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Database: UniProt
Entry: A0A4S4GW61_9BACT
LinkDB: A0A4S4GW61_9BACT
Original site: A0A4S4GW61_9BACT 
ID   A0A4S4GW61_9BACT        Unreviewed;       894 AA.
AC   A0A4S4GW61;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   02-APR-2025, entry version 22.
DE   RecName: Full=4-alpha-glucanotransferase {ECO:0000256|ARBA:ARBA00020295};
DE            EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560};
DE   AltName: Full=Amylomaltase {ECO:0000256|ARBA:ARBA00031423};
DE   AltName: Full=Disproportionating enzyme {ECO:0000256|ARBA:ARBA00031501};
GN   ORFNames=E5990_07430 {ECO:0000313|EMBL:THG48265.1};
OS   Muribaculaceae bacterium.
OC   Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
OC   Muribaculaceae.
OX   NCBI_TaxID=2498093 {ECO:0000313|EMBL:THG48265.1, ECO:0000313|Proteomes:UP000305401};
RN   [1] {ECO:0000313|EMBL:THG48265.1, ECO:0000313|Proteomes:UP000305401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NM86_A22 {ECO:0000313|EMBL:THG48265.1,
RC   ECO:0000313|Proteomes:UP000305401};
RA   Navarre W., Wong E., Huang K.C., Tropini C., Ng K., Yu B.;
RT   "Microbes associate with the intestines of laboratory mice.";
RL   Submitted (APR-2019) 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC       {ECO:0000256|ARBA:ARBA00005684}.
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:THG48265.1}.
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DR   EMBL; SSTG01000089; THG48265.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4S4GW61; -.
DR   OrthoDB; 9811841at2; -.
DR   Proteomes; UP000305401; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05467; CBM20; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR002044; CBM20.
DR   InterPro; IPR003385; Glyco_hydro_77.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR32518; -; 1.
DR   PANTHER; PTHR32518:SF3; 4-ALPHA-GLUCANOTRANSFERASE; 1.
DR   Pfam; PF00686; CBM_20; 2.
DR   Pfam; PF02446; Glyco_hydro_77; 1.
DR   SMART; SM01065; CBM_2; 2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 2.
DR   PROSITE; PS51166; CBM20; 2.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          1..100
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
FT   DOMAIN          125..241
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
SQ   SEQUENCE   894 AA;  103571 MW;  C2893B8326A2A24E CRC64;
     MKINFNIDYK TQWGETLYIC GNDSLLGSGN IDAALKMHVD GVGLWTATVD ISDKNVRNLE
     YGYVVRNDNG SERREWGGCC HSIDLSNAAE SYDIYDAWRD IPLDKPYYSS AFTQCINRRN
     DRCEAVVPAP GFLTLSVDAP TVGPDEVLAL CGACDSLGEW NPEKALPMSD AGYPVWKINI
     DLSRTILPIE FKFIVLDKDT RALKAWDGGD NRRLASMTKN RHVSMVVSGM RFRDPRALWR
     GAGVAIPVFS VRTRDDFGVG DFYSLTKMVD WAVATGQKFL QILPINDTTM THTWTDSYPY
     NACTSFGLHP MYMHLQELGR LKDKARQAYF DDLACELNNL PTVDYERVNE GKLQFISEIF
     AQEGAKTLNS SDFTKFLIDN EYWLKPYAAF CVLRDKFGTP EFGKWGEYAE YTQAKADRVY
     AENTPQMNQV YYTQYHLDRQ MRRVHEYASA HGVAFKGDIP IGISRDSADA WINPRLFNLD
     CQAGAPPDDF SVLGQNWGLP TYNWEEMWKD RFAWWKSRFC KMAEYFDAYR IDHVLGFFRI
     WQIPMTAVHG LLGIFNPALP YSADELKSLY DFWIDADVHT KPFIMDWFLN DFFGEYTDEA
     RERFLNGLGH GRYELKSGFD TQRKIADYFS SQDKTEKNRR MCEALLGLAD QVLFIEDPDR
     KGKYHPRISA QYTYVYRQLN DYEKWCFNRL YNDFFYHRHN DYWYGKAMWK LPNLIDATPM
     LTCAEDLGMI PACVPAVMDQ LRILSLEIQR MPKDPSAKFG NTWNYPYLSV CTTSTHDMGG
     IRQWWEDNPQ MAQEFYNEVL HQEGSAPRVA EPWICDQILN LNLKSPSMLA ILPLQDWLSV
     SPDLRRPDPF EEQINEPSNP RHYWRYRMHL NVEDLLGAET FNRDLADRVH NSGR
//
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