ID   A0A927BB96_9BACT        Unreviewed;       932 AA.
AC   A0A927BB96;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   02-APR-2025, entry version 11.
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=IC235_04370 {ECO:0000313|EMBL:MBD2767130.1};
OS   Hymenobacter montanus.
OC   Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
OC   Hymenobacteraceae; Hymenobacter.
OX   NCBI_TaxID=2771359 {ECO:0000313|EMBL:MBD2767130.1, ECO:0000313|Proteomes:UP000612233};
RN   [1] {ECO:0000313|EMBL:MBD2767130.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BT664 {ECO:0000313|EMBL:MBD2767130.1};
RA   Kim M.K.;
RL   Submitted (SEP-2020) 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:MBD2767130.1}.
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DR   EMBL; JACXAD010000004; MBD2767130.1; -; Genomic_DNA.
DR   RefSeq; WP_191003967.1; NZ_JACXAD010000004.1.
DR   Proteomes; UP000612233; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000612233};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          1..101
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
FT   DOMAIN          158..272
FT                   /note="CBM20"
FT                   /evidence="ECO:0000259|PROSITE:PS51166"
FT   REGION          125..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..147
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   932 AA;  106319 MW;  45EBBFF2E2628861 CRC64;
     MILRFSLPYR TVYGQQLAVC GSHPELGNWQ LAAAASMHYD EATGCWSHEL TVADAAGELT
     YKYALLDANT GGQHWEFGPN RTVVYDASRA QRLSLADYWR PPTQPENELL TAAFTKALFR
     RPAPAVAPAA PKANKGKASA KASSTTAPPA PGNQRPAAQA PAAGETVFRL VAPRVAPHYQ
     LCVLGSDPAL GAWDNTKGLV LADSEYPTWT GTIRLENPTE DCHYKYAIWD AQAGHALDME
     GGENRVVPAT HQQTTARVFN DEAYRHPDAW RGAGVALPVF AMRSASGLGV GEFSDLKLLT
     DWAVQTGLKL VQILPINDTT ATHTWVDSYP YAAISVFALH PQFIHLEGIA PLQDKKAARE
     LAQLKAELNA KDFVDYEPMM KAKWKFLRLL YQQEKKAFLA DAGYRTFYAS QADWLVPYAA
     FSALRDRFGT ADFQQWPAEF RTPQNLSELT AETAPDYDEY GLFFFTQFHL DQQLREAVSY
     ARGRGVVLKG DLPIGIYRHS VDAWTQPELY HLDRQAGAPP DDFSTTGQNW RFPTYNWERM
     AQDGYAWWKQ RLGHLSRYFD ALRIDHILGF FRIWEMPIES VEGLLGHFAP ALPLHRHEIE
     RRLGWFNYSR LCEPYIRWHM LQDIFQGEAQ AVFDEYLYDA SYGRIHLKEH VDNQRKIEAY
     IARKVAAAPE HADYFAWLQK GLFQLVNEVL FVPAGNDFYH PRITLNKSYS FRELHSDEDR
     RRLYDDIYTD FFFHRHEEFW RQQGLVKLPP VRYATDMLIC GEDLGMVPAS VPGVMKELGI
     LGLNIQRMPA NPETEFGHPD AAPYLSVVTT SSHDMSTVRG WWEEDRVRTQ RFFETMLGHW
     REIAPFYCEA WVAREILVQH LHSPAMWAIF PLQDLLAMDN HLRRANPHDE QINVPSNPAH
     FWKYRLHLPL EELVDAVGFN EPLRAMVTAS GR
//