CEGT_HUMAN
ID CEGT_HUMAN Reviewed; 394 AA.
AC Q16739; Q5T258;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Ceramide glucosyltransferase {ECO:0000305};
DE EC=2.4.1.80 {ECO:0000269|PubMed:8643456};
DE AltName: Full=GLCT-1;
DE AltName: Full=Glucosylceramide synthase;
DE Short=GCS {ECO:0000303|PubMed:33361282};
DE AltName: Full=Glycosylceramide synthase {ECO:0000305};
DE AltName: Full=UDP-glucose ceramide glucosyltransferase;
DE AltName: Full=UDP-glucose:N-acylsphingosine D-glucosyltransferase;
GN Name=UGCG {ECO:0000312|HGNC:HGNC:12524};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Melanoma;
RX PubMed=8643456; DOI=10.1073/pnas.93.10.4638;
RA Ichikawa S., Sakiyama H., Suzuki G., Hidari K.I.-P., Hirabayashi Y.;
RT "Expression cloning of a cDNA for human ceramide glucosyltransferase that
RT catalyzes the first glycosylation step of glycosphingolipid synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4638-4643(1996).
RN [2]
RP ERRATUM OF PUBMED:8643456.
RX PubMed=8901638; DOI=10.1073/pnas.93.22.12654;
RA Ichikawa S., Sakiyama H., Suzuki G., Hidari K.I.-P., Hirabayashi Y.;
RL Proc. Natl. Acad. Sci. U.S.A. 93:12654-12654(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [7]
RP FUNCTION.
RX PubMed=1532799; DOI=10.1083/jcb.117.2.259;
RA Jeckel D., Karrenbauer A., Burger K.N., van Meer G., Wieland F.;
RT "Glucosylceramide is synthesized at the cytosolic surface of various Golgi
RT subfractions.";
RL J. Cell Biol. 117:259-267(1992).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=9545298; DOI=10.1074/jbc.273.16.9651;
RA Watanabe R., Wu K., Paul P., Marks D.L., Kobayashi T., Pittelkow M.R.,
RA Pagano R.E.;
RT "Up-regulation of glucosylceramide synthase expression and activity during
RT human keratinocyte differentiation.";
RL J. Biol. Chem. 273:9651-9655(1998).
RN [9]
RP INTERACTION WITH RTN1, AND SUBCELLULAR LOCATION.
RX PubMed=12873973;
RA Di Sano F., Fazi B., Citro G., Lovat P.E., Cesareni G., Piacentini M.;
RT "Glucosylceramide synthase and its functional interaction with RTN-1C
RT regulate chemotherapeutic-induced apoptosis in neuroepithelioma cells.";
RL Cancer Res. 63:3860-3865(2003).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=33361282; DOI=10.1194/jlr.ra120001043;
RA Boer D.E., Mirzaian M., Ferraz M.J., Zwiers K.C., Baks M.V., Hazeu M.D.,
RA Ottenhoff R., Marques A.R.A., Meijer R., Roos J.C.P., Cox T.M., Boot R.G.,
RA Pannu N., Overkleeft H.S., Artola M., Aerts J.M.;
RT "Human glucocerebrosidase mediates formation of xylosyl-cholesterol by
RT beta-xylosidase and transxylosidase reactions.";
RL J. Lipid Res. 62:100018-100018(2021).
CC -!- FUNCTION: Participates in the initial step of the glucosylceramide-
CC based glycosphingolipid/GSL synthetic pathway at the cytosolic surface
CC of the Golgi (PubMed:8643456, PubMed:1532799). Catalyzes the transfer
CC of glucose from UDP-glucose to ceramide to produce
CC glucosylceramide/GlcCer (such as beta-D-glucosyl-(1<->1')-N-acylsphing-
CC 4-enine) (PubMed:1532799, PubMed:8643456). GlcCer is the core component
CC of glycosphingolipids/GSLs, amphipathic molecules consisting of a
CC ceramide lipid moiety embedded in the outer leaflet of the membrane,
CC linked to one of hundreds of different externally oriented
CC oligosaccharide structures (PubMed:8643456). Glycosphingolipids are
CC essential components of membrane microdomains that mediate membrane
CC trafficking and signal transduction, implicated in many fundamental
CC cellular processes, including growth, differentiation, migration,
CC morphogenesis, cell-to-cell and cell-to-matrix interactions (By
CC similarity). They are required for instance in the proper development
CC and functioning of the nervous system (By similarity). As an example of
CC their role in signal transduction, they regulate the leptin
CC receptor/LEPR in the leptin-mediated signaling pathway (By similarity).
