ID G0VSE8_MEGEL Unreviewed; 1132 AA.
AC G0VSE8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=4-alpha-glucanotransferase {ECO:0000256|ARBA:ARBA00020295, ECO:0000256|RuleBase:RU361207};
DE EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560, ECO:0000256|RuleBase:RU361207};
DE AltName: Full=Amylomaltase {ECO:0000256|ARBA:ARBA00031423, ECO:0000256|RuleBase:RU361207};
DE AltName: Full=Disproportionating enzyme {ECO:0000256|ARBA:ARBA00031501, ECO:0000256|RuleBase:RU361207};
GN ORFNames=MELS_1970 {ECO:0000313|EMBL:CCC74188.1};
OS Megasphaera elsdenii DSM 20460.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1064535 {ECO:0000313|EMBL:CCC74188.1, ECO:0000313|Proteomes:UP000010111};
RN [1] {ECO:0000313|EMBL:CCC74188.1, ECO:0000313|Proteomes:UP000010111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20460 {ECO:0000313|EMBL:CCC74188.1,
RC ECO:0000313|Proteomes:UP000010111};
RX PubMed=21914887; DOI=10.1128/JB.05861-11;
RA Marx H., Graf A.B., Tatto N., Thallinger G.G., Mattanovich D., Sauer M.;
RT "Genome Sequence of the Ruminal Bacterium Megasphaera elsdenii.";
RL J. Bacteriol. 193:5578-5579(2011).
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:0000256|ARBA:ARBA00000439,
CC ECO:0000256|RuleBase:RU361207};
CC -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC {ECO:0000256|ARBA:ARBA00005684, ECO:0000256|RuleBase:RU361207}.
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DR EMBL; HE576794; CCC74188.1; -; Genomic_DNA.
DR RefSeq; WP_014016909.1; NZ_CP027570.1.
DR AlphaFoldDB; G0VSE8; -.
DR STRING; 1064535.MELS_1970; -.
DR KEGG; med:MELS_1970; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG1640; Bacteria.
DR eggNOG; COG3280; Bacteria.
DR HOGENOM; CLU_007997_0_1_9; -.
DR Proteomes; UP000010111; 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:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11338; AmyAc_CMD; 1.
DR CDD; cd02857; E_set_CDase_PDE_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004185; Glyco_hydro_13_lg-like_dom.
DR InterPro; IPR003385; Glyco_hydro_77.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR045857; O16G_dom_2.
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; PF00128; Alpha-amylase; 1.
DR Pfam; PF02446; Glyco_hydro_77; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361207};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU361207};
KW Reference proteome {ECO:0000313|Proteomes:UP000010111};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:CCC74188.1}.
FT DOMAIN 137..534
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1132 AA; 128358 MW; 63C21A943A716D3F CRC64;
MDLRLYHNSH EFYYRSSFGA VPSGSRLILR LRAGGSDARN CRARIRLWQS NVGESFVPMT
YQDGIFTGCV TMPPKGCLVW YYFIVDDGHE TVYYGNNYDR LGGEGAKYPE VPPAYQVTVY
DKDAHTPDWF KHAIVYQIFP DRFRHGTHTT GRLYGKKGAV IHSDWDDVPY YCKREGQGDI
VYYDFFGGNL AGIREKLPYL KELGITAIYL NPIFESSSNH RYGTADYFRV DPMLGTNEEF
AAFCQAAKEA GIHIILDGVF SHTGADSIYF NRFGNYPGVG AYQSKESPYY EWYRFKQYPD
DYESWWGVSD LPDVEETTPS YMDFIIDSED SVLKYWLNEG ISGWRLDVID ELPVPFLRQF
YHTLKEEKPD AILIGEVWED ASNKVSYSEQ REYLCGYDID SAMNYAQRAI MLDFMTGVKD
ARRMNAELTR LIENYPPENF YAMLNLIGSH DIERILTVLT KAGGTDVATA EETGKKRLKL
LTAWQMTMPG APCIYYGDEV GVTGGKDPDN RRTYPWGHED LDLLSWTKAL TRLRTAHDAL
QTGRFIPLYA DGDVFAFARV IEGGQDVFGK PAEDGFFIIA MNRNPSALRT ISIYTDGLAY
GKLTNALHPR MTPVTTVNSR LTLTLPPLKV VILQGKEAGT KRAGVLLHPT SLPAACGNGV
LGPAAYRFVD FLKAAGQRVW QILPLTPPLM GDSPYLSESA FAGNEALISL EVLRDWGWLR
QEALDDFLAQ GQKTTSWHSL AAYKAKILWD MSHDPDLTIP WEPFRAFCEK NAYWLDDYAL
FRAVRDFFGG RCWTEWPEDI RHHSREALAQ YGRELAGAVS HVKFMQYIFS RQWHDVRAYA
AKNGVSVLGD VPMFVAHNSA DCWAHQDQFD LDEMGNPSSV AGVPPDYFSA DGQLWGNPLY
DYQAMAADNY QWWTDRFRRM MDLVDEVRVD HFRGFAAYWA VPAGSETAKS GAWKEGPGLD
LFRAVYQKIG RLRLVAEDLG VITDDVCTLK DALHLPGMKV IQFHLKDRAD GRLAFDTEPD
CIAYTGTHDN NTIRGWYEDD LSPSQQLHVR QMLGLSDEAA PQEIVGALIA YTCRRRAETV
IIPMQDLLAL PSSGRMNTPG VAEGNWHWQL KDGQLTFDIA RWLAKVCRES GR
//
