ID TGT_HUMAN Reviewed; 403 AA. AC Q9BXR0; B4DFM7; Q96BQ4; Q9BXQ9; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 3. DT 27-MAR-2024, entry version 183. DE RecName: Full=Queuine tRNA-ribosyltransferase catalytic subunit 1 {ECO:0000255|HAMAP-Rule:MF_03218}; DE EC=2.4.2.64 {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:20354154}; DE AltName: Full=Guanine insertion enzyme {ECO:0000255|HAMAP-Rule:MF_03218}; DE AltName: Full=tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_03218}; GN Name=QTRT1 {ECO:0000255|HAMAP-Rule:MF_03218}; Synonyms=TGT, TGUT; 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] (ISOFORM 1), FUNCTION, AND PATHWAY. RC TISSUE=Spleen; RX PubMed=11255023; DOI=10.1016/s0378-1119(01)00368-7; RA Deshpande K.L., Katze J.R.; RT "Characterization of cDNA encoding the human tRNA-guanine transglycosylase RT (TGT) catalytic subunit."; RL Gene 265:205-212(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Amygdala; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-403 (ISOFORM 1). RC TISSUE=Brain; 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 [5] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, RP MUTAGENESIS OF ASP-279, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=20354154; DOI=10.1261/rna.1997610; RA Chen Y.C., Kelly V.P., Stachura S.V., Garcia G.A.; RT "Characterization of the human tRNA-guanine transglycosylase: confirmation RT of the heterodimeric subunit structure."; RL RNA 16:958-968(2010). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [9] RP FUNCTION. RX PubMed=30093495; DOI=10.15252/embj.201899777; RA Tuorto F., Legrand C., Cirzi C., Federico G., Liebers R., Mueller M., RA Ehrenhofer-Murray A.E., Dittmar G., Groene H.J., Lyko F.; RT "Queuosine-modified tRNAs confer nutritional control of protein RT translation."; RL EMBO J. 37:0-0(2018). RN [10] RP FUNCTION. RX PubMed=34009357; DOI=10.1093/nar/gkab289; RA Fergus C., Al-Qasem M., Cotter M., McDonnell C.M., Sorrentino E., RA Chevot F., Hokamp K., Senge M.O., Southern J.M., Connon S.J., Kelly V.P.; RT "The human tRNA-guanine transglycosylase displays promiscuous nucleobase RT preference but strict tRNA specificity."; RL Nucleic Acids Res. 49:4877-4890(2021). RN [11] {ECO:0007744|PDB:6H42, ECO:0007744|PDB:6H45} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 12-403 IN COMPLEX WITH ZINC AND RP QUEUINE, COFACTOR, AND SUBUNIT. RX PubMed=30149595; DOI=10.3390/biom8030081; RA Johannsson S., Neumann P., Ficner R.; RT "Crystal Structure of the Human tRNA Guanine Transglycosylase Catalytic RT Subunit QTRT1."; RL Biomolecules 8:0-0(2018). RN [12] {ECO:0007744|PDB:7NQ4} RP X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) IN COMPLEX WITH QTRT2; QUEUINE AND RP ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT. RX PubMed=34241577; DOI=10.1080/15476286.2021.1950980; RA Sievers K., Welp L., Urlaub H., Ficner R.; RT "Structural and functional insights into human tRNA guanine RT transgylcosylase."; RL RNA Biol. 18:382-396(2021). CC -!- FUNCTION: Catalytic subunit of the queuine tRNA-ribosyltransferase CC (TGT) that catalyzes the base-exchange of a guanine (G) residue with CC queuine (Q) at position 34 (anticodon wobble position) in tRNAs with CC GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the CC hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- CC cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (PubMed:11255023, CC PubMed:20354154, PubMed:34009357, PubMed:34241577). Catalysis occurs CC through a double-displacement mechanism. The nucleophile active site CC attacks the C1' of nucleotide 34 to detach the guanine base from the CC RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor CC active site deprotonates the incoming queuine, allowing a nucleophilic CC attack on the C1' of the ribose to form the product (By similarity). CC Modification of cytoplasmic tRNAs with queuosine controls the CC elongation speed of cognate codons, thereby ensuring the correct CC folding of nascent proteins to maintain proteome integrity CC (PubMed:30093495). {ECO:0000255|HAMAP-Rule:MF_03218, CC ECO:0000269|PubMed:11255023, ECO:0000269|PubMed:20354154, CC ECO:0000269|PubMed:30093495, ECO:0000269|PubMed:34009357, CC ECO:0000269|PubMed:34241577}. CC -!