ID W1WUT3_ECOLX Unreviewed; 693 AA.
AC W1WUT3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=Q609_ECAC01687G0002 {ECO:0000313|EMBL:ETJ21977.1};
OS Escherichia coli DORA_A_5_14_21.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=1403943 {ECO:0000313|EMBL:ETJ21977.1, ECO:0000313|Proteomes:UP000018853};
RN [1] {ECO:0000313|EMBL:ETJ21977.1, ECO:0000313|Proteomes:UP000018853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DORA_A_5_14_21 {ECO:0000313|Proteomes:UP000018853};
RA Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA Banfield J.F.;
RT "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT community with otherwise low bacterial novelty that shifts toward anaerobic
RT metabolism during the third week of life.";
RL Submitted (DEC-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}.
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:ETJ21977.1}.
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DR EMBL; AZLZ01001687; ETJ21977.1; -; Genomic_DNA.
DR AlphaFoldDB; W1WUT3; -.
DR PATRIC; fig|1403943.3.peg.3553; -.
DR Proteomes; UP000018853; 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: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 Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:ETJ21977.1}.
FT DOMAIN 53..128
FT /note="MalQ N-terminal beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF21226"
SQ SEQUENCE 693 AA; 78403 MW; 5E89F435E8E803C5 CRC64;
MESKRLDNAA LAAGISPNYI NAHGKPQSIS AETKRRLLDA MHQRTATKVA VTPVPNVMVY
TSGKKMPMVV EGSGEYSWLL TTEEGTQYKG HVTGGKAFNL PTKLPEGYHT LTLTQDDQRA
HCRVIVAPKR CYEPQALLNK QKLWGACVQL YTLRSEKNWG IGDFGDLKAM LVDVAKRGGS
FIGLNPIHAL YPANPESASP YSPSSRRWLN VIYIDVNAVE DFHLSEEAQA WWKLPTTQQT
LQQARDADWV DYSTVTALKM TALRMAWKGF AQRDDEQMAA FRQFVAEQGD SLFWQAAFDA
LHAQQVKEDE MRWGWPAWPE MYQNVDSPEV RQFCEEHRDD VDFYLWLQWL AYSQFADCWE
ISQGYEMPIG LYRDLAVGVA EGGAETWCDR ELYCLKASVG APPDILGPLG QNWGLPPMDP
HIITARAYEP FIELLRANMQ NCGALRIDHV MSMLRLWWIP YGETADQGAY VHYPVDDLLS
ILALESKRHR CMVIGEDLGT VPVEIVGKLR SSGVYSYKVL YFENDHEKTF RSPKAYPEQS
MAVAATHDLP TLRGYWESGD LTLGKTLGLY PDEVVLRGLY QDRELAKQGL LDALHKYGCL
PKRAGHKASL MSMTPTLNRG LQRYIADSNS ALLGLQPEDW LDMAEPVNIP GTSYQYKNWR
RKLSATLEAM FADDGVNKLL KDLDRRRRAA AKK
//