CC They also play an important role in the establishment of the skin
CC barrier regulating keratinocyte differentiation and the proper assembly
CC of the cornified envelope (By similarity). The biosynthesis of GSLs is
CC also required for the proper intestinal endocytic uptake of nutritional
CC lipids (By similarity). Catalyzes the synthesis of
CC xylosylceramide/XylCer (such as beta-D-xylosyl-(1<->1')-N-acylsphing-4-
CC enine) using UDP-Xyl as xylose donor (PubMed:33361282).
CC {ECO:0000250|UniProtKB:O88693, ECO:0000269|PubMed:1532799,
CC ECO:0000269|PubMed:33361282, ECO:0000269|PubMed:8643456,
CC ECO:0000303|PubMed:8643456}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine + UDP-alpha-D-glucose = a beta-D-
CC glucosyl-(1<->1')-N-acylsphing-4-enine + H(+) + UDP;
CC Xref=Rhea:RHEA:12088, ChEBI:CHEBI:15378, ChEBI:CHEBI:22801,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.80;
CC Evidence={ECO:0000269|PubMed:8643456};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12089;
CC Evidence={ECO:0000269|PubMed:8643456};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine + UDP-alpha-D-xylose = a beta-D-
CC xylosyl-(1<->1')-N-acylsphing-4-enine + H(+) + UDP;
CC Xref=Rhea:RHEA:70243, ChEBI:CHEBI:15378, ChEBI:CHEBI:52639,
CC ChEBI:CHEBI:57632, ChEBI:CHEBI:58223, ChEBI:CHEBI:189068;
CC Evidence={ECO:0000269|PubMed:33361282};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70244;
CC Evidence={ECO:0000269|PubMed:33361282};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(9Z-octadecenoyl)-sphing-4-enine + UDP-alpha-D-xylose =
CC beta-D-xylosyl-(1<->1')-N-(9Z-octadecenoyl)-sphing-4-enine + H(+) +
CC UDP; Xref=Rhea:RHEA:70247, ChEBI:CHEBI:15378, ChEBI:CHEBI:57632,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:77996, ChEBI:CHEBI:189081;
CC Evidence={ECO:0000269|PubMed:33361282};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70248;
CC Evidence={ECO:0000269|PubMed:33361282};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000305|PubMed:33361282, ECO:0000305|PubMed:8643456}.
CC -!- SUBUNIT: Interacts with RTN1; regulates the ceramide
CC glucosyltransferase activity of UGCG. {ECO:0000269|PubMed:12873973}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12873973}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9R0E0}.
CC -!- TISSUE SPECIFICITY: Found in all tissues examined.
CC {ECO:0000269|PubMed:8643456}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during keratinocyte differentiation.
CC {ECO:0000269|PubMed:9545298}.
CC -!- DOMAIN: The D1, D2, D3, (Q/R)XXRW motif is a critical part of the GCS
CC active site, involved in catalysis and UDP-sugar binding.
CC {ECO:0000250|UniProtKB:Q9R0E0}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; D50840; BAA09451.1; -; mRNA.
DR EMBL; AK314847; BAG37364.1; -; mRNA.
DR EMBL; AL442066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471105; EAW59091.1; -; Genomic_DNA.
DR EMBL; BC038711; AAH38711.1; -; mRNA.
DR CCDS; CCDS6782.1; -.
DR RefSeq; NP_003349.1; NM_003358.2.
DR AlphaFoldDB; Q16739; -.
DR SMR; Q16739; -.
DR BioGRID; 113204; 35.
DR IntAct; Q16739; 14.
DR MINT; Q16739; -.
DR STRING; 9606.ENSP00000363397; -.
DR BindingDB; Q16739; -.
DR ChEMBL; CHEMBL2063; -.
DR DrugBank; DB09039; Eliglustat.
DR DrugBank; DB00419; Miglustat.
DR DrugCentral; Q16739; -.
DR GuidetoPHARMACOLOGY; 2528; -.
DR SwissLipids; SLP:000000674; -.
DR SwissLipids; SLP:000000675; -.
DR CAZy; GT21; Glycosyltransferase Family 21.
DR TCDB; 4.D.1.4.1; the putative vectorial glycosyl polymerization (vgp) family.
DR iPTMnet; Q16739; -.
DR PhosphoSitePlus; Q16739; -.
DR SwissPalm; Q16739; -.
DR BioMuta; UGCG; -.
DR DMDM; 2498228; -.
DR EPD; Q16739; -.
DR jPOST; Q16739; -.
DR MassIVE; Q16739; -.
DR MaxQB; Q16739; -.
DR PaxDb; Q16739; -.
DR PeptideAtlas; Q16739; -.
DR PRIDE; Q16739; -.
DR ProteomicsDB; 61050; -.
DR Antibodypedia; 15178; 191 antibodies from 30 providers.
