MGT5A_HUMAN
ID MGT5A_HUMAN Reviewed; 741 AA.
AC Q09328; D3DP70;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A;
DE EC=2.4.1.155 {ECO:0000269|PubMed:10395745, ECO:0000269|PubMed:30140003};
DE AltName: Full=Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase V {ECO:0000303|PubMed:10395745};
DE AltName: Full=GlcNAc-T V {ECO:0000303|PubMed:10395745};
DE Short=GNT-V;
DE AltName: Full=Mannoside acetylglucosaminyltransferase 5;
DE AltName: Full=N-acetylglucosaminyl-transferase V;
DE Contains:
DE RecName: Full=Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A {ECO:0000305};
DE AltName: Full=Secreted beta-1,6-N-acetylglucosaminyltransferase V {ECO:0000303|PubMed:17142794};
DE Short=Secreted GNT-V {ECO:0000303|PubMed:17142794};
DE Flags: Precursor;
GN Name=MGAT5; Synonyms=GGNT5;
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].
RC TISSUE=Liver;
RX PubMed=8292036; DOI=10.1006/bbrc.1994.1045;
RA Nishikawa A., Saito H., Gu J., Ihara Y., Soejima H., Wada Y., Sekiya C.,
RA Kangawa K., Niikawa N., Taniguchi N.;
RT "cDNA cloning and chromosomal mapping of human N-
RT acetylglucosaminyltransferase V+.";
RL Biochem. Biophys. Res. Commun. 198:318-327(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND GLYCOSYLATION.
RX PubMed=10395745; DOI=10.1006/abbi.1999.1252;
RA Park C., Jin U.H., Lee Y.C., Cho T.J., Kim C.H.;
RT "Characterization of UDP-N-acetylglucosamine: alpha-6-d-mannoside beta-1,6-
RT N-acetylglucosaminyltransferase V from a human hepatoma cell line Hep3B.";
RL Arch. Biochem. Biophys. 367:281-288(1999).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION (SECRETED ALPHA-1,6-MANNOSYLGLYCOPROTEIN
RP 6-BETA-N-ACETYLGLUCOSAMINYLTRANSFERASE A).
RX PubMed=11872751; DOI=10.1074/jbc.m200521200;
RA Saito T., Miyoshi E., Sasai K., Nakano N., Eguchi H., Honke K.,
RA Taniguchi N.;
RT "A secreted type of beta 1,6-N-acetylglucosaminyltransferase V (GnT-V)
RT induces tumor angiogenesis without mediation of glycosylation: a novel
RT function of GnT-V distinct from the original glycosyltransferase
RT activity.";
RL J. Biol. Chem. 277:17002-17008(2002).
RN [5]
RP PROTEIN SEQUENCE OF 31-35 (SECRETED ALPHA-1,6-MANNOSYLGLYCOPROTEIN
RP 6-BETA-N-ACETYLGLUCOSAMINYLTRANSFERASE A), FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, SUBCELLULAR LOCATION, TOPOLOGY, GLYCOSYLATION, AND MUTAGENESIS OF
RP LEU-29; LEU-30 AND HIS-31.
RX PubMed=17142794; DOI=10.1096/fj.05-5066com;
RA Nakahara S., Saito T., Kondo N., Moriwaki K., Noda K., Ihara S.,
RA Takahashi M., Ide Y., Gu J., Inohara H., Katayama T., Tohyama M., Kubo T.,
RA Taniguchi N., Miyoshi E.;
RT "A secreted type of beta1,6 N-acetylglucosaminyltransferase V (GnT-V), a
RT novel angiogenesis inducer, is regulated by gamma-secretase.";
RL FASEB J. 20:2451-2459(2006).
RN [6]
RP FUNCTION, AND INDUCTION BY IFNG.
RX PubMed=22614033; DOI=10.3892/ijo.2012.1484;
RA Yang H.M., Yu C., Yang Z.;
RT "N-acetylglucosaminyltransferase V negatively regulates integrin
RT alpha5beta1-mediated monocyte adhesion and transmigration through vascular
RT endothelium.";
RL Int. J. Oncol. 41:589-598(2012).
