ID E1LUS2_STRMT Unreviewed; 505 AA.
AC E1LUS2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 41.
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:EFN99775.1};
GN ORFNames=SMSK597_1718 {ECO:0000313|EMBL:EFN99775.1};
OS Streptococcus mitis SK597.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=585204 {ECO:0000313|EMBL:EFN99775.1, ECO:0000313|Proteomes:UP000003316};
RN [1] {ECO:0000313|EMBL:EFN99775.1, ECO:0000313|Proteomes:UP000003316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK597 {ECO:0000313|EMBL:EFN99775.1,
RC ECO:0000313|Proteomes:UP000003316};
RA Daugherty S.C., Tallon L.J., Jones K.M., Liu X., Kilian M., Tettelin H.;
RL Submitted (SEP-2010) 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:EFN99775.1}.
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DR EMBL; AEDV01000090; EFN99775.1; -; Genomic_DNA.
DR RefSeq; WP_000747302.1; NZ_AEDV01000090.1.
DR AlphaFoldDB; E1LUS2; -.
DR eggNOG; COG1640; Bacteria.
DR Proteomes; UP000003316; 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; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361207};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU361207,
KW ECO:0000313|EMBL:EFN99775.1};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:EFN99775.1}.
SQ SEQUENCE 505 AA; 58077 MW; 7CAB1F21A75F35A4 CRC64;
MKKRQSGVLM HISSLPGAYG IGSFGQSAYD FVDFLVRTKQ RYWQILPLGT TSYGDSPYQS
FSAFAGNTHF IDLDILVEQG LLEASDLEGV DFGSDASEVD YAKIYYARRP LLEKAVKRFF
EVGDVKDFEK FAQDNQSWLE LFAEYMAIKE HFENLAWTEW PDADARARKA SALESYREQL
ADKLVYHRVT QYFFFQQWLK LKAYANDNHI EIVGDMPIYV AEDSSDMWAN PHLFKTDVNG
KATCIAGCPP DEFSATGQLW GNPIYDWKAM DKDGYKWWIE RLRESFKIYD IVRIDHFRGF
ESYWEIPAGS DTAAPGEWVK GPGYKLFAAV KEELGELNII AEDLGFMTDE VIELRERTGF
PGMKILQFAF NPEDESIDSP HLAPANSVMY TGTHDNNTVL GWYRNEIDDA TREYMARYTN
RKEYETVPHA MLRTVFSSVS FMAIATMQDL LELDEAARMN FPSTLGGNWS WRMTEDQLTP
AVEEGLLDLT TIYRRINENL VELKK
//
