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Database: UniProt
Entry: Q3KD67_PSEPF
LinkDB: Q3KD67_PSEPF
Original site: Q3KD67_PSEPF 
ID   Q3KD67_PSEPF            Unreviewed;       692 AA.
AC   Q3KD67;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 109.
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:ABA74288.1};
GN   OrderedLocusNames=Pfl01_2547 {ECO:0000313|EMBL:ABA74288.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA74288.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA74288.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA74288.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(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; CP000094; ABA74288.1; -; Genomic_DNA.
DR   RefSeq; WP_011333966.1; NC_007492.2.
DR   AlphaFoldDB; Q3KD67; -.
DR   CAZy; GH77; Glycoside Hydrolase Family 77.
DR   KEGG; pfo:Pfl01_2547; -.
DR   eggNOG; COG1640; Bacteria.
DR   HOGENOM; CLU_022072_1_0_6; -.
DR   Proteomes; UP000002704; 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   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   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:ABA74288.1};
KW   Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:ABA74288.1}.
SQ   SEQUENCE   692 AA;  76001 MW;  168D918D06FF3BF1 CRC64;
     MSDAQLEILA SRAGLAVDWI DANGRAQKVA PAVLRNVLIG LGHPAGTAQE IDASLLELQQ
     VQENRHLPPL LTADVGVGVD LARYFEPETP CEIHLEDGSR LSLKLDAEAV LPGEIPVGYQ
     QVHIADQQFT LAVAPERCFS VGDAVDSPIP RAWGLSVQLY GLRRPGDGGF GDTQALEELA
     RVAGERGADA LAISPLHAMF SADTGRYSPY SPSSRLFLNP LYAAPGAILG ERALRDAIDA
     AGLTEQFEQL QNLKLIDWPK AAEAKLKLLQ ALYDGFISGE HPLHADFSSF RDAGGEALEN
     HCRFEAIQEM RAARGESLDW RQWPEHWHDP RGAALGAFAE EYAERISYFA FCQWLIHRCL
     ERAQTAARSA GMGIGLIADL AVGADGAGSQ AWSFQDELLA SLTVGAPPDI LNRSGQGWGI
     SAFSPEGLVR NGFRAFIDML RANFAHAGGL RIDHVMGLQR LWVIPNGAVP ADGAYLYYPV
     DDLLRLLTLE SHRHQAIVLG EDLGTVPDGL REKLIARAML GMRVLLFEQD NTFFKPILDW
     PDNALATTST HDLPTLNGWW HGRDIDWNAR LGLIDANGEI DWRRYRERER EGLRNALSQD
     PQNFREESHE ADQVVDAAVR FLGHTRAPLV LLPLEDALGL DEQANLPGTI DTHPNWSRRL
     PATSETLLDG VDAARRLELL ACARLQAAER DQ
//
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