- CATALYTIC ACTIVITY: CC Reaction=guanosine(34) in tRNA + queuine = guanine + queuosine(34) in CC tRNA; Xref=Rhea:RHEA:16633, Rhea:RHEA-COMP:10341, Rhea:RHEA- CC COMP:18571, ChEBI:CHEBI:16235, ChEBI:CHEBI:17433, ChEBI:CHEBI:74269, CC ChEBI:CHEBI:194431; EC=2.4.2.64; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03218, ECO:0000269|PubMed:20354154, CC ECO:0000269|PubMed:34241577}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03218, ECO:0000269|PubMed:30149595, CC ECO:0000269|PubMed:34241577}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.34 uM for tRNA(Tyr) {ECO:0000269|PubMed:20354154}; CC KM=0.41 uM for guanine {ECO:0000269|PubMed:20354154}; CC Note=kcat is 0.0056 sec(-1) with tRNA(Tyr) as substrate and 0.00586 CC sec(-1) with guanine as substrate. {ECO:0000269|PubMed:20354154}; CC -!- SUBUNIT: Heterodimer of a catalytic subunit QTRT1 and an accessory CC subunit QTRT2. {ECO:0000255|HAMAP-Rule:MF_03218, CC ECO:0000269|PubMed:20354154, ECO:0000269|PubMed:30149595, CC ECO:0000269|PubMed:34241577}. CC -!- INTERACTION: CC Q9BXR0; Q9H974: QTRT2; NbExp=2; IntAct=EBI-716832, EBI-1221028; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03218}. CC Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03218}; CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03218}; CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03218}. Note=Weakly CC associates with mitochondria, possibly via QTRT2. {ECO:0000255|HAMAP- CC Rule:MF_03218}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BXR0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BXR0-2; Sequence=VSP_056470, VSP_056471; CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. CC {ECO:0000255|HAMAP-Rule:MF_03218}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH15350.1; Type=Erroneous initiation; Evidence={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; AF302783; AAG60033.1; -; mRNA. DR EMBL; AF302784; AAG60034.1; -; mRNA. DR EMBL; AK294166; BAG57488.1; -; mRNA. DR EMBL; AC011475; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015350; AAH15350.1; ALT_INIT; mRNA. DR CCDS; CCDS12248.1; -. [Q9BXR0-1] DR RefSeq; NP_112486.1; NM_031209.2. [Q9BXR0-1] DR PDB; 6H42; X-ray; 2.45 A; A/B=11-403. DR PDB; 6H45; X-ray; 2.40 A; A/B=12-403. DR PDB; 7NQ4; X-ray; 2.88 A; A=1-403. DR PDBsum; 6H42; -. DR PDBsum; 6H45; -. DR PDBsum; 7NQ4; -. DR AlphaFoldDB; Q9BXR0; -. DR SMR; Q9BXR0; -. DR BioGRID; 123623; 39. DR ComplexPortal; CPX-6662; tRNA-guanine transglycosylase complex. DR IntAct; Q9BXR0; 19. DR STRING; 9606.ENSP00000250237; -. DR BindingDB; Q9BXR0; -. DR ChEMBL; CHEMBL6004; -. DR GlyGen; Q9BXR0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BXR0; -. DR PhosphoSitePlus; Q9BXR0; -. DR SwissPalm; Q9BXR0; -. DR BioMuta; QTRT1; -. DR DMDM; 239938842; -. DR EPD; Q9BXR0; -. DR jPOST; Q9BXR0; -. DR MassIVE; Q9BXR0; -. DR MaxQB; Q9BXR0; -. DR PaxDb; 9606-ENSP00000250237; -. DR PeptideAtlas; Q9BXR0; -. DR ProteomicsDB; 4060; -. DR ProteomicsDB; 79483; -. [Q9BXR0-1] DR Pumba; Q9BXR0; -. DR Antibodypedia; 25490; 181 antibodies from 20 providers. DR DNASU; 81890; -. DR Ensembl; ENST00000250237.10; ENSP00000250237.4; ENSG00000213339.9. [Q9BXR0-1] DR Ensembl; ENST00000421333.6; ENSP00000389126.2; ENSG00000213339.9. [Q9BXR0-2] DR GeneID; 81890; -. DR KEGG; hsa:81890; -. DR MANE-Select; ENST00000250237.10; ENSP00000250237.4; NM_031209.3; NP_112486.1. DR UCSC; uc002mpr.4; human. [Q9BXR0-1] DR