ID   A0A127VB07_9SPHI        Unreviewed;      1320 AA.
AC   A0A127VB07;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=4-alpha-glucanotransferase {ECO:0000256|ARBA:ARBA00020295, ECO:0000256|RuleBase:RU361207};
DE            EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560, ECO:0000256|RuleBase:RU361207};
DE   AltName: Full=Amylomaltase {ECO:0000256|ARBA:ARBA00031423, ECO:0000256|RuleBase:RU361207};
DE   AltName: Full=Disproportionating enzyme {ECO:0000256|ARBA:ARBA00031501, ECO:0000256|RuleBase:RU361207};
GN   ORFNames=AY601_1560 {ECO:0000313|EMBL:AMP98475.1};
OS   Pedobacter cryoconitis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=188932 {ECO:0000313|EMBL:AMP98475.1, ECO:0000313|Proteomes:UP000071561};
RN   [1] {ECO:0000313|EMBL:AMP98475.1, ECO:0000313|Proteomes:UP000071561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 27485 {ECO:0000313|EMBL:AMP98475.1,
RC   ECO:0000313|Proteomes:UP000071561};
RA   Lee J., Kim O.-S.;
RT   "Complete genome sequence of Pedobacter cryoconitis PAMC 27485.";
RL   Submitted (MAR-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         ECO:0000256|RuleBase:RU361207};
CC   -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC       {ECO:0000256|ARBA:ARBA00005684, ECO:0000256|RuleBase:RU361207}.
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DR   EMBL; CP014504; AMP98475.1; -; Genomic_DNA.
DR   RefSeq; WP_068398795.1; NZ_CP014504.1.
DR   KEGG; pcm:AY601_1560; -.
DR   PATRIC; fig|188932.3.peg.1623; -.
DR   OrthoDB; 9811841at2; -.
DR   Proteomes; UP000071561; 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:UniProtKB-KW.
DR   CDD; cd11336; AmyAc_MTSase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 3.30.1590.10; Maltooligosyl trehalose synthase, domain 2; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR003385; Glyco_hydro_77.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013797; Maltooligo_trehalose_synth_4.
DR   InterPro; IPR012767; Trehalose_TreY.
DR   NCBIfam; TIGR00217; malQ; 1.
DR   NCBIfam; TIGR02401; trehalose_TreY; 1.
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; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361207};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU361207};
KW   Reference proteome {ECO:0000313|Proteomes:UP000071561};
KW   Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:AMP98475.1}.
FT   DOMAIN          6..575
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1320 AA;  151692 MW;  45CAF39ABC577379 CRC64;
     MFNPISTYRI QFHADFTFND FRKLIPYVHQ LGVKTIYASP IFTAVPGSMH GYDGLNPIQI
     NPEIGSLAEL KLIAKELAAV KMGWIQDIVP NHMAYDFRNP WLMDVLKKGE KSKYRNHFDI
     ISQDLAKEPL MAPFLGAALE EEIANKNLSL VAQKGEWFLK YHESYWPLRK GTDLKGSILE
     ITGQQFYRLC SYQESNERMN YRRFFTVNSL ICLNMQSKIT FDDFHVLIKE LVDQKIFQGL
     RIDHIDGLFD PKQYLENLRA LCGKDVYIVA EKILEPGEIL PAEWPIQGTT GYDYLGLANQ
     LYTNEQSEKK FNNFYENLTD DHQSVEEQIL EKKRKILSTA MQGELENLYQ LLLNIIPEGP
     ERMAIGDFGV FKHIISELLI LCPVYRFYGN AYPLPPQEME AMEKLFAALE KDKELVKPVQ
     FIKKALLYEH ISFYQRLMQF SGPLMAKGVE DTLMYTYNRH IGNNEVGDSP AVFGLKASDF
     HEAILNRGEN WPLTMNSTAT HDTKRGEDAR ARLSILTDLK GEWLQQVKEW NVLNATDGAS
     PDENDTYFIY QTLVSTYDER EDSEVYQKRF LDYIEKALRE AKEKSGWENP DMDYEAATSA
     FVKRILDTKR EFWTVFSDFF RRLAHLGMVK SLSSLILKHG VPGIPDTYQG TELWDFSMVD
     PDNRRPVDYA LRVQYMDDFL KKSFHIKLLW QESSAGEIKL LILQKLLKFR AAYAELFRIG
     LYIPLKVTGL HAADFIAFAR RYKTDWAIFV VPVNVAALLN AQNNLHFELG DTQVVLPAGA
     PSVYLDLIEN QSCKAENSVL VLQDIFKSVP FGVLHQKVEH QERGAGILMH ITSLPSAFGI
     GDMGPEAFNF MDFLASSGQK YWQILPLNPL LDTQAYSPYA SGSVMAANPV LISPELLIKD
     GFLEPDVIKA KHRKVKRKVN FTSAVQEKKL MLSLAYQRFK QKSNGKDQAF SDFSSNEAYW
     LEDYALYEVL KTLNDNKPWY EWQKELKDRE LTALSKVREQ HEDAINEVKW YQFIFFKQWN
     ELKAQAVNLN IKLIGDLPFY AALDSCDVWA NQELFEISPS GEMKAIAGVP PDYFNADGQL
     WGMPVYNWKA MKKSNYEWWV QRIKRNIELY DLIRLDHFRA FSSYWEVPAD SSSAKFGNWK
     QGPGSQVFDV LEAHFGTIPF IAEDLGEIDA EVTALRDHYQ LPGMKVLQFA FGEDSPASVH
     APHNFTSVNC LVYTGTHDNN TTRNWYAKDI SHGDRSRIDS YTGIKVSKRN IAQVLIRLAY
     ASTAKVVIVP LQDILNKGAK ARMNVPASIK RNWVWRVKSK ELNDAIGVYL RDLVQLYGRS
//