RN [7] {ECO:0007744|PDB:5ZIB, ECO:0007744|PDB:5ZIC}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 121-741, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, GLYCOSYLATION AT ASN-433,
RP DISULFIDE BONDS, AND MUTAGENESIS OF GLU-280; GLU-287; GLU-297; GLU-429;
RP GLU-520 AND GLU-526.
RX PubMed=30140003; DOI=10.1038/s41467-018-05931-w;
RA Nagae M., Kizuka Y., Mihara E., Kitago Y., Hanashima S., Ito Y., Takagi J.,
RA Taniguchi N., Yamaguchi Y.;
RT "Structure and mechanism of cancer-associated N-
RT acetylglucosaminyltransferase-V.";
RL Nat. Commun. 9:3380-3380(2018).
CC -!- FUNCTION: Catalyzes the addition of N-acetylglucosamine (GlcNAc) in
CC beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked
CC oligosaccharides (PubMed:10395745, PubMed:30140003). Catalyzes an
CC important step in the biosynthesis of branched, complex-type N-glycans,
CC such as those found on EGFR, TGFR (TGF-beta receptor) and CDH2
CC (PubMed:10395745, PubMed:22614033, PubMed:30140003). Via its role in
CC the biosynthesis of complex N-glycans, plays an important role in the
CC activation of cellular signaling pathways, reorganization of the actin
CC cytoskeleton, cell-cell adhesion and cell migration. MGAT5-dependent
CC EGFR N-glycosylation enhances the interaction between EGFR and LGALS3
CC and thereby prevents rapid EGFR endocytosis and prolongs EGFR
CC signaling. Required for efficient interaction between TGFB1 and its
CC receptor. Enhances activation of intracellular signaling pathways by
CC several types of growth factors, including FGF2, PDGF, IGF, TGFB1 and
CC EGF. MGAT5-dependent CDH2 N-glycosylation inhibits CDH2-mediated
CC homotypic cell-cell adhesion and contributes to the regulation of
CC downstream signaling pathways. Promotes cell migration. Contributes to
CC the regulation of the inflammatory response. MGAT5-dependent TCR N-
CC glycosylation enhances the interaction between TCR and LGALS3, limits
CC agonist-induced TCR clustering, and thereby dampens TCR-mediated
CC responses to antigens. Required for normal leukocyte evasation and
CC accumulation at sites of inflammation (By similarity). Inhibits
CC attachment of monocytes to the vascular endothelium and subsequent
CC monocyte diapedesis (PubMed:22614033). {ECO:0000250|UniProtKB:Q8R4G6,
CC ECO:0000269|PubMed:10395745, ECO:0000269|PubMed:22614033,
CC ECO:0000269|PubMed:30140003}.
CC -!- FUNCTION: [Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-
CC acetylglucosaminyltransferase A]: Promotes proliferation of umbilical
CC vein endothelial cells and angiogenesis, at least in part by promoting
CC the release of the growth factor FGF2 from the extracellular matrix.
CC {ECO:0000269|PubMed:11872751}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-
CC (1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-
CC D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-
CC GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAcl-
CC (1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:16921, Rhea:RHEA-COMP:14374, Rhea:RHEA-COMP:14377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:139507, ChEBI:CHEBI:139510; EC=2.4.1.155;
CC Evidence={ECO:0000269|PubMed:10395745, ECO:0000269|PubMed:17142794,
CC ECO:0000269|PubMed:30140003};
CC -!- ACTIVITY REGULATION: Activity is increased by Mn(2+) and Mg(2+).
CC {ECO:0000269|PubMed:10395745}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.78 mM for GlcNAc {ECO:0000269|PubMed:30140003};
CC KM=5.8 mM for GlcNAc {ECO:0000269|PubMed:10395745};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:10395745};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:10395745};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:10395745, ECO:0000269|PubMed:17142794,
CC ECO:0000269|PubMed:30140003}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P97259}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:17142794}.
CC -!- SUBCELLULAR LOCATION: [Secreted alpha-1,6-mannosylglycoprotein 6-beta-
CC N-acetylglucosaminyltransferase A]: Secreted
CC {ECO:0000269|PubMed:17142794}.
CC -!- INDUCTION: Induced by IFNG treatment in monocytes (in vitro).
CC {ECO:0000269|PubMed:22614033}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10395745,
CC ECO:0000269|PubMed:17142794, ECO:0000269|PubMed:30140003}.
