramer. Homohexamer (By similarity). The CC hexameric form exhibits both enzyme activities, whereas the dimeric CC form only catalyzes the phosphorylation of N-acyl-D-mannosamine (By CC similarity). {ECO:0000250|UniProtKB:O35826, CC ECO:0000250|UniProtKB:Q9Y223}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:O35826}. CC -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in liver. Also CC found at high levels in lung, brain and kidney. CC {ECO:0000269|PubMed:10103025}. CC -!- DEVELOPMENTAL STAGE: In the embryo, expressed at day 7 dpc, 11 dpc and CC 15 dpc. {ECO:0000269|PubMed:10103025}. CC -!- PTM: Phosphorylated. Phosphorylation by PKC activates the UDP-N- CC acetylglucosamine 2-epimerase activity. {ECO:0000269|PubMed:10745088}. CC -!- DISRUPTION PHENOTYPE: Knockout of the gene is embryonic lethal. CC {ECO:0000269|PubMed:11929971}. CC -!- SIMILARITY: In the N-terminal section; belongs to the UDP-N- CC acetylglucosamine 2-epimerase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the ROK (NagC/XylR) CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ132236; CAB36908.1; -; mRNA. DR EMBL; BC015277; AAH15277.1; -; mRNA. DR EMBL; BC051254; AAH51254.1; -; mRNA. DR EMBL; AK033507; BAC28328.1; -; mRNA. DR EMBL; AK033691; BAC28432.1; -; mRNA. DR CCDS; CCDS51170.1; -. DR RefSeq; NP_001177343.1; NM_001190414.1. DR RefSeq; NP_056643.3; NM_015828.3. DR AlphaFoldDB; Q91WG8; -. DR SMR; Q91WG8; -. DR BioGRID; 206129; 1. DR STRING; 10090.ENSMUSP00000030201; -. DR iPTMnet; Q91WG8; -. DR PhosphoSitePlus; Q91WG8; -. DR SwissPalm; Q91WG8; -. DR EPD; Q91WG8; -. DR jPOST; Q91WG8; -. DR MaxQB; Q91WG8; -. DR PaxDb; 10090-ENSMUSP00000030201; -. DR ProteomicsDB; 267633; -. DR Pumba; Q91WG8; -. DR Antibodypedia; 2058; 286 antibodies from 28 providers. DR DNASU; 50798; -. DR Ensembl; ENSMUST00000102936.9; ENSMUSP00000100000.3; ENSMUSG00000028479.19. DR GeneID; 50798; -. DR KEGG; mmu:50798; -. DR UCSC; uc008srm.2; mouse. DR AGR; MGI:1354951; -. DR CTD; 10020; -. DR MGI; MGI:1354951; Gne. DR VEuPathDB; HostDB:ENSMUSG00000028479; -. DR eggNOG; ENOG502QUGI; Eukaryota. DR GeneTree; ENSGT00390000017246; -. DR InParanoid; Q91WG8; -. DR OMA; HELYFKK; -. DR OrthoDB; 5489121at2759; -. DR BRENDA; 2.7.1.60; 3474. DR BRENDA; 3.2.1.183; 3474. DR Reactome; R-MMU-4085001; Sialic acid metabolism. DR UniPathway; UPA00630; -. DR BioGRID-ORCS; 50798; 12 hits in 83 CRISPR screens. DR ChiTaRS; Gne; mouse. DR PRO; PR:Q91WG8; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; Q91WG8; Protein. DR Bgee; ENSMUSG00000028479; Expressed in submandibular gland and 265 other cell types or tissues. DR ExpressionAtlas; Q91WG8; baseline and differential. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; ISS:MGI. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009384; F:N-acylmannosamine kinase activity; ISS:UniProtKB. DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IDA:UniProtKB. DR GO; GO:0006045; P:N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046380; P:N-acetylneuraminate biosynthetic process; IMP:UniProtKB. DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; TAS:MGI. 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. DR Genevisible; Q91WG8; MM. PE 1: Evidence at protein level; KW Allosteric enzyme; ATP-binding; Cytoplasm; Hydrolase; Kinase; Magnesium; KW Metal-binding; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transferase; Zinc. FT CHAIN 1..722 FT /note="Bifunctional UDP-N-acetylglucosamine 2-epimerase/N- FT acetylmannosamine kinase" FT /id="PRO_0000095717" FT REGION 1..? FT /note="UDP-N-acetylglucosamine 2-epimerase" FT /evidence="ECO:0000250|UniProtKB:O35826" FT REGION 406..722 FT /note="N-acetylmannosamine kinase" FT /evidence="ECO:0000250|UniProtKB:O35826" FT ACT_SITE 517 FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 19 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 23 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 113 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 220 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 253 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 259 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /ligand_note="allosteric inhibitor" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 271 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /ligand_note="allosteric inhibitor" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 280 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /ligand_note="allosteric