ID E2X8W1_SHIDY Unreviewed; 694 AA.
AC E2X8W1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=Asd1617_04837 {ECO:0000313|EMBL:AHA67664.1};
OS Shigella dysenteriae 1617.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=754093 {ECO:0000313|EMBL:AHA67664.1, ECO:0000313|Proteomes:UP000031647};
RN [1] {ECO:0000313|EMBL:AHA67664.1, ECO:0000313|Proteomes:UP000031647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1617 {ECO:0000313|EMBL:AHA67664.1,
RC ECO:0000313|Proteomes:UP000031647};
RA Aksomboon Vongsawan A., Kapatral V., Vaisvil B., Serichantalergs O.,
RA Hale T.L., Mason C.J.;
RT "Comparative genomics of Sd1617 to representative strains in evaluating its
RT pathogenesis.";
RL Submitted (SEP-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 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; CP006736; AHA67664.1; -; Genomic_DNA.
DR RefSeq; WP_000444321.1; NZ_ADUT01000021.1.
DR AlphaFoldDB; E2X8W1; -.
DR KEGG; sdz:Asd1617_04837; -.
DR PATRIC; fig|754093.4.peg.4703; -.
DR HOGENOM; CLU_022072_1_1_6; -.
DR Proteomes; UP000031647; 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:AHA67664.1};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:AHA67664.1}.
FT DOMAIN 53..128
FT /note="MalQ N-terminal beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF21226"
SQ SEQUENCE 694 AA; 78516 MW; E0C5BF20600B99AF CRC64;
MESKRLDNAA LAAGISPNYI NAHGKPQSIS AETKRRLLDA MHQRTATKVA VTPVPNVMVY
TSGKKMPMVV EGSGEYSWLL TTEEGTQYKG HITGGKAFNL PTKLPEGYHT LTLTQEDQRA
HCRVIVAPKR CYEPQALLNK QKLWGACVQL YTLRSEKNWG IGDFGDLKAM LVDVAKRGGS
FIGLNPIHAL YPANPESASP YSPSSRRWLN VIYIDVNAVE DFHLSEEAQA WWQLPTTQQT
LQQARDADWV DYSTVTALKM TALRMAWKGF AQRDDEQMAA FRQFVADQGD SLFWQAAFDA
LHAQQVKEDE MRWGWPAWPE MYKNVDSPEV RQFCEEHRDD 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
RKLSATLETM FADDGVNKLL KDLDRRRRAA AKKK
//