ID F5T811_9FIRM Unreviewed; 534 AA.
AC F5T811;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 Name=malQ {ECO:0000313|EMBL:EGL37785.1};
GN ORFNames=HMPREF9124_0073 {ECO:0000313|EMBL:EGL37785.1};
OS Oribacterium sp. oral taxon 108 str. F0425.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Oribacterium.
OX NCBI_TaxID=904296 {ECO:0000313|EMBL:EGL37785.1, ECO:0000313|Proteomes:UP000003787};
RN [1] {ECO:0000313|EMBL:EGL37785.1, ECO:0000313|Proteomes:UP000003787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0425 {ECO:0000313|EMBL:EGL37785.1,
RC ECO:0000313|Proteomes:UP000003787};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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:EGL37785.1}.
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DR EMBL; AFIH01000001; EGL37785.1; -; Genomic_DNA.
DR AlphaFoldDB; F5T811; -.
DR STRING; 904296.HMPREF9124_0073; -.
DR eggNOG; COG1640; Bacteria.
DR Proteomes; UP000003787; 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 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 SUPFAM; SSF51445; (Trans)glycosidases; 2.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361207};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU361207,
KW ECO:0000313|EMBL:EGL37785.1};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:EGL37785.1}.
FT REGION 245..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 62044 MW; EAF5B93FE1F0780C CRC64;
MDKTRSAGIL MPVFSLPGEY GIGSFGKDAE EFIDIVAETG NRVWQVLPMG PTSYGDSPYQ
SFSSFAINPY YIDLEGLKEE GLLTEEELKE EKEAFLSSGE KIDYGLLYQR RYPLLRKAYE
RWKAAGGNPD TLIAGRRREN LDYCLFMALK DFSEGCAWPD FPKEFRDKEE SALKSFLEEH
KDEVTYYAFM QWKAEAQWKA VQDYAHERGV LIFGDLPIYC AMDSADVWGN RKIFDFSWEG
RKLKKEEPEE SSEQEQEKEK QDIHSAEEES YPGFVAGVPP DAFSATGQLW GNPLYDWEEQ
AKDNYSFWCK RMEYCFSLYD LIRIDHFRGF EAYYAVPFGE ETAVNGSWRK GPGIALFDAL
HRYFQKESLP VIAEDLGVIT EEVRELMRKT AYPGMKVLQF AFGGDYENDY LPHMFQDNNS
VMYTGTHDND TLRNWFETLG EEERNKIYRY LSRSQNDWNA MTELLIKEAL SATSYLCIIP
AGDYLELLSE GRINAPGTDA GNWQWRMKKH AFSPERKKIM RDMLETYGRR TDKR
//