AGR; HGNC:23797; -. DR CTD; 81890; -. DR DisGeNET; 81890; -. DR GeneCards; QTRT1; -. DR HGNC; HGNC:23797; QTRT1. DR HPA; ENSG00000213339; Low tissue specificity. DR MIM; 609615; gene. DR neXtProt; NX_Q9BXR0; -. DR OpenTargets; ENSG00000213339; -. DR PharmGKB; PA134963074; -. DR VEuPathDB; HostDB:ENSG00000213339; -. DR eggNOG; KOG3908; Eukaryota. DR GeneTree; ENSGT00530000063679; -. DR HOGENOM; CLU_022060_0_1_1; -. DR InParanoid; Q9BXR0; -. DR OMA; IDLFDCV; -. DR OrthoDB; 167782at2759; -. DR PhylomeDB; Q9BXR0; -. DR TreeFam; TF300732; -. DR BioCyc; MetaCyc:HS05270-MONOMER; -. DR BRENDA; 2.4.2.29; 2681. DR BRENDA; 2.4.2.64; 2681. DR PathwayCommons; Q9BXR0; -. DR Reactome; R-HSA-6782315; tRNA modification in the nucleus and cytosol. DR SignaLink; Q9BXR0; -. DR BioGRID-ORCS; 81890; 25 hits in 1158 CRISPR screens. DR ChiTaRS; QTRT1; human. DR GenomeRNAi; 81890; -. DR Pharos; Q9BXR0; Tbio. DR PRO; PR:Q9BXR0; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q9BXR0; Protein. DR Bgee; ENSG00000213339; Expressed in mucosa of transverse colon and 141 other cell types or tissues. DR ExpressionAtlas; Q9BXR0; baseline and differential. DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB. DR GO; GO:1990234; C:transferase complex; IPI:ComplexPortal. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0008479; F:tRNA-guanosine(34) queuine transglycosylase activity; IDA:UniProtKB. DR GO; GO:0006400; P:tRNA modification; TAS:UniProtKB. DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IDA:UniProtKB. DR Gene3D; 3.20.20.105; Queuine tRNA-ribosyltransferase-like; 1. DR HAMAP; MF_00168; Q_tRNA_Tgt; 1. DR InterPro; IPR004803; TGT. DR InterPro; IPR036511; TGT-like_sf. DR InterPro; IPR002616; tRNA_ribo_trans-like. DR NCBIfam; TIGR00430; Q_tRNA_tgt; 1. DR NCBIfam; TIGR00449; tgt_general; 1. DR PANTHER; PTHR43530; QUEUINE TRNA-RIBOSYLTRANSFERASE CATALYTIC SUBUNIT 1; 1. DR PANTHER; PTHR43530:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE CATALYTIC SUBUNIT 1; 1. DR Pfam; PF01702; TGT; 1. DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1. DR Genevisible; Q9BXR0; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Glycosyltransferase; Membrane; Metal-binding; Mitochondrion; KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome; KW Transferase; tRNA processing; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..403 FT /note="Queuine tRNA-ribosyltransferase catalytic subunit 1" FT /id="PRO_0000135565" FT REGION 260..266 FT /note="RNA binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218" FT REGION 284..288 FT /note="RNA binding; important for wobble base 34 FT recognition" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218" FT ACT_SITE 105 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218" FT ACT_SITE 279 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218" FT BINDING 105 FT /ligand="queuine" FT /ligand_id="ChEBI:CHEBI:17433" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218, FT ECO:0000269|PubMed:30149595, ECO:0000269|PubMed:34241577, FT ECO:0007744|PDB:6H45, ECO:0007744|PDB:7NQ4" FT BINDING 159 FT /ligand="queuine" FT /ligand_id="ChEBI:CHEBI:17433" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218, FT ECO:0000269|PubMed:30149595, ECO:0000269|PubMed:34241577, FT ECO:0007744|PDB:6H45, ECO:0007744|PDB:7NQ4" FT BINDING 202 FT /ligand="queuine" FT /ligand_id="ChEBI:CHEBI:17433" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218, FT ECO:0000269|PubMed:34241577, ECO:0007744|PDB:7NQ4" FT BINDING 229 FT /ligand="queuine" FT /ligand_id="ChEBI:CHEBI:17433" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218, FT ECO:0000269|PubMed:30149595, ECO:0000269|PubMed:34241577, FT ECO:0007744|PDB:6H45, ECO:0007744|PDB:7NQ4" FT BINDING 317 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218, FT ECO:0000269|PubMed:30149595, ECO:0000269|PubMed:34241577, FT