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Database: UniProt
Entry: C9KN24_9FIRM
LinkDB: C9KN24_9FIRM
Original site: C9KN24_9FIRM 
ID   C9KN24_9FIRM            Unreviewed;      1181 AA.
AC   C9KN24;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
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   Name=malQ {ECO:0000313|EMBL:EEX68763.1};
GN   ORFNames=MITSMUL_04835 {ECO:0000313|EMBL:EEX68763.1};
OS   Mitsuokella multacida DSM 20544.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Mitsuokella.
OX   NCBI_TaxID=500635 {ECO:0000313|EMBL:EEX68763.1, ECO:0000313|Proteomes:UP000003671};
RN   [1] {ECO:0000313|EMBL:EEX68763.1, ECO:0000313|Proteomes:UP000003671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20544 {ECO:0000313|EMBL:EEX68763.1,
RC   ECO:0000313|Proteomes:UP000003671};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2009) 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}.
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:EEX68763.1}.
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DR   EMBL; ABWK02000017; EEX68763.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9KN24; -.
DR   STRING; 500635.MITSMUL_04835; -.
DR   CAZy; CBM34; Carbohydrate-Binding Module Family 34.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   CAZy; GH77; Glycoside Hydrolase Family 77.
DR   PATRIC; fig|500635.8.peg.1528; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG1640; Bacteria.
DR   HOGENOM; CLU_007997_0_1_9; -.
DR   Proteomes; UP000003671; 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:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11338; AmyAc_CMD; 1.
DR   CDD; cd02857; E_set_CDase_PDE_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
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; IPR004185; Glyco_hydro_13_lg-like_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; IPR014756; Ig_E-set.
DR   InterPro; IPR045857; O16G_dom_2.
DR   NCBIfam; TIGR00217; malQ; 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.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361207};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU361207,
KW   ECO:0000313|EMBL:EEX68763.1};
KW   Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:EEX68763.1}.
FT   DOMAIN          174..580
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1181 AA;  136185 MW;  4761B73211B432A8 CRC64;
     MHRKYKKIQN EQVRRRAADD AAFLLEGGVF MLTQDQVWHD SQDINYRSPV GAAEAGSKVR
     MSLRLRTKEG IRQVILRCWQ DQTGEYLIPL ETKDDPFQEE HLYSGWLPLP EKGGLVWYYF
     IISMEDGTWY YGNNPEQLGG MGTLYDHVPP SFQITVFNKG AKTPDWFKHA VMYQIFPDRF
     SREGNTIIEK KGAVFHACWQ DDPCYYKDPD TKEIVAYDFF GGNLKGIEKK LDYLKDLGIS
     VIYLNPVFES ESNHHYDTGD YHKIDPILGS NEDFRHLVDT AKAKGIRIIL DGVFSHTGSN
     SRYFNREGQY NTIGAFQSPD SPYYEWYNFR NFPYEYESWW NFSTLPDVKE TTPSYMDFII
     YDKDSVMHHW MKEGIAGWRL DVIDELPAAF SQAFFAELKK TDPDAVMIGE VWEDASHKVA
     YGVPREYLCG QEMDSAMNYP FRQILFDFLL GRTDARMSLR RFESLRENYP RENFYAMMNL
     IGSHDVERAI TVLGEEPFYD GMPAIEQSRA RLSDDQYNLG MARLFMAALW QMTYPGVPCV
     YYGDEIAMQG FKDPYNRRPY DWEHGDTYVR SRYERMIRVR NEHTALQTGE LLPLYAEGDV
     MAFARLVRGG RDVFGEPAKD ECFISLFNRS LKEKKTVTLQ VGDFADGVFA DAFHPETRFT
     VENGQLTVTL LPLKGFLLQN IPPEHRYKHE AGVLLHPTSL PSKYGVGDFG KEAYRFVDFL
     EKAGQHVWQI LPLGPVGFSY SPYQSPSAFA GNPLLIDIDE LVEKGWLSKQ EAKVTYADFD
     SSADFEPART FKNKCLRKAH AAFQRDAEAQ ADYEAFCRKE AYWLDDYALF EAAKRDYDNK
     GWMDWPENIK KREPAALASL AKRLAEDIAL QKFMQYLFHR QWQRLHDYAK EKGIRIMGDM
     PIFLAQDSAD VWANQQLFDL NPDGTAHTVA GVPPDYFSAT GQLWGNPQYN WQAMKAENYA
     WWKKRFQKLY EMVDIVRIDH FRGFESYWEV DGKAKNAIKG RWLPGPGKPF FDEVRRTLGD
     LPIVAEDLGI ITPEVEKLRD DCGFPGMKVL EFTLYLNHQH RLSTVVPENS IVYTGTHDNN
     TLVGWLKDEV TPSLRKAIAD LVRADVRKPE EIASHLVGFA YASNARLAVV PMQDLLQLDG
     SARMNTPGTS EGNWRWCMRP GDLEKVDAAK LHELAVRTGR A
//
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