MGTA_THEMA
ID MGTA_THEMA Reviewed; 441 AA.
AC P80099;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 159.
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=mgtA; OrderedLocusNames=TM_0364;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-23, AND CHARACTERIZATION.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=1628664; DOI=10.1111/j.1432-1033.1992.tb17023.x;
RA Liebl W., Feil R., Gabelsberger J., Kellermann J., Schleifer K.-H.;
RT "Purification and characterization of a novel thermostable 4-alpha-
RT glucanotransferase of Thermotoga maritima cloned in Escherichia coli.";
RL Eur. J. Biochem. 207:81-88(1992).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=12139940; DOI=10.1016/s0022-2836(02)00570-3;
RA Roujeinikova A., Raasch C., Sedelnikova S., Liebl W., Rice D.W.;
RT "Crystal structure of Thermotoga maritima 4-alpha-glucanotransferase and
RT its acarbose complex: implications for substrate specificity and
RT catalysis.";
RL J. Mol. Biol. 321:149-162(2002).
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 1 Ca(2+) ion per subunit.;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35451.1; -; Genomic_DNA.
DR RefSeq; NP_228175.1; NC_000853.1.
DR RefSeq; WP_004083169.1; NZ_CP011107.1.
DR PDB; 1LWH; X-ray; 2.60 A; A/B=1-441.
DR PDB; 1LWJ; X-ray; 2.50 A; A/B=1-441.
DR PDBsum; 1LWH; -.
DR PDBsum; 1LWJ; -.
DR AlphaFoldDB; P80099; -.
DR SMR; P80099; -.
DR STRING; 243274.THEMA_02895; -.
DR DrugBank; DB04439; Modified Acarbose Pentasaccharide.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR DNASU; 897323; -.
DR EnsemblBacteria; AAD35451; AAD35451; TM_0364.
DR KEGG; tma:TM0364; -.
DR eggNOG; COG0366; Bacteria.
DR InParanoid; P80099; -.
DR OMA; EGQTFWK; -.
DR OrthoDB; 1573900at2; -.
DR BRENDA; 2.4.1.25; 6331.
DR EvolutionaryTrace; P80099; -.
DR Proteomes; UP000008183; 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:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.90.400.10; -; 1.
DR InterPro; IPR015261; 4-alpha-glucanotransf_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF09178; DUF1945; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Cytoplasm;
KW Direct protein sequencing; Glycosyltransferase; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..441
FT /note="4-alpha-glucanotransferase"
FT /id="PRO_0000054336"
FT ACT_SITE 186
FT /note="Nucleophile"
FT ACT_SITE 216
FT /note="Proton donor"
FT BINDING 13
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 15
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 17
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT SITE 278
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 1
FT /note="M -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:1LWJ"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 162..176
FT /evidence="ECO:0007829|PDB:1LWJ"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:1LWJ"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 237..248
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 253..262
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:1LWJ"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 291..302
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:1LWJ"
FT TURN 312..317
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 372..385
FT /evidence="ECO:0007829|PDB:1LWJ"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 393..399
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 401..410
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 413..420
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:1LWJ"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:1LWJ"
SQ SEQUENCE 441 AA; 51843 MW; 9FB4C2ABC9D3DF3A CRC64;
MIGYQIYVRS FRDGNLDGVG DFRGLKNAVS YLKELGIDFV WLMPVFSSIS FHGYDVVDFY
SFKAEYGSER EFKEMIEAFH DSGIKVVLDL PIHHTGFLHT WFQKALKGDP HYRDYYVWAN
KETDLDERRE WDGEKIWHPL EDGRFYRGLF GPFSPDLNYD NPQVFDEMKR LVLHLLDMGV
DGFRFDAAKH MRDTIEQNVR FWKYFLSDLK GIFLAEIWAE ARMVDEHGRI FGYMLNFDTS
HCIKEAVWKE NTRVLIESIE RAVIGKDYLP VNFTSNHDMS RLASFEGGFS KEKIKLSISI
LFTLPGVPLV FYGDELGMKG VYQKPNTEVV LDPFPWNESM CVEGQTFWKW PAYNGPFSGI
SVEYQKRDPD SILSHTLGWT RFRKENQWID RAKLEFLCKE DKFLVYRLYD DQHSLKVFHN
LSGEEVVFEG VKMKPYKTEV V
