MALQ_THELN
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 03-AUG-2022, entry version 119.
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}.
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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 PRIDE; O32462; -.
DR EnsemblBacteria; EHR79231; EHR79231; OCC_10078.
DR GeneID; 16548782; -.
DR KEGG; tlt:OCC_10078; -.
DR HOGENOM; CLU_026700_0_0_2; -.
DR OMA; HFMSAGL; -.
DR OrthoDB; 3280at2157; -.
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 Gene3D; 2.70.98.10; -; 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 Pfam; PF09094; DUF1925; 1.
DR Pfam; PF09095; DUF1926; 1.
DR Pfam; PF03065; Glyco_hydro_57; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 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