CC -!- PTM: A secreted form is released from the membrane after cleavage by
CC gamma-secretase. {ECO:0000269|PubMed:17142794}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 18 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Alpha-
CC 1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferaseV;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_533";
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DR EMBL; D17716; BAA04570.1; -; mRNA.
DR EMBL; AF113921; AAD22449.1; -; mRNA.
DR EMBL; CH471058; EAX11657.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11658.1; -; Genomic_DNA.
DR CCDS; CCDS2171.1; -.
DR PIR; JC2074; JC2074.
DR RefSeq; NP_002401.1; NM_002410.4.
DR RefSeq; XP_005263725.1; XM_005263668.4.
DR RefSeq; XP_005263726.1; XM_005263669.4.
DR RefSeq; XP_005263727.1; XM_005263670.3.
DR RefSeq; XP_006712597.1; XM_006712534.3.
DR RefSeq; XP_011509501.1; XM_011511199.2.
DR RefSeq; XP_011509502.1; XM_011511200.1.
DR RefSeq; XP_011509503.1; XM_011511201.2.
DR RefSeq; XP_011509504.1; XM_011511202.1.
DR RefSeq; XP_016859636.1; XM_017004147.1.
DR RefSeq; XP_016859637.1; XM_017004148.1.
DR PDB; 5ZIB; X-ray; 1.90 A; A=121-741.
DR PDB; 5ZIC; X-ray; 2.10 A; A/B=213-329, A/B=345-741.
DR PDB; 6YJQ; X-ray; 1.90 A; AAA/BBB=214-328, AAA/BBB=346-741.
DR PDB; 6YJR; X-ray; 2.20 A; AAA/BBB=214-741.
DR PDB; 6YJS; X-ray; 1.60 A; AAA/BBB=214-741.
DR PDB; 6YJT; X-ray; 1.70 A; AAA/BBB=214-741.
DR PDB; 6YJU; X-ray; 1.96 A; AAA/BBB=214-741.
DR PDB; 6YJV; X-ray; 1.70 A; AAA/BBB=214-741.
DR PDBsum; 5ZIB; -.
DR PDBsum; 5ZIC; -.
DR PDBsum; 6YJQ; -.
DR PDBsum; 6YJR; -.
DR PDBsum; 6YJS; -.
DR PDBsum; 6YJT; -.
DR PDBsum; 6YJU; -.
DR PDBsum; 6YJV; -.
DR AlphaFoldDB; Q09328; -.
DR SMR; Q09328; -.
DR BioGRID; 110405; 64.
DR CORUM; Q09328; -.
DR IntAct; Q09328; 16.
DR STRING; 9606.ENSP00000386377; -.
DR ChEMBL; CHEMBL1795131; -.
DR CAZy; GT18; Glycosyltransferase Family 18.
DR GlyGen; Q09328; 7 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q09328; -.
DR PhosphoSitePlus; Q09328; -.
DR BioMuta; MGAT5; -.
DR DMDM; 1169980; -.
DR EPD; Q09328; -.
DR jPOST; Q09328; -.
DR MassIVE; Q09328; -.
DR MaxQB; Q09328; -.
DR PaxDb; Q09328; -.
DR PeptideAtlas; Q09328; -.
DR PRIDE; Q09328; -.
DR ProteomicsDB; 58719; -.
DR Antibodypedia; 33554; 161 antibodies from 25 providers.
DR DNASU; 4249; -.
DR Ensembl; ENST00000281923.4; ENSP00000281923.2; ENSG00000152127.9.
DR Ensembl; ENST00000409645.5; ENSP00000386377.1; ENSG00000152127.9.
DR GeneID; 4249; -.
DR KEGG; hsa:4249; -.
DR MANE-Select; ENST00000281923.4; ENSP00000281923.2; NM_002410.5; NP_002401.1.
DR UCSC; uc002ttw.5; human.
DR CTD; 4249; -.
DR DisGeNET; 4249; -.
DR GeneCards; MGAT5; -.
DR HGNC; HGNC:7049; MGAT5.
DR HPA; ENSG00000152127; Low tissue specificity.
DR MIM; 601774; gene.
DR neXtProt; NX_Q09328; -.
DR OpenTargets; ENSG00000152127; -.
