ID MALQ_THELN Reviewed; 659 AA. AC O32462; H3ZLH6; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 125. 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=jgt; ORFNames=OCC_10078; OS Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=523849; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19 AND 427-437, RP AND CHARACTERIZATION. RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C; RX PubMed=9310375; DOI=10.1111/j.1432-1033.1997.00171.x; RA Jeon B.-S., Taguchi H., Sakai H., Ohshima T., Wakagi T., Matsuzawa H.; RT "4-alpha-glucanotransferase from the hyperthermophilic archaeon RT Thermococcus litoralis. Enzyme purification and characterization, and gene RT cloning, sequencing and expression in Escherichia coli."; RL Eur. J. Biochem. 248:171-178(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C; RX PubMed=22493191; DOI=10.1128/jb.00123-12; RA Gardner A.F., Kumar S., Perler F.B.; RT "Genome sequence of the model hyperthermophilic archaeon Thermococcus RT litoralis NS-C."; RL J. Bacteriol. 194:2375-2376(2012). RN [3] RP PROTEIN SEQUENCE OF 1-35, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, SUBUNIT, AND INDUCTION. RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C; RX PubMed=10348846; DOI=10.1128/jb.181.11.3358-3367.1999; RA Xavier K.B., Peist R., Kossmann M., Boos W., Santos H.; RT "Maltose metabolism in the hyperthermophilic archaeon Thermococcus RT litoralis: purification and characterization of key enzymes."; RL J. Bacteriol. 181:3358-3367(1999). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=12618437; DOI=10.1074/jbc.m213134200; RA Imamura H., Fushinobu S., Yamamoto M., Kumasaka T., Jeon B.S., Wakagi T., RA Matsuzawa H.; RT "Crystal structures of 4-alpha-glucanotransferase from Thermococcus RT litoralis and its complex with an inhibitor."; RL J. Biol. Chem. 278:19378-19386(2003). CC -!- FUNCTION: Catalyzes the transglycosylation of maltooligosaccharides, CC yielding maltooligosaccharides of various lengths and glucose. Maltose CC and glucose can be used as acceptors in the transfer reaction. CC {ECO:0000269|PubMed:10348846}. 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; Evidence={ECO:0000269|PubMed:10348846}; CC -!- ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoic acid, CC monoiodoacetic acid, mercury and nickel ions. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC Vmax=13 umol/min/mg enzyme with maltose as substrate CC {ECO:0000269|PubMed:10348846}; CC Vmax=26 umol/min/mg enzyme with maltotriose as substrate CC {ECO:0000269|PubMed:10348846}; CC Temperature dependence: CC Optimum temperature is 85-100 degrees Celsius. CC {ECO:0000269|PubMed:10348846}; CC -!- SUBUNIT: homodimer. {ECO:0000269|PubMed:10348846}. CC -!- INDUCTION: Expressed constitutively. {ECO:0000269|PubMed:10348846}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family. {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; D88253; BAA22063.1; -; Genomic_DNA. DR EMBL; CP006670; EHR79231.1; -; Genomic_DNA. DR RefSeq; WP_004067291.1; NC_022084.1. DR PDB; 1K1W; X-ray; 2.80 A; A=1-659. DR PDB; 1K1X; X-ray; 2.40 A; A/B=1-659. DR PDB; 1K1Y; X-ray; 2.40 A; A/B=1-659. DR PDBsum; 1K1W; -. DR PDBsum; 1K1X; -. DR PDBsum; 1K1Y; -. DR AlphaFoldDB; O32462; -. DR SMR; O32462; -. DR STRING; 523849.OCC_10078; -. DR CAZy; GH57; Glycoside Hydrolase Family 57. DR PaxDb; 523849-OCC_10078; -. DR GeneID; 16548782; -. DR KEGG; tlt:OCC_10078; -. DR HOGENOM; CLU_026700_0_0_2; -. DR OrthoDB; 18576at2157; -. DR BRENDA; 2.4.1.25; 6302. DR EvolutionaryTrace; O32462; -. DR PRO; PR:O32462; -. DR Proteomes; UP000015502; Chromosome. 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:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR CDD; cd10793; GH57N_TLGT_like; 1. DR Gene3D; 2.70.98.10; -; 1. DR Gene3D; 3.20.110.20; -; 1. DR InterPro; IPR015179; A-amylase/a-glucTrfase_C. DR InterPro; IPR015178; A-amylase/a-glucTrfase_central. DR InterPro; IPR011013; Gal_mutarotase_sf_dom. DR InterPro; IPR014718; GH-type_carb-bd. DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl. DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf. DR InterPro; IPR004300; Glyco_hydro_57_N. DR PANTHER; PTHR36306:SF1; 4-ALPHA-GLUCANOTRANSFERASE; 1. DR PANTHER; PTHR36306; ALPHA-AMYLASE-RELATED-RELATED; 1. DR Pfam; PF09094; AmyA-A_glucT_m; 1. DR Pfam; PF09095; AmyA-gluTrfs_C; 1. DR Pfam; PF03065; Glyco_hydro_57; 1. DR SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1. DR SUPFAM; SSF74650; Galactose mutarotase-like; 1. DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing; KW Glycosyltransferase; Transferase. FT CHAIN 1..659 FT /note="4-alpha-glucanotransferase" FT /id="PRO_0000184577" FT ACT_SITE 123 FT /note="Nucleophile" FT ACT_SITE 214 FT /note="Proton donor" FT STRAND 4..12 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 20..29 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 31..38 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 46..50 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 52..61 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 63..74 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 78..82 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 95..111 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 122..124 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 130..136 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 141..145 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 146..152 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 163..167 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 170..177 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 179..184 FT /evidence="ECO:0007829|PDB:1K1X" FT TURN 185..187 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 190..198 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 208..214 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 215..217 FT /evidence="ECO:0007829|PDB:1K1X" FT TURN 218..220 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 224..228 FT /evidence="ECO:0007829|PDB:1K1X" FT TURN 229..231 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 233..243 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 247..249 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 252..258 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 274..278 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 282..296 FT /evidence="ECO:0007829|PDB:1K1X" FT TURN 297..299 FT /evidence="ECO:0007829|PDB:1K1X" FT TURN 302..304 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 313..315 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 316..319 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 321..337 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 341..350 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 353..356 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 359..361 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 363..365 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 367..381 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 389..391 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 393..398 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 400..404 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 406..412 FT /evidence="ECO:0007829|PDB:1K1X" FT TURN 414..418 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 420..425 FT /evidence="ECO:0007829|PDB:1K1X" FT TURN 426..429 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 442..444 FT /evidence="ECO:0007829|PDB:1K1W" FT HELIX 472..475 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 487..493 FT /evidence="ECO:0007829|PDB:1K1X" FT HELIX 499..503 FT /evidence="ECO:0007829|PDB:1K1X" FT TURN 504..506 FT /evidence="ECO:0007829|PDB:1K1Y" FT STRAND 514..516 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 519..523 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 526..552 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 555..566 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 570..578 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 588..599 FT /evidence="ECO:0007829|PDB:1K1X" FT TURN 600..603 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 604..627 FT /evidence="ECO:0007829|PDB:1K1X" FT STRAND 630..658 FT /evidence="ECO:0007829|PDB:1K1X" SQ SEQUENCE 659 AA; 77885 MW; F789AFF9BF8281AC CRC64; MERINFIFGI HNHQPLGNFG WVFEEAYNRS YRPFMEILEE FPEMKVNVHF SGPLLEWIEE NKPDYLDLLR SLIKRGQLEI VVAGFYEPVL AAIPKEDRLV QIEMLKDYAR KLGYDAKGVW LTERVWQPEL VKSLREAGIE YVVVDDYHFM SAGLSKEELF WPYYTEDGGE VITVFPIDEK LRYLIPFRPV KKTIEYLESL TSDDPSKVAV FHDDGEKFGV WPGTYEWVYE KGWLREFFDA ITSNEKINLM TYSEYLSKFT PRGLVYLPIA SYFEMSEWSL PAKQAKLFVE FVEQLKEEGK FEKYRVFVRG GIWKNFFFKY PESNFMHKRM LMVSKAVRDN PEARKYILKA QCNDAYWHGV FGGIYLPHLR RTVWENIIKA QRYLKPENKI LDVDFDGRAE IMVENDGFIA TIKPHYGGSI FELSSKRKAV NYNDVLPRRW EHYHEVPEAT KPEKESEEGI ASIHELGKQI PEEIRRELAY DWQLRAILQD HFIKPEETLD NYRLVKYHEL GDFVNQPYEY EMIENGVKLW REGGVYAEEK IPARVEKKIE LTEDGFIAKY RVLLEKPYKA LFGVEINLAV HSVMEKPEEF EAKEFEVNDP YGIGKVRIEL DKAAKVWKFP IKTLSQSEAG WDFIQQGVSY TMLFPIEKEL EFTVRFREL //