ID MALQ_SYNY3 Reviewed; 505 AA. AC P72785; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 130. DE RecName: Full=4-alpha-glucanotransferase; DE EC=2.4.1.25; DE AltName: Full=Amylomaltase; DE AltName: Full=Disproportionating enzyme; DE Short=D-enzyme; GN Name=malQ; OrderedLocusNames=sll1676; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). CC -!- CATALYTIC ACTIVITY: CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new CC position in an acceptor, which may be glucose or a (1->4)-alpha-D- CC glucan.; EC=2.4.1.25; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the disproportionating enzyme family. CC {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; BA000022; BAA16800.1; -; Genomic_DNA. DR PIR; S74648; S74648. DR AlphaFoldDB; P72785; -. DR SMR; P72785; -. DR IntAct; P72785; 1. DR STRING; 1148.gene:10497656; -. DR CAZy; GH77; Glycoside Hydrolase Family 77. DR PaxDb; 1148-1651873; -. DR EnsemblBacteria; BAA16800; BAA16800; BAA16800. DR KEGG; syn:sll1676; -. DR eggNOG; COG1640; Bacteria. DR InParanoid; P72785; -. DR PhylomeDB; P72785; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR003385; Glyco_hydro_77. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR NCBIfam; TIGR00217; malQ; 1. DR PANTHER; PTHR32438; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC/AMYLOPLASTIC; 1. DR PANTHER; PTHR32438:SF5; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC_AMYLOPLASTIC; 1. DR Pfam; PF02446; Glyco_hydro_77; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cytoplasm; Glycosyltransferase; KW Reference proteome; Transferase. FT CHAIN 1..505 FT /note="4-alpha-glucanotransferase" FT /id="PRO_0000170131" SQ SEQUENCE 505 AA; 57180 MW; 488623C9FA4C9D59 CRC64; MLDKRCSGIL LHPTSLPSRF GIGDLGDGAF QFIDFLADAD QSVWQILPLG PTGFGNSPYL CYSALAINPW LISLDRLAEE GFLPPSLLDQ APPFTNPRVD YDQAIAYKSQ VLKQAFAQFR TNIELAIEQE FAEFCQAQSD WLADYALFMA IKEAHNGAGW HQWDKDIAWR EPEALKIWGD RLKTEVLYHQ FLQFLGFRQW QEVKAYANQR HIAIFGDLPI YVAHDSADVW ANPENFCLDP ETGEAAMMAG VPPDYFSATG QLWGNPVYDW ETLKATGFAW WIKRFKANLQ YLDIVRIDHF RGFESYWGVP QGEKTAENGE WYPAPGKEFF QALGKALGDN LPIVAEDLGV ITPEVEALRD EFNFPGMKVL HFAFDSDRGN PFLPFNYSNG NAVVYTGTHD NDTTVGWFQE RSEDDQQKVI NYLGCVCNEG IHWSLIRLAS SSVAALAIFP LQDILGLGSD CRMNLPGTAA GNWGWRYHPD QLNDWLSGHL SFITELYGRR IYHTD //