ID A0A385Z7H9_CALGI Unreviewed; 477 AA. AC A0A385Z7H9; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 29-MAY-2024, entry version 16. DE RecName: Full=Glycosyltransferase {ECO:0000256|RuleBase:RU362057}; DE EC=2.4.1.- {ECO:0000256|RuleBase:RU362057}; OS Calotropis gigantea (Giant milkweed) (Asclepias gigantea). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Gentianales; Apocynaceae; Asclepiadoideae; Asclepiadeae; OC Asclepiadinae; Calotropis. OX NCBI_TaxID=4066 {ECO:0000313|EMBL:AYC35243.1}; RN [1] {ECO:0000313|EMBL:AYC35243.1} RP NUCLEOTIDE SEQUENCE. RA Wen C., Huang W., Zhu X.-L., Zhang F., Jiang R.-W.; RT "Probing the Catalytic Promiscuity of a Novel Steroid Glycosyltransferase RT from Asclepias curassavica, an Evolvable Enzyme from the UGT74AN RT Subfamily."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:7W09, ECO:0007829|PDB:7W0K} RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH UDP AND RP UDP-ALPHA-D-GLUCOSE, AND GLYCOSYLATION AT GLY-23; TRP-371 AND GLN-393. RX DOI=10.1021/acscatal.1c05729; RA Huang W., He Y., Jiang R., Deng Z., Long F.; RT "Functional and Structural Dissection of a Plant Steroid 3-O- RT Glycosyltransferase Facilitated the Engineering Enhancement of Sugar Donor RT Promiscuity."; RL ACS Catal. 0:2927-2937(2022). CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family. CC {ECO:0000256|ARBA:ARBA00009995, ECO:0000256|RuleBase:RU003718}. 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; MF942417; AYC35243.1; -; mRNA. DR PDB; 7W09; X-ray; 1.95 A; A=1-477. DR PDB; 7W0K; X-ray; 2.04 A; A=1-477. DR PDB; 7W0Z; X-ray; 2.10 A; A=1-477. DR PDB; 7W10; X-ray; 2.15 A; A=1-477. DR PDB; 7W11; X-ray; 2.45 A; A=1-477. DR PDB; 7W1B; X-ray; 2.15 A; A=1-477. DR PDB; 7W1H; X-ray; 2.15 A; A=1-477. DR AlphaFoldDB; A0A385Z7H9; -. DR SMR; A0A385Z7H9; -. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0080043; F:quercetin 3-O-glucosyltransferase activity; IEA:TreeGrafter. DR GO; GO:0080044; F:quercetin 7-O-glucosyltransferase activity; IEA:TreeGrafter. DR CDD; cd03784; GT1_Gtf-like; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR InterPro; IPR002213; UDP_glucos_trans. DR InterPro; IPR035595; UDP_glycos_trans_CS. DR PANTHER; PTHR11926; GLUCOSYL/GLUCURONOSYL TRANSFERASES; 1. DR PANTHER; PTHR11926:SF1539; UDP-GLYCOSYLTRANSFERASE 74E1-RELATED; 1. DR Pfam; PF00201; UDPGT; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. DR PROSITE; PS00375; UDPGT; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:7W09, ECO:0007829|PDB:7W0K}; KW Glycosyltransferase {ECO:0000256|RuleBase:RU003718}; KW Nucleotide-binding {ECO:0007829|PDB:7W0K, ECO:0007829|PDB:7W0Z}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003718}. FT BINDING 24 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0007829|PDB:7W1H" FT BINDING 26 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0007829|PDB:7W0K, ECO:0007829|PDB:7W0Z" FT BINDING 26 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0007829|PDB:7W1H" FT BINDING 141 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0007829|PDB:7W1H" FT BINDING 258 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0007829|PDB:7W0K, ECO:0007829|PDB:7W1B" FT BINDING 283 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0007829|PDB:7W0K, ECO:0007829|PDB:7W0Z" FT BINDING 283 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0007829|PDB:7W1H" FT BINDING 350 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0007829|PDB:7W1H" FT BINDING 351 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0007829|PDB:7W0K, ECO:0007829|PDB:7W0Z" FT BINDING 351 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0007829|PDB:7W1H" FT BINDING 353 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0007829|PDB:7W10, ECO:0007829|PDB:7W1B" FT BINDING 353 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0007829|PDB:7W1H" FT BINDING 368 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0007829|PDB:7W0K, ECO:0007829|PDB:7W0Z" FT BINDING 371 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0007829|PDB:7W1H" FT BINDING 372 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0007829|PDB:7W0K, ECO:0007829|PDB:7W0Z" FT BINDING 372 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0007829|PDB:7W1H" FT BINDING 373 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0007829|PDB:7W0K, ECO:0007829|PDB:7W0Z" FT BINDING 373 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0007829|PDB:7W1H" FT BINDING 376 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0007829|PDB:7W0K, ECO:0007829|PDB:7W0Z" FT BINDING 376 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0007829|PDB:7W1H" FT BINDING 392 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0007829|PDB:7W1H" FT BINDING 393 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0007829|PDB:7W1H" FT CARBOHYD 23 FT /note="Glucose" FT /evidence="ECO:0007829|PDB:7W11" FT CARBOHYD 371 FT /note="Glucose" FT /evidence="ECO:0007829|PDB:7W11" FT CARBOHYD 393 FT /note="Glucose" FT /evidence="ECO:0007829|PDB:7W11" SQ SEQUENCE 477 AA; 53617 MW; A837611F8AED2833 CRC64; MGTIEISSPS KTHILAFPFP EKGHINPMLH LCNRLASKGF RVTLITTIST YKDVKNKIKC KSKGGLINLE SIPDGTDKNL GMNGYFNQFK NSVTESVAGI IEEYKLGHDF PPPKVLIYDS TMPWMLDVAH GHGILGASLF TQPCCVSVVY YHMLQGTIDF HREQSSSSKV LLLPCLPPLE DRDLPEFDYF KEDSGFVSNL LLNQFLNIDK IDYVLFNTFE MLESEIANWM SNKWKILTIG PTAPTAAAAA AANNYLFETN TEVCMKWLDE REPNSVIYVS FGSIASLTEQ QMEEISQALF TTNFNFLWVV REEERTKLPN CLNNNNNNNN NPSSESFTTA AGKLGLIINW CPQLDVLRHE SVACFMTHCG WNSTLEAISS GVPMICVPQW VDQTTNAKFI QDVWKIGVRV NNNNGENGGL VKKEEIERCI KEVCESEKGK ELKRNAMKWK DLSKEAVSEG GSSDTNLEYF ASTLLFY //