ID   N2BV96_9ACTN            Unreviewed;      1103 AA.
AC   N2BV96;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=HMPREF1091_00086 {ECO:0000313|EMBL:EMZ42528.1};
OS   Atopobium minutum 10063974.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Atopobium.
OX   NCBI_TaxID=997872 {ECO:0000313|EMBL:EMZ42528.1, ECO:0000313|Proteomes:UP000012651};
RN   [1] {ECO:0000313|EMBL:EMZ42528.1, ECO:0000313|Proteomes:UP000012651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10063974 {ECO:0000313|EMBL:EMZ42528.1,
RC   ECO:0000313|Proteomes:UP000012651};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Lambert T., Marvaud J.-C.,
RA   Courvalin P., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Atopobium minutum 10063974.";
RL   Submitted (MAR-2013) 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:EMZ42528.1}.
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DR   EMBL; AGXC01000001; EMZ42528.1; -; Genomic_DNA.
DR   RefSeq; WP_002562861.1; NZ_KB822533.1.
DR   AlphaFoldDB; N2BV96; -.
DR   PATRIC; fig|997872.3.peg.87; -.
DR   HOGENOM; CLU_007997_2_0_11; -.
DR   OrthoDB; 9811841at2; -.
DR   Proteomes; UP000012651; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11338; AmyAc_CMD; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 3.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR003385; Glyco_hydro_77.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   PANTHER; PTHR32438; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR   PANTHER; PTHR32438:SF5; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02446; Glyco_hydro_77; 2.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000012651};
KW   Transferase {ECO:0000313|EMBL:EMZ42528.1}.
FT   DOMAIN          147..559
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1103 AA;  125263 MW;  10474335AB7AC1D5 CRC64;
     MNALHNSRLE AYRFPYGAVP VDSVVRLSLD VWDENSPVTT EDKTSQISCD LRIWIDGKGE
     TLIPMEASQQ DDHLRFSCTP TFTQAQIVWY CFRLQNAEGH QWFYGASEGQ VGGVGTLREW
     MGPSFQITAY TPRTTQPDWY RGGVAYQIFP DRFSRDKNWE QRAQQALRLH PHGVARHIQQ
     DWNEPPYYIR DEKGRVQRWD FYGGSINGIR EKLDYLQGMG ITILYLNPIF EAASNHRYDT
     GNYLQIDPLL GDLQDFTLLC KEAQDRGISI ILDGVFNHSG CDSLYFNKYN NYDSVGAYQS
     KDSVYRDWYK FDKKTGEYQS WWGVDDLPDI DEHSQTYRDY MFGKDGVVRS WLRAGARGWR
     LDVADELPDD FIKELRRAAL AERSDALILG EVWEDASNKI SYGKLRQYFL GDELDAVMNY
     NLREALLGYV RGDMSASVLR ERMESMHENY PPDAFVEAFN LLGTHDTARI LTLLGAPDPH
     NMDGQHGSYR LSESERGLAK GRLWLATLVQ MLLPGVPCIY YGDEAGLEGT TDPFNRAAFP
     WGHEDTDCQA IIRNALTLRK TLPLSEADHF FTLDLGDEVF GFVRKNNQHN QSVAVLINRN
     PAVAHEVRVP LLGSCVDELI AGQKLVVDNG VVQLNLPPLG SAVLYFHADK SLGAVPVPGS
     GVLCHVSSLP EALDETGAVE GEQGCLGASA RRFCDWLAQA HQTYWQVLPV NPTDEFGSPY
     AGISAFANNV KFISARERAQ YERAGFSQKD YHEFVDKNAS WLIPYSYFMA LKYDQKGVLW
     RDWPENLRTY DQKTIADYLA QRPHLSQVAK TIRRDQFEFE RQWNALHSYA NERGIHIIGD
     IPLYISGDSA DVWMHQDLFA LDTLGNPALV AGVPSDAFSS EGQRWGNPVY NWDAMRATGY
     EWWLERLARS FELYDYVRLD HFIGFCSYYA IPQDLPIQAG HWCLGPGREL FQKAYERFGN
     LPVIAEDLGM VTPAVRALMA SCGFYGMEVS LFSDYFSQDG WYVPAHKVAY TTTHDTQTLV
     GWCEDHFGKQ DAGARAQEML TLADGSNASL VIVQLQDVLG LDDTHRMNIP GSTQHNWQWV
     CSWDQLDASC ATLRALTEKF GRA
//