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Database: UniProt
Entry: B7L4U5_ECO55
LinkDB: B7L4U5_ECO55
Original site: B7L4U5_ECO55 
ID   B7L4U5_ECO55            Unreviewed;       694 AA.
AC   B7L4U5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
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:CAV00189.1};
GN   OrderedLocusNames=EC55989_3824 {ECO:0000313|EMBL:CAV00189.1};
OS   Escherichia coli (strain 55989 / EAEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585055 {ECO:0000313|EMBL:CAV00189.1, ECO:0000313|Proteomes:UP000000746};
RN   [1] {ECO:0000313|Proteomes:UP000000746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55989 / EAEC {ECO:0000313|Proteomes:UP000000746};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928145; CAV00189.1; -; Genomic_DNA.
DR   RefSeq; WP_000444333.1; NC_011748.1.
DR   AlphaFoldDB; B7L4U5; -.
DR   CAZy; GH77; Glycoside Hydrolase Family 77.
DR   KEGG; eck:EC55989_3824; -.
DR   HOGENOM; CLU_022072_1_1_6; -.
DR   Proteomes; UP000000746; 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   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR003385; Glyco_hydro_77.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR048458; MalQ_N.
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; PF02446; Glyco_hydro_77; 1.
DR   Pfam; PF21226; MalQ_N; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361207};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU361207,
KW   ECO:0000313|EMBL:CAV00189.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000746};
KW   Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:CAV00189.1}.
FT   DOMAIN          53..128
FT                   /note="MalQ N-terminal beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF21226"
SQ   SEQUENCE   694 AA;  78471 MW;  2924D66E6FAF0B36 CRC64;
     MESKRLDNAA LAAGISPNYI NAHGKPQSIS AETKRRLLDA MHQRTATKVA VTPVPNVMVY
     TSGKKMPMVV EGSGEYSWLL TTEEGTQYKG HVTGGKAFNL PTKLPEGYHT LTLTQDDQRA
     HCRVIVAPKR CYEPQALLNK QKLWGACVQL YTLRSEKNWG IGDFGDLKAM LVDVAIRGGS
     FIGLNPIHAL YPANPESASP YSPSSRRWLN VIYIDVNAVE DFHLSEEAQA WWQLPTTQQT
     LQQARDADWV DYSTVTALKM TALRMAWKGF AQRDDEQMAA FRQFVAEQGD SLFWQAAFDA
     LHAQQVKEDE MRWGWPAWPE MYQNVDSPEV RQFCEEHRND VDFYLWLQWL AYSQFAACWE
     ISQGYEMPIG LYRDLAVGVA EGGAETWCDR ELYCLKASVG APPDILGPLG QNWGLPPMDP
     HIITARAYEP FIELLRANMQ NCGALRIDHV MSMLRLWWIP YGETADQGAY VHYPVDDLLS
     ILALESKRHR CMVIGEDLGT VPVEIVGKLR SSGVYSYKVL YFENDHEKTF RAPKAYPEQS
     MAVAATHDLP TLRGYWESGD LTLGKTLGLY PDEVVLRGLY QDRELAKQGL LDALHKYGCL
     PKRAGHKASL MSMTPTLNRG LQRYIADSNS ALLGLQPEDW LDMAEPVNIP GTSYQYKNWR
     RKLSATLESM FADDGVNKLL KDLDRRRRAA AKKK
//
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