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Database: UniProt
Entry: F8N899_9BACT
LinkDB: F8N899_9BACT
Original site: F8N899_9BACT 
ID   F8N899_9BACT            Unreviewed;       894 AA.
AC   F8N899;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, 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=Premu_2189 {ECO:0000313|EMBL:EGN57578.1};
OS   Hallella multisaccharivorax DSM 17128.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Hallella.
OX   NCBI_TaxID=688246 {ECO:0000313|EMBL:EGN57578.1, ECO:0000313|Proteomes:UP000002772};
RN   [1] {ECO:0000313|Proteomes:UP000002772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17128 {ECO:0000313|Proteomes:UP000002772};
RX   PubMed=22180809; DOI=10.4056/sigs.2164949;
RA   Pati A., Gronow S., Lu M., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Mavromatis K., Mikhailova N., Huntemann M., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Detter J.C., Brambilla E.M., Rohde M.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Ivanova N.;
RT   "Non-contiguous finished genome sequence of the opportunistic oral pathogen
RT   Prevotella multisaccharivorax type strain (PPPA20).";
RL   Stand. Genomic Sci. 5:41-49(2011).
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; GL945017; EGN57578.1; -; Genomic_DNA.
DR   RefSeq; WP_007575229.1; NZ_GL945017.1.
DR   AlphaFoldDB; F8N899; -.
DR   STRING; 688246.Premu_2189; -.
DR   eggNOG; COG1640; Bacteria.
DR   HOGENOM; CLU_014132_0_0_10; -.
DR   OrthoDB; 9811841at2; -.
DR   Proteomes; UP000002772; 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; cd05467; CBM20; 1.
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; 4-ALPHA-GLUCANOTRANSFERASE; 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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycosyltransferase {ECO:0000313|EMBL:EGN57578.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002772};
KW   Transferase {ECO:0000313|EMBL:EGN57578.1}.
FT   DOMAIN          124..230
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
SQ   SEQUENCE   894 AA;  105289 MW;  314DF3156015328A CRC64;
     MNFRFNVDYR TRFGEEVVLN VVNDASEGAS LSKFRMMTQN GTRWSCELNI PAVKDRLSYY
     YDIESQGSSE KHEWTTILHT LELNIVNGKD YTVYDKWHDI PEDSYFYSSA FTDCIRTCRV
     KKPSRSTFAR VIRFIVRAPQ LNNSSLAIVG DGEALGNWDA AKARPMTEHN YNEWAVDLDA
     SWFAGDTIEF KFIAVNNSDK QDVLWEEGYN RTVKVPPLSD GQVVVYDLSQ AFFQIYNTRV
     AGTLVPVFSL RTKESFGVGD FGDLEKMLDF MRATGQKVLQ VLPVNDTTIT HTWTDSYPYS
     CISIFALHPQ YVNLHRLPLL DDKEKREHYD KLRHELNALP QIDYERVNDA KMAYLRDLYA
     QVGAKVLGTH AFKEYFKENE RWLVPYAQYC TLRDKYGTAD FLQWKDHNQW DEAERKRLSE
     PHTKEYKEVA FWYYVQFVLD SQMKAVHEYA RQHHVILKGD IPIGVNRYGC DVWTEPRYFN
     LNGQAGAPPD AFSTNGQNWG FPTYNWEEMI KDGCQWWVRR FKNMARYFDA YRIDHVLGFF
     RIWEIPSNAV HGLLGQFSPA LGMTADEIRG YGLNFQEKRF TEPFITDWVL DRVFKERADE
     VREKYLDRID GERYKMKPQF DTQKKIQKLF ENVTDTQELN FRDGLYALIS DVLFVRDRSD
     RNKFHPRISA QFDFIYESLY DNDKGAFNRL YNDYYYRRNN QFWYSEAMKK LPVLVQATRM
     LACAEDLGMV PDCVSWVMNQ LRILSLEIQS MPKDPHVRFG HLSSNPYRSV CTFSTHDMST
     MRQWWDEDWN RTQEYYNSML YHQGPAPHPL PGWLARDILS CQLTSPSMLC VLSIQDWMAM
     DEQLRLADAD RERINVPAIV PYYWRYRMHV NIEDLINSES FAQNIKDLVL ESGR
//
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