ID A0A133Q952_9BACT Unreviewed; 897 AA.
AC A0A133Q952;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=HMPREF3226_01235 {ECO:0000313|EMBL:KXA39400.1};
OS Prevotella corporis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=28128 {ECO:0000313|EMBL:KXA39400.1, ECO:0000313|Proteomes:UP000070533};
RN [1] {ECO:0000313|Proteomes:UP000070533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJR7716 {ECO:0000313|Proteomes:UP000070533};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2016) 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}.
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:KXA39400.1}.
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DR EMBL; LRQG01000092; KXA39400.1; -; Genomic_DNA.
DR RefSeq; WP_060940599.1; NZ_KQ957245.1.
DR AlphaFoldDB; A0A133Q952; -.
DR STRING; 28128.HMPREF3226_01235; -.
DR PATRIC; fig|28128.5.peg.1259; -.
DR eggNOG; COG1640; Bacteria.
DR OrthoDB; 9811841at2; -.
DR Proteomes; UP000070533; 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:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
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; AMYLOMALTASE; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF02446; Glyco_hydro_77; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000070533};
KW Transferase {ECO:0000313|EMBL:KXA39400.1}.
FT DOMAIN 126..233
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
SQ SEQUENCE 897 AA; 104816 MW; 0E7C8A97685D6E85 CRC64;
MNLQFCIEYQ TYYGQDLVLN VITGRQFGDA NISQYRMHTA DGLHWLVDIN REVTPGSQLD
YFYSVHVGDY EESREWVVAP HRIVFNSVDA LNYRIFDHWR VIPDNAYLYT SAITDCVVGS
TIAKAGQKKI KRCVCLKVQA PQLGVGDELR LVGADPVLGA WKERKALKMV RQNVNEWIVC
IDAASLASSK MEFKFLIENA SKEYSPLWEN CNNRTIELPV MEEGDTVVYE LDEAYFALPP
VRVAGTLVPV FSLRSKDSFG IGDFGDLKKM IDWVSLTKQR LLQILPINDT TITHTWTDSY
PYSCISIFAL HPQYVDLTKL PELADKSQRE RFEALRKELN ALPQIDYERV NAAKEEYLKL
IYKQVGKTVI ASRDFKNFFV ENEEWLVPYA QYCYLRDKNG TADFSKWPDH QQWDEAERQP
LSSPRNKAYK DVEFYYFVQF ILSSQLKAVH DYATSRRVIL KGDIPIGVNR YGCDVWTEPR
YFNLNGQAGA PPDGFSANGQ NWGFPTYNWD EMIKDGCRWW VRRFQNMSNY FDAYRIDHVL
GFFRIWEIPV HSVHGLLGQF APALGMSREE IEGYGLHWQE ELFTEPFITD WVLDRIFKEH
ADEVRNTYLI HKWGDRYSMR AEYDTQRKVE AAFEGRDTEK DIWIRDGLYA LISDVLFVRD
HKDPNRFHPR ITVQMDFIYE SLYDSDKAIF NRLYNDYFYR RNNQFWYQEA MKKLPKLVNA
TRMLVCAEDL GMVPDCVAWV MNELKILSLE IQSMPKDPKV TFGHLGANPY RSVSTISTHD
MATLRQWWDE DWERAQHYFN SMLHQDGPAS HPLPGWTARE IVGRHLASPS MLCVLGIQDW
MSIDERLRLA DANAERINVP ANPKHYWRYR MHIGIEELMK VNDFNHNITD LIAQSGR
//