ID D5H6V2_SALRM Unreviewed; 506 AA.
AC D5H6V2;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
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:CBH23757.1};
GN OrderedLocusNames=SRM_00836 {ECO:0000313|EMBL:CBH23757.1};
OS Salinibacter ruber (strain M8).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=761659 {ECO:0000313|EMBL:CBH23757.1, ECO:0000313|Proteomes:UP000000933};
RN [1] {ECO:0000313|EMBL:CBH23757.1, ECO:0000313|Proteomes:UP000000933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:CBH23757.1,
RC ECO:0000313|Proteomes:UP000000933};
RX PubMed=20164864; DOI=10.1038/ismej.2010.6;
RA Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P.,
RA Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I.,
RA Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R.,
RA Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.;
RT "Fine-scale evolution: genomic, phenotypic and ecological differentiation
RT in two coexisting Salinibacter ruber strains.";
RL ISME J. 4:882-895(2010).
RN [2] {ECO:0000313|Proteomes:UP000000933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|Proteomes:UP000000933};
RG Genoscope;
RT "Genome sequence of Salinibacter ruber M8.";
RL Submitted (APR-2010) 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; FP565814; CBH23757.1; -; Genomic_DNA.
DR RefSeq; WP_013061266.1; NC_014032.1.
DR AlphaFoldDB; D5H6V2; -.
DR KEGG; srm:SRM_00836; -.
DR PATRIC; fig|761659.10.peg.932; -.
DR HOGENOM; CLU_014132_1_0_10; -.
DR Proteomes; UP000000933; 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:CBH23757.1};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:CBH23757.1}.
SQ SEQUENCE 506 AA; 57245 MW; 7771D06E44ACC2D9 CRC64;
MDSRRTSGLL LPVSALPSRY GIGDLGPAAF QFADLLTRTN QRLWQVLPVG PIGPGASPYS
SPSTFAGNPL LISPEPLVED GLLTEDDLAP LTELPADHVD YARLVPRKRK VLRTAFRRFR
ADVSTPEATR VQQFRASQSA WLDDYALYAA LKDAHGGSAW TEWSSALVRR DLEALKRARD
EHETAIERHV YWQYLFHRQW TALQAYCHAR DIRLFGDLPI YVAPDSADVW AHQERFRLDD
DGTPTSVAGV PPDYFSPEGQ RWGNPLYRWD RMEEHDFAWW TERLRRAFEL FDLVRLDHFR
GFDEYWSIPA GHDTAIDGSW ESGPGAAFFR AMEDEFGELP VVAEDLGIVT DSVGALRDTF
DFPGMAVLQF AFGGGPDNDF LPHHHRRNMV AYTGTHDNNT IVGWWRDDLS DKERNFAHSY
LNLPDTNPDE SVHRQALRAM MASVADRVVT PLQDVIGLGS EGRINTPGTM GDNWAWRFTP
DQIAEEDETR LAQLTHLYGR ASGYGD
//