DR PharmGKB; PA30784; -.
DR VEuPathDB; HostDB:ENSG00000152127; -.
DR eggNOG; ENOG502QTNG; Eukaryota.
DR GeneTree; ENSGT00940000153470; -.
DR HOGENOM; CLU_016749_1_0_1; -.
DR InParanoid; Q09328; -.
DR OMA; DGRRKHC; -.
DR OrthoDB; 179031at2759; -.
DR PhylomeDB; Q09328; -.
DR TreeFam; TF313714; -.
DR BioCyc; MetaCyc:HS07793-MON; -.
DR BRENDA; 2.4.1.155; 2681.
DR PathwayCommons; Q09328; -.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR Reactome; R-HSA-975577; N-Glycan antennae elongation.
DR SignaLink; Q09328; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 4249; 8 hits in 1077 CRISPR screens.
DR ChiTaRS; MGAT5; human.
DR GeneWiki; MGAT5; -.
DR GenomeRNAi; 4249; -.
DR Pharos; Q09328; Tbio.
DR PRO; PR:Q09328; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q09328; protein.
DR Bgee; ENSG00000152127; Expressed in renal glomerulus and 188 other tissues.
DR Genevisible; Q09328; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0030144; F:alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:ARUK-UCL.
DR GO; GO:1903614; P:negative regulation of protein tyrosine phosphatase activity; IDA:ARUK-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:ARUK-UCL.
DR GO; GO:1904894; P:positive regulation of receptor signaling pathway via STAT; IDA:ARUK-UCL.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:ARUK-UCL.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IDA:UniProtKB.
DR GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR InterPro; IPR027833; DUF4525.
DR InterPro; IPR026116; GlyclTrfase_18.
DR Pfam; PF15027; DUF4525; 1.
DR Pfam; PF15024; Glyco_transf_18; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW Secreted; Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..741
FT /note="Alpha-1,6-mannosylglycoprotein 6-beta-N-
FT acetylglucosaminyltransferase A"
FT /id="PRO_0000080522"
FT CHAIN 31..741
FT /note="Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-
FT acetylglucosaminyltransferase A"
FT /evidence="ECO:0000305"
FT /id="PRO_0000445692"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..741
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:17142794"
FT REGION 213..741
FT /note="Sufficient for catalytic activity"
FT /evidence="ECO:0000269|PubMed:30140003"
FT REGION 264..269
FT /note="Important for activity in FGF2 release"
FT /evidence="ECO:0000269|PubMed:11872751"
FT BINDING 378..379
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30140003"
FT BINDING 526
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:30140003"
FT BINDING 554
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:30140003"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:30140003,
FT ECO:0007744|PDB:5ZIB"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 145..183
FT /evidence="ECO:0000269|PubMed:30140003,
FT ECO:0007744|PDB:5ZIB"
FT DISULFID 156..196
FT /evidence="ECO:0000269|PubMed:30140003,
FT ECO:0007744|PDB:5ZIB"
FT DISULFID 172..338
FT /evidence="ECO:0000269|PubMed:30140003,
FT ECO:0007744|PDB:5ZIB"
FT DISULFID 372..626
FT /evidence="ECO:0000269|PubMed:30140003,
FT ECO:0007744|PDB:5ZIB, ECO:0007744|PDB:5ZIC"
FT DISULFID 649..724
FT /evidence="ECO:0000269|PubMed:30140003,
FT ECO:0007744|PDB:5ZIB, ECO:0007744|PDB:5ZIC"
FT DISULFID 653..726
FT /evidence="ECO:0000269|PubMed:30140003,
FT ECO:0007744|PDB:5ZIB, ECO:0007744|PDB:5ZIC"
FT DISULFID 660..713
FT /evidence="ECO:0000269|PubMed:30140003,
FT ECO:0007744|PDB:5ZIB, ECO:0007744|PDB:5ZIC"
FT DISULFID 681..702
FT /evidence="ECO:0000269|PubMed:30140003,
FT ECO:0007744|PDB:5ZIB, ECO:0007744|PDB:5ZIC"
FT DISULFID 737..740
FT /evidence="ECO:0000269|PubMed:30140003,
FT ECO:0007744|PDB:5ZIB, ECO:0007744|PDB:5ZIC"
FT MUTAGEN 29
FT /note="L->D: No effect on the biosynthesis of the secreted
FT form."
