MALQ_STRPN
ID MALQ_STRPN Reviewed; 505 AA.
AC P0A3Q0; P29851;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=4-alpha-glucanotransferase;
DE EC=2.4.1.25;
DE AltName: Full=Amylomaltase;
DE AltName: Full=Disproportionating enzyme;
DE Short=D-enzyme;
GN Name=malQ; Synonyms=malM; OrderedLocusNames=SP_2107;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6297760; DOI=10.1016/0092-8674(82)90126-x;
RA Lacks S.A., Dunn J.J., Greenberg B.;
RT "Identification of base mismatches recognized by the heteroduplex-DNA-
RT repair system of Streptococcus pneumoniae.";
RL Cell 31:327-336(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC {ECO:0000305}.
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DR EMBL; J01796; AAA26923.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK76166.1; -; Genomic_DNA.
DR PIR; E95246; E95246.
DR RefSeq; WP_000747291.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P0A3Q0; -.
DR SMR; P0A3Q0; -.
DR STRING; 170187.SP_2107; -.
DR CAZy; GH77; Glycoside Hydrolase Family 77.
DR PRIDE; P0A3Q0; -.
DR EnsemblBacteria; AAK76166; AAK76166; SP_2107.
DR GeneID; 60233823; -.
DR GeneID; 66807186; -.
DR KEGG; spn:SP_2107; -.
DR eggNOG; COG1640; Bacteria.
DR OMA; ETVPHAM; -.
DR PhylomeDB; P0A3Q0; -.
DR BioCyc; SPNE170187:G1FZB-2195-MON; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 InterPro; IPR003385; Glyco_hydro_77.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR32438; PTHR32438; 1.
DR Pfam; PF02446; Glyco_hydro_77; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR TIGRFAMs; TIGR00217; malQ; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Glycosyltransferase; Transferase.
FT CHAIN 1..505
FT /note="4-alpha-glucanotransferase"
FT /id="PRO_0000170129"
SQ SEQUENCE 505 AA; 58076 MW; D4529A000A6D01A5 CRC64;
MKKRQSGVLM HISSLPGAYG IGSFGQSAYD FVDFLVRTKQ RYWQILPLGA TSYGDSPYQS
FSAFAGNTHF IDLDILVEQG LLEASDLEGV DFGSDASEVD YAKIYYARRP LLEKAVKRFF
EVGDVKDFEK FAQDNQSWLE LFAEYMAIKE YFDNLAWTEW PDADARARKA SALESYREQL
ADKLVYHRVT QYFFFQQWLK LKAYANDNHI EIVGDMPIYV AEDSSDMWAN PHLFKTDVNG
KATCIAGCPP DEFSVTGQLW GNPIYDWEAM DKDGYKWWIE RLRESFKIYD IVRIDHFRGF
ESYWEIPAGS DTAAPGEWVK GPGYKLFAAV KEELGELNII AEDLGFMTDE VIELRERTGF
PGMKILQFAF NPEDESIDSP HLAPANSVMY TGTHDNNTVL GWYRNEIDDA TREYMARYTN
RKEYETVVHA MLRTVFSSVS FMAIATMQDL LELDEAARMN FPSTLGGNWS WRMTEDQLTP
AVEEGLLDLT TIYRRINENL VDLKK