ID   MALQ_HAEIN              Reviewed;         699 AA.
AC   P45176;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 119.
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; OrderedLocusNames=HI_1356;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; L42023; AAC23003.1; -; Genomic_DNA.
DR   PIR; H64118; H64118.
DR   RefSeq; NP_439507.1; NC_000907.1.
DR   AlphaFoldDB; P45176; -.
DR   SMR; P45176; -.
DR   STRING; 71421.HI_1356; -.
DR   CAZy; GH77; Glycoside Hydrolase Family 77.
DR   EnsemblBacteria; AAC23003; AAC23003; HI_1356.
DR   KEGG; hin:HI_1356; -.
DR   PATRIC; fig|71421.8.peg.1409; -.
DR   eggNOG; COG1640; Bacteria.
DR   HOGENOM; CLU_022072_1_1_6; -.
DR   OMA; GPVGQNW; -.
DR   PhylomeDB; P45176; -.
DR   BioCyc; HINF71421:G1GJ1-1381-MON; -.
DR   Proteomes; UP000000579; 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;
KW   Reference proteome; Transferase.
FT   CHAIN           1..699
FT                   /note="4-alpha-glucanotransferase"
FT                   /id="PRO_0000170126"
SQ   SEQUENCE   699 AA;  80252 MW;  80D6E1D51EC2E1E9 CRC64;
     MVSMQISDSL KQKAEKCGIA LSHYDIDGHL IFADEKTVST FVELLQPPPK AKGQFDDVLA
     AFENEPIDYR LNRLDLPPSA EYRYQLTDES NAILLEKILS NLSVLSLPPL PFGYYQLSIF
     SDTEQYRIRL LISPKTAFQP PVLENKKVWG VNVQLYSLRS EQNWGIGDFG DLAYLIEQSA
     KQGADYVGIN PLHLPYPAVP NWASPYSSSS RRWLNFLYLD IPDLPEFKRC RSVQNWFKRE
     DIQAKIAALR ESDCVDYSSI LALKLTALEP LFDFFQRSQS VEIVTRRKIF AEYLKNKGEP
     LLLQGLFNVL DLQEHADHQA EENTIGWLGW RKEWQHLSAA KRKALLKTHH EKIQFFAWLQ
     WLTEEQLSAL QNLCKQSGMK LGIYGDLAVN SSRGSADVWS DPDLYCVNAS IGAPPDPLGP
     VGQNWNLPPY NPTVLKARGF APFIDMLCAN MQYFGVLRID HVMGLFRLWW IPKGKTAADG
     AYVHYPFDEL MAILAIESVR NECLIIGEDL GTVPDEVRWK LNEFQIFSYF VLYFAQRNGE
     FPRISDYPRN AYATIGTHDV PSLQSFWHCR DLELFNQLGI LNGEVLKQKY DQRVMDKQAL
     LNSLHRDNYL PPHYEGDALS MAMHDYLNRM IHYYLAESNS RLIGVQLENL LSQEISFNLP
     STSNEYPNWC KKLAQPLAFI FSNEALKTFF VQINQGRNV