ID A0A101G7G7_9FIRM Unreviewed; 690 AA.
AC A0A101G7G7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=XD78_1306 {ECO:0000313|EMBL:KUK53323.1};
OS Desulfotomaculum sp. 46_296.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Desulfotomaculum.
OX NCBI_TaxID=1635262 {ECO:0000313|EMBL:KUK53323.1, ECO:0000313|Proteomes:UP000053813};
RN [1] {ECO:0000313|Proteomes:UP000053813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUK53323.1}.
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DR EMBL; LGFZ01000036; KUK53323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101G7G7; -.
DR STRING; 1635262.XD78_1306; -.
DR PATRIC; fig|1635262.3.peg.2252; -.
DR Proteomes; UP000053813; Unassembled WGS sequence.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR003385; Glyco_hydro_77.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR048458; MalQ_N.
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; PF02446; Glyco_hydro_77; 1.
DR Pfam; PF21226; MalQ_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361207};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU361207};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:KUK53323.1}.
FT DOMAIN 94..166
FT /note="MalQ N-terminal beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF21226"
SQ SEQUENCE 690 AA; 79870 MW; F203737D9928935D CRC64;
MSVSELRLLN ELAGLYGIEA AFREVPGLQK QAPADSLTAV LKIFGAPLER MQDIRSAIRQ
RKLELLQRCL EPVVVCRNTN PVYLTLRLPE DKSGLKAEVR LETEGGEFMN WMLDLSVLPV
LKTETVEGAV YITKKYTLPN SLPWGYHSLS LNLQGHSYKT LLICAPYQAF SLRLKKNERL
WGVFIPLYAL NSSRSWGAGD LTDLELLIKW THELGGHLTG ALPLLTTFLD EPFSPSPYTP
VSRLFWSEFY LDITCLEELK TNNQARELLD SSTFKERIDD LRSRPLVDYL HVMAAKRKVL
EYLADGFFQK KDRRREEFQD WVHERQTVSD YARFRACTEK QGCGWPSWPL HLREGIIREE
DYETRAEQYH LYVQWAIDRQ FNELSTRARD LGQKLYLDFP LGVHCAGYDV WRERSVFALD
ASSGAPPDMF YSQGQNWGFP PLHPEKIRQQ GYKYYLSGLR HHLKYAGILR LDHVAGLHRL
FWIPKGMTAA DGVYVKYKAD EFYAILTLES QRYRSVIIGE DLGNVPGYIR KQMLKNKIYR
MYVASLEYRP NPQQALGLIP EKALASLNTH DLPPFTAFWQ EKGRNVADRI CLPLYLHQQG
WLPSPTLDNY EVLKGCLKHL AASRADIFLI NLEDLWQETN SQNIPGEINH PNWSRKARFP
IEVFTNNTSL ITLLKEIKRL RESPSRRPRK
//