DR DNASU; 7357; -.
DR Ensembl; ENST00000374279.4; ENSP00000363397.3; ENSG00000148154.10.
DR GeneID; 7357; -.
DR KEGG; hsa:7357; -.
DR MANE-Select; ENST00000374279.4; ENSP00000363397.3; NM_003358.3; NP_003349.1.
DR UCSC; uc004bft.4; human.
DR CTD; 7357; -.
DR DisGeNET; 7357; -.
DR GeneCards; UGCG; -.
DR HGNC; HGNC:12524; UGCG.
DR HPA; ENSG00000148154; Tissue enhanced (bone).
DR MIM; 602874; gene.
DR neXtProt; NX_Q16739; -.
DR OpenTargets; ENSG00000148154; -.
DR PharmGKB; PA37169; -.
DR VEuPathDB; HostDB:ENSG00000148154; -.
DR eggNOG; KOG2547; Eukaryota.
DR GeneTree; ENSGT00390000012898; -.
DR HOGENOM; CLU_030898_0_0_1; -.
DR InParanoid; Q16739; -.
DR OMA; HGSMPFH; -.
DR OrthoDB; 793389at2759; -.
DR PhylomeDB; Q16739; -.
DR TreeFam; TF314564; -.
DR BioCyc; MetaCyc:HS07494-MON; -.
DR BRENDA; 2.4.1.80; 2681.
DR PathwayCommons; Q16739; -.
DR Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
DR SignaLink; Q16739; -.
DR SIGNOR; Q16739; -.
DR UniPathway; UPA00222; -.
DR BioGRID-ORCS; 7357; 53 hits in 1089 CRISPR screens.
DR ChiTaRS; UGCG; human.
DR GeneWiki; UGCG; -.
DR GenomeRNAi; 7357; -.
DR Pharos; Q16739; Tclin.
DR PRO; PR:Q16739; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q16739; protein.
DR Bgee; ENSG00000148154; Expressed in upper leg skin and 185 other tissues.
DR ExpressionAtlas; Q16739; baseline and differential.
DR Genevisible; Q16739; HS.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0008120; F:ceramide glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0102769; F:dihydroceramide glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
DR GO; GO:1903575; P:cornified envelope assembly; ISS:UniProtKB.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
DR GO; GO:0006679; P:glucosylceramide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
DR GO; GO:0098856; P:intestinal lipid absorption; ISS:UniProtKB.
DR GO; GO:0030216; P:keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0033210; P:leptin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; ISS:UniProtKB.
DR GO; GO:0006497; P:protein lipidation; ISS:UniProtKB.
DR GO; GO:0009966; P:regulation of signal transduction; ISS:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR025993; Ceramide_glucosylTrfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR12726; PTHR12726; 1.
DR Pfam; PF13506; Glyco_transf_21; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Acetylation; Glycosyltransferase; Golgi apparatus; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..394
FT /note="Ceramide glucosyltransferase"
FT /id="PRO_0000059176"
FT TOPO_DOM 1..10
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..287
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..348
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 92
FT /note="D1"
FT /evidence="ECO:0000305"
FT MOTIF 144
FT /note="D2"
FT /evidence="ECO:0000305"
FT MOTIF 236
FT /note="D3"
FT /evidence="ECO:0000305"
FT MOTIF 272..276
FT /note="(Q/R)XXRW"
FT /evidence="ECO:0000305"
FT ACT_SITE 236
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9R0E0"
FT SITE 193
FT /note="May play an important role in binding to the
FT inhibitors DEPC and PDMP"
FT /evidence="ECO:0000250"
FT MOD_RES 117
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O88693"
SQ SEQUENCE 394 AA; 44854 MW; 3B998569F8A96449 CRC64;
MALLDLALEG MAVFGFVLFL VLWLMHFMAI IYTRLHLNKK ATDKQPYSKL PGVSLLKPLK
GVDPNLINNL ETFFELDYPK YEVLLCVQDH DDPAIDVCKK LLGKYPNVDA RLFIGGKKVG
INPKINNLMP GYEVAKYDLI WICDSGIRVI PDTLTDMVNQ MTEKVGLVHG LPYVADRQGF
AATLEQVYFG TSHPRYYISA NVTGFKCVTG MSCLMRKDVL DQAGGLIAFA QYIAEDYFMA
KAIADRGWRF AMSTQVAMQN SGSYSISQFQ SRMIRWTKLR INMLPATIIC EPISECFVAS
LIIGWAAHHV FRWDIMVFFM CHCLAWFIFD YIQLRGVQGG TLCFSKLDYA VAWFIRESMT
IYIFLSALWD PTISWRTGRY RLRCGGTAEE ILDV