inhibitor" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 281 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /ligand_note="allosteric inhibitor" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 282 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 301 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 302 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 307 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 321 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 413 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 416 FT /ligand="an N-acyl-D-mannosamine 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57666" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 417 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 418 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 420 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 476 FT /ligand="an N-acyl-D-mannosamine" FT /ligand_id="ChEBI:CHEBI:16062" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 476 FT /ligand="an N-acyl-D-mannosamine 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57666" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 477 FT /ligand="an N-acyl-D-mannosamine" FT /ligand_id="ChEBI:CHEBI:16062" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 477 FT /ligand="an N-acyl-D-mannosamine 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57666" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 489 FT /ligand="an N-acyl-D-mannosamine" FT /ligand_id="ChEBI:CHEBI:16062" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 489 FT /ligand="an N-acyl-D-mannosamine 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57666" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 516 FT /ligand="an N-acyl-D-mannosamine" FT /ligand_id="ChEBI:CHEBI:16062" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 516 FT /ligand="an N-acyl-D-mannosamine 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57666" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 517 FT /ligand="an N-acyl-D-mannosamine" FT /ligand_id="ChEBI:CHEBI:16062" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 517 FT /ligand="an N-acyl-D-mannosamine 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57666" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 545 FT /ligand="an N-acyl-D-mannosamine 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57666" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 566 FT /ligand="an N-acyl-D-mannosamine" FT /ligand_id="ChEBI:CHEBI:16062" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 569 FT /ligand="an N-acyl-D-mannosamine" FT /ligand_id="ChEBI:CHEBI:16062" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 569 FT /ligand="an N-acyl-D-mannosamine 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57666" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 569 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 579 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 581 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 586 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="structural" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 588 FT /ligand="an N-acyl-D-mannosamine" FT /ligand_id="ChEBI:CHEBI:16062" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT BINDING 588 FT /ligand="an N-acyl-D-mannosamine 6-phosphate" FT /ligand_id="ChEBI:CHEBI:57666" FT /evidence="ECO:0000250|UniProtKB:Q9Y223" FT CONFLICT 566..567 FT /note="EL -> DV (in Ref. 1; CAB36908)" FT /evidence="ECO:0000305" FT CONFLICT 623 FT /note="G -> V (in Ref. 1; CAB36908)" FT /evidence="ECO:0000305" SQ SEQUENCE 722 AA; 79199 MW; 0DFDD681BFD17984 CRC64; MEKNGNNRKL RVCVATCNRA DYSKLAPIMF GIKTEPAFFE LDVVVLGSHL IDDYGNTYRM IEQDDFDINT RLHTIVRGED EAAMVESVGL ALVKLPDVLN RLKPDIMIVH GDRFDALALA TSAALMNIRI LHIEGGEVSG TIDDSIRHAI TKLAHYHVCC TRSAEQHLIS MCEDHDRILL AGCPSYDKLL SAKNKDYMSI IRMWLGDDVK CKDYIVALQH PVTTDIKHSI KMFELTLDAL ISFNKRTLVL FPNIDAGSKE MVRVMRKKGI EHHPNFRAVK HVPFDQFIQL VAHAGCMIGN SSCGVREVGA FGTPVINLGT RQIGRETGEN VLHVRDADTQ DKILQALHLQ FGKQYPCSKI YGDGNAVPRI LKFLKSIDLQ EPLQKKFCFP PVKENISQDI DHILETLSAL AVDLGGTNLR VAIVSMKGEI VKKYTQFNPK TYEERISLIL QMCVEAAAEA VKLNCRILGV GISTGGRVNP QEGVVLHSTK LIQEWNSVDL RTPLSDTLHL PVWVDNDGNC AAMAERKFGQ GKGQENFVTL ITGTGIGGGI IHQHELIHGS SFCAAELGHL VVSLDGPDCS CGSHGCIEAY ASGMALQREA KKLHDEDLLL VEGMSVPKDE AVGALHLIQA AKLGNVKAQS ILRTAGTALG LGVVNILHTM NPSLVILSGV LASHYIHIVK DVIRQQALSS VQDVDVVVSD LVDPALLGAA SMVLDYTTRR IH //