FT /evidence="ECO:0000269|PubMed:17142794"
FT MUTAGEN 30
FT /note="L->D: No effect on the biosynthesis of the secreted
FT form."
FT /evidence="ECO:0000269|PubMed:17142794"
FT MUTAGEN 31
FT /note="H->A: No effect on the biosynthesis of the secreted
FT form."
FT /evidence="ECO:0000269|PubMed:17142794"
FT MUTAGEN 280
FT /note="E->A: Decreased catalytic activity."
FT /evidence="ECO:0000269|PubMed:30140003"
FT MUTAGEN 287
FT /note="E->A: Decreased catalytic activity."
FT /evidence="ECO:0000269|PubMed:30140003"
FT MUTAGEN 297
FT /note="E->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:30140003"
FT MUTAGEN 429
FT /note="E->A: Decreased catalytic activity."
FT /evidence="ECO:0000269|PubMed:30140003"
FT MUTAGEN 520
FT /note="E->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:30140003"
FT MUTAGEN 526
FT /note="E->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:30140003"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:5ZIC"
FT HELIX 236..259
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:5ZIC"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:5ZIC"
FT HELIX 296..310
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 321..327
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 353..363
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 364..373
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 389..394
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 434..440
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 463..470
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 499..507
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 523..529
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 533..543
FT /evidence="ECO:0007829|PDB:5ZIB"
FT TURN 545..547
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 549..551
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 560..563
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 565..570
FT /evidence="ECO:0007829|PDB:5ZIB"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 584..595
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 605..607
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 609..622
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 625..629
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 635..637
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 638..643
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 649..654
FT /evidence="ECO:0007829|PDB:5ZIB"
FT TURN 655..657
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 662..667
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:5ZIC"
FT HELIX 671..675
FT /evidence="ECO:0007829|PDB:5ZIB"
FT TURN 676..678
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 682..687
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 693..696
FT /evidence="ECO:0007829|PDB:5ZIB"
FT TURN 697..700
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 701..707
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 708..710
FT /evidence="ECO:0007829|PDB:5ZIB"
FT STRAND 718..727
FT /evidence="ECO:0007829|PDB:5ZIB"
FT HELIX 738..740
FT /evidence="ECO:0007829|PDB:5ZIB"
SQ SEQUENCE 741 AA; 84543 MW; 1073F8E67AD0E23B CRC64;
MALFTPWKLS SQKLGFFLVT FGFIWGMMLL HFTIQQRTQP ESSSMLREQI LDLSKRYIKA
LAEENRNVVD GPYAGVMTAY DLKKTLAVLL DNILQRIGKL ESKVDNLVVN GTGTNSTNST
TAVPSLVALE KINVADIING AQEKCVLPPM DGYPHCEGKI KWMKDMWRSD PCYADYGVDG
STCSFFIYLS EVENWCPHLP WRAKNPYEEA DHNSLAEIRT DFNILYSMMK KHEEFRWMRL
RIRRMADAWI QAIKSLAEKQ NLEKRKRKKV LVHLGLLTKE SGFKIAETAF SGGPLGELVQ
WSDLITSLYL LGHDIRISAS LAELKEIMKK VVGNRSGCPT VGDRIVELIY IDIVGLAQFK
KTLGPSWVHY QCMLRVLDSF GTEPEFNHAN YAQSKGHKTP WGKWNLNPQQ FYTMFPHTPD
NSFLGFVVEQ HLNSSDIHHI NEIKRQNQSL VYGKVDSFWK NKKIYLDIIH TYMEVHATVY
GSSTKNIPSY VKNHGILSGR DLQFLLRETK LFVGLGFPYE GPAPLEAIAN GCAFLNPKFN
PPKSSKNTDF FIGKPTLREL TSQHPYAEVF IGRPHVWTVD LNNQEEVEDA VKAILNQKIE
PYMPYEFTCE GMLQRINAFI EKQDFCHGQV MWPPLSALQV KLAEPGQSCK QVCQESQLIC
EPSFFQHLNK DKDMLKYKVT CQSSELAKDI LVPSFDPKNK HCVFQGDLLL FSCAGAHPRH
QRVCPCRDFI KGQVALCKDC L
