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 04-NOV-2026, entry version 174. 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; Thermotogati; Thermotogota; Thermotogae; Thermotogales; OC 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. 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}. 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; AE000512; AAD35451.1; -; Genomic_DNA. DR RefSeq; WP_004083169.1; NC_000853.1. 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 SMR; P80099; -. DR STRING; 243274.TM_0364; -. DR DrugBank; DB04439; Modified Acarbose Pentasaccharide. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR PaxDb; 243274-TM_0364; -. DR DNASU; 897323; -. DR EnsemblBacteria; AAD35451; AAD35451; TM_0364. DR KEGG; tma:TM0364; -. DR KEGG; tmi:THEMA_02895; -. DR KEGG; tmm:Tmari_0362; -. DR KEGG; tmw:THMA_0372; -. DR eggNOG; COG0366; Bacteria. DR InParanoid; P80099; -. DR OMA; AAPKDCH; -. DR OrthoDB; 9805159at2; -. DR BRENDA; 2.4.1.25; 6331. DR EvolutionaryTrace; P80099; -. DR FunFam; 3.90.400.10:FF:000010; 4-alpha-glucanotransferase; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1. DR Gene3D; 3.90.400.10; Oligo-1,6-glucosidase, Domain 2; 1. DR InterPro; IPR015261; 4-alpha-glucanotransf_C. DR InterPro; IPR006046; Alpha_amylase. DR InterPro; IPR006047; GH13_cat_dom. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR045857; O16G_dom_2. DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1. DR PANTHER; PTHR10357:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 1. DR Pfam; PF00128; Alpha-amylase; 2. DR Pfam; PF09178; MGTA_C; 1. DR PRINTS; PR00110; ALPHAAMYLASE. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IDA:UniProtKB. DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central. DR Proteomes; UP000008183; Chromosome. DR AlphaFoldDB; P80099; -. DR MDposit; P80099; -. 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 //