GenomeNet

Database: UniProt
Entry: A0A133Q952_9BACT
LinkDB: A0A133Q952_9BACT
Original site: A0A133Q952_9BACT 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system