ECO:0007744|PDB:6H45, ECO:0007744|PDB:7NQ4" FT BINDING 319 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218, FT ECO:0000269|PubMed:30149595, ECO:0000269|PubMed:34241577, FT ECO:0007744|PDB:6H45, ECO:0007744|PDB:7NQ4" FT BINDING 322 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218, FT ECO:0000269|PubMed:30149595, ECO:0000269|PubMed:34241577, FT ECO:0007744|PDB:6H45, ECO:0007744|PDB:7NQ4" FT BINDING 348 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218, FT ECO:0000269|PubMed:30149595, ECO:0000269|PubMed:34241577, FT ECO:0007744|PDB:6H45, ECO:0007744|PDB:7NQ4" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 139 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 178..225 FT /note="SIRWLDRCIAAHQRPDKQNLFAIIQGGLDADLRATCLEEMTKRDVPGF -> FT PLGLVTGALLQVNPLAGPVHCSPSAAGQAEPLRHYPGWAGRRSPGHLP (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056470" FT VAR_SEQ 226..403 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056471" FT MUTAGEN 279 FT /note="D->N: Loss of transglycosylase activity." FT /evidence="ECO:0000269|PubMed:20354154" FT STRAND 16..22 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 24..26 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 29..35 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 38..45 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 50..53 FT /evidence="ECO:0007829|PDB:7NQ4" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 59..64 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 77..82 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 83..88 FT /evidence="ECO:0007829|PDB:7NQ4" FT HELIX 91..96 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 100..104 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 108..114 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 115..117 FT /evidence="ECO:0007829|PDB:7NQ4" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:7NQ4" FT STRAND 125..128 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 135..138 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 140..150 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 153..156 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 169..187 FT /evidence="ECO:0007829|PDB:6H42" FT TURN 192..194 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 196..201 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 207..217 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 223..227 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 236..249 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 256..259 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 264..272 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 277..279 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 282..288 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 291..294 FT /evidence="ECO:0007829|PDB:6H42" FT STRAND 297..300 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 304..306 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 320..324 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 327..336 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 338..365 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 369..381 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 384..386 FT /evidence="ECO:0007829|PDB:6H42" FT HELIX 389..397 FT /evidence="ECO:0007829|PDB:6H42" SQ SEQUENCE 403 AA; 44048 MW; 1E30F3C7BF47A106 CRC64; MAGAATQASL ESAPRIMRLV AECSRSRARA GELWLPHGTV ATPVFMPVGT QATMKGITTE QLDALGCRIC LGNTYHLGLR PGPELIQKAN GLHGFMNWPH NLLTDSGGFQ MVSLVSLSEV TEEGVRFRSP YDGNETLLSP EKSVQIQNAL GSDIIMQLDD VVSSTVTGPR VEEAMYRSIR WLDRCIAAHQ RPDKQNLFAI IQGGLDADLR ATCLEEMTKR DVPGFAIGGL SGGESKSQFW RMVALSTSRL PKDKPRYLMG VGYATDLVVC VALGCDMFDC VFPTRTARFG SALVPTGNLQ LRKKVFEKDF GPIDPECTCP TCQKHSRAFL HALLHSDNTA ALHHLTVHNI AYQLQLMSAV RTSIVEKRFP DFVRDFMGAM YGDPTLCPTW ATDALASVGI TLG //