ID D7I808_9BACE Unreviewed; 893 AA.
AC D7I808;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=HMPREF9007_00308 {ECO:0000313|EMBL:EFI06219.1};
OS Bacteroides sp. 1_1_14.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=469585 {ECO:0000313|EMBL:EFI06219.1, ECO:0000313|Proteomes:UP000003951};
RN [1] {ECO:0000313|EMBL:EFI06219.1, ECO:0000313|Proteomes:UP000003951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_1_14 {ECO:0000313|EMBL:EFI06219.1,
RC ECO:0000313|Proteomes:UP000003951};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Strauss J., Daigneault M., McDonald J., Ambrose C.E.,
RA Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain 1_1_14.";
RL Submitted (MAR-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 -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC {ECO:0000256|ARBA:ARBA00005684}.
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DR EMBL; GG774702; EFI06219.1; -; Genomic_DNA.
DR AlphaFoldDB; D7I808; -.
DR HOGENOM; CLU_014132_0_0_10; -.
DR Proteomes; UP000003951; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05816; CBM20_DPE2_repeat2; 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; IPR034841; CBM20_DPE2_2.
DR InterPro; IPR002044; CBM_fam20.
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; 1.
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; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Transferase {ECO:0000313|EMBL:EFI06219.1}.
FT DOMAIN 119..235
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 893 AA; 105122 MW; 31FA407C66A17BDD CRC64;
MTVSFNIEYR TSWGEEVRIA GLLPESIPMH TTDGIYWTAD VELEVPKEGM TINYSYQIEQ
NQIIIRKEWD SFPRRLFLSG NSKKKYQIKD CWKNIPEQLY YYSSAFTEAL LAHPDRAEIP
PCHRKGLVIK AYAPRINKDY CLAICGNQKA LGNWDPDKAI PMSDANFPEW QIELDASKLK
FPLEYKFILY HKEEKKADCW ENNPNRYLAD PELKTNETLV ISDRYAYFDI PVWKGAGIAI
PVFSLKSENS FGVGDFGDLK RMIDWAVSTQ QKVIQILPIN DTTMTHAWTD SYPYNSISIY
AFHPMYADIK QMGTLKDKSA AAKFNKKQKE LNGLPAMDYE AVNQTKWEYF RLIFKQEGEK
VLASGEFGEF FNANKEWLQP YAVFSYLRDA FQTPNFREWP RHSVYNAQDI EKMCRPESVD
YPHIALYYYI QFHLHLQLVA ATKYAREHGV VLKGDIPIGI SRNSVEAWTE PYYFNLNGQA
GAPPDDFSVN GQNWGFPTYN WDVMEKDGYR WWMKRFQKMS EYFDAYRIDH ILGFFRIWEI
PMHAVHGLLG QFIPSIPMSR EEIESYGLPF REEYLIPYIH ESFLGQVFGP HTDYVKQTFL
LPAETPGVYH MKPEFTTQRE VESFFAGKND ENSLWIRDGL YTLISDVLFV PDTKEKDKYH
PRIGIQRDFI FRSLNEQEQN AFNRLYDQYY YHRHNEFWRQ QAMKKLPQLT QSTRMLVCGE
DLGMIPDCVS SVMNDLRILS LEIQRMPKNP MHEFGYLNEY PYRSVCTIST HDMSTLRGWW
EEDYLQTQRY YNTMLGHYGT APTVATPELC EEVVRNHLKS NSILCILSLQ DWLSIDGKWR
NPNVQEERIN VPANPRNYWR YRMHLTLEQL MKAEALNDKI RELIKYTGRA PKK
//
