ID Q030T7_LACLS Unreviewed; 667 AA.
AC Q030T7;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=4-alpha-glucanotransferase {ECO:0000256|ARBA:ARBA00020295};
DE EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560};
DE AltName: Full=Amylomaltase {ECO:0000256|ARBA:ARBA00031423};
DE AltName: Full=Disproportionating enzyme {ECO:0000256|ARBA:ARBA00031501};
GN OrderedLocusNames=LACR_0723 {ECO:0000313|EMBL:ABJ72285.1};
OS Lactococcus lactis subsp. cremoris (strain SK11).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=272622 {ECO:0000313|EMBL:ABJ72285.1, ECO:0000313|Proteomes:UP000000240};
RN [1] {ECO:0000313|EMBL:ABJ72285.1, ECO:0000313|Proteomes:UP000000240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK11 {ECO:0000313|EMBL:ABJ72285.1,
RC ECO:0000313|Proteomes:UP000000240};
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA Kozyavkin S., Weimer B., Mills D.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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 -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC {ECO:0000256|ARBA:ARBA00005684}.
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DR EMBL; CP000425; ABJ72285.1; -; Genomic_DNA.
DR RefSeq; WP_011675655.1; NC_008527.1.
DR AlphaFoldDB; Q030T7; -.
DR CAZy; GH77; Glycoside Hydrolase Family 77.
DR KEGG; llc:LACR_0723; -.
DR HOGENOM; CLU_014132_2_1_9; -.
DR Proteomes; UP000000240; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR003385; Glyco_hydro_77.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR32518; -; 1.
DR PANTHER; PTHR32518:SF3; 4-ALPHA-GLUCANOTRANSFERASE; 1.
DR Pfam; PF02446; Glyco_hydro_77; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Transferase {ECO:0000313|EMBL:ABJ72285.1}.
SQ SEQUENCE 667 AA; 78937 MW; 7BEFEBEA4A0475BB CRC64;
MVTNTFSIEP YGEKAYHTGI AVPVFSLRTE NSSGVGQFSD LKKLADFTYR SGMDVIQLLP
INDTTTFMDW RDSYPYRAIS VFALHPLYLD IHEFWKSYTK EQQEKLLILE SELNSLEKID
YERCLALKWE YAQIIYQNLA VKYQKTKSYQ QFYKQNEEWL KAYACFSYLR DINKSANFLA
WGKNANYDKN LFDKLKKETS QLDLYIFVQY LLHSQLTEAV DYCHKLGIAL KGDIAIGIAH
DSVDAWTHPE LFHLDKQAGA PPDVFAVNGQ NWGFPTYNWE KMAEDGYDWW KKRLTAMSNY
FDAYRLDHIL GFFRIWQMPE NSVRGLLGQF SPALALSAEE IENNYGIPFR QWGIERFILP
FIKDWVIDEV FGRDNRDWII QTFLDYIGDS NYRFKAEFNN QKAIENTQME NWVREGLYKL
QENVIFLKDD ENSEKYHPRI GLLSTISFRE FGDDYKGRLE RLYNDYFYGR NYDFWKEKAY
EKLPALKNAT KMLACGEDLG MVPDNVPDVM YHLDILRLII ERMPADERFV SSLSEVPYLS
VVTTSSHDTS PLRAWWEENH DLTQRYYNEV MGWYGEAPNY ASVEIIQEII KRNLNSNAMM
VILPIQDWLA MSEHFRKENA KSEQINIPAD PYHYWNYRLH CNLQALIENQ EWTDFLKNFI
KESKRAY
//
