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Database: UniProt
Entry: F2N9S9_CORGP
LinkDB: F2N9S9_CORGP
Original site: F2N9S9_CORGP 
ID   F2N9S9_CORGP            Unreviewed;      1099 AA.
AC   F2N9S9;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   08-NOV-2023, entry version 60.
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   OrderedLocusNames=Corgl_1074 {ECO:0000313|EMBL:AEB07182.1};
OS   Coriobacterium glomerans (strain ATCC 49209 / DSM 20642 / JCM 10262 / PW2).
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae; Coriobacterium.
OX   NCBI_TaxID=700015 {ECO:0000313|EMBL:AEB07182.1, ECO:0000313|Proteomes:UP000006851};
RN   [1] {ECO:0000313|Proteomes:UP000006851}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 49209 / DSM 20642 / JCM 10262 / PW2
RC   {ECO:0000313|Proteomes:UP000006851};
RX   PubMed=23961308; DOI=10.4056/sigs.3507020;
RA   Stackebrandt E., Zeytun A., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA   Chen A., Palaniappan K., Chang Y.J., Land M., Hauser L., Rohde M.,
RA   Pukall R., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Coriobacterium glomerans type strain (PW2(T))
RT   from the midgut of Pyrrhocoris apterus L. (red soldier bug).";
RL   Stand. Genomic Sci. 8:15-25(2013).
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; CP002628; AEB07182.1; -; Genomic_DNA.
DR   RefSeq; WP_013708925.1; NC_015389.1.
DR   AlphaFoldDB; F2N9S9; -.
DR   STRING; 700015.Corgl_1074; -.
DR   KEGG; cgo:Corgl_1074; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG1640; Bacteria.
DR   HOGENOM; CLU_007997_1_1_11; -.
DR   OMA; DPYNRGT; -.
DR   OrthoDB; 9811841at2; -.
DR   Proteomes; UP000006851; Chromosome.
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   Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR013783; Ig-like_fold.
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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006851}.
FT   DOMAIN          137..552
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1099 AA;  121959 MW;  C5C2A9A1182AFA30 CRC64;
     MKLRHNSRSC DCRAPFGAVR AGTTVRLAVH VEDADFASIR LSLRTWVDGR GERIDDMPAV
     GNGTFEVSLA CPEPEIVWYL FIARAADGTA TYLGAPTGRT GGEGVAYASI DAPSFQITVF
     QHRAIRPTWY EHGIVYQIFP DRYRRDAGWR ERTAAVLDRP RAGIARRLVE DWNEPPSYRR
     ANDGSIACWD FYGGSLKGIE DDLQRLAELG VSAIYLNPIF EAASNHRYDT ADYLSIDPIL
     GTEKDFRHLC AAARERGISI ILDGVFNHTG DDSIYFNRYG NYPGAGAWSG PESPWRDAYK
     FDDDGGYRCW WGVKNMPDLN QDSPLVRELI LGADGVVRHW LRAGARGWRL DVADELSDGF
     IADIKRAVME ERPDGLVLGE VWEDASNKSS YGKLRRYLLG QELDSAMNYP FRSMVIDYLL
     GVRSARDTAE TIESLRENYP PEALACALNL LGSHDKPRIA SVLGGGPDES QLPESERGTW
     RLDPHAMGLA KGRFWLASLM QMTFPGVPSI YYGDEYGLEG LSDPGNRRTL PDERDVFDHD
     MLTIVRNAAA LRRALPLMVT GDISAEARSD DVLSYTRRDA SGLSATVILN SDCASQHAVS
     IPMLGQAASD LISGRELGRN EDGTVTVELA PLGSAVVHFH DRRRMQKPLA PGAGIMCHLT
     SMPTEDGRAG RLGAAARRFI DRLHAMGARY WQVLPVNPTD GFNSPYAGPS AFAGSSALLP
     GTAGEIERDF ESWRDTGGEH DAAFLEFAQT QAAWLAPYCA FMAIKRHMGG ASRHEWPARF
     KRYDPSLLDD GDLAREARFQ AYLQFCFETA WGEMSAYAHE RGIEIIGDIP MYVSDESADV
     WSAPELFNLD DDGRPTEVAG APPDDFAPDG QLWGNPTFRW DRMRHDGFTW WLARLRRAQR
     LYDHVRLDHF LGYHSYFSIP AGGACSAGRW LPGPGADLFQ LAYDAWGPLP FIAEDLGYLT
     PGVRALCATC GFPGMDVMQF EDYDVRAGFY PQAGKICYTS THDTSTLIGF CERSYANGDR
     EQARRIAEAL LGAALHSDAD VVITPLQDIL ELDDQARMNV PGVAEGNWTW RAREADVIDA
     VPRIREMLER SGRISAASR
//
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