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Entry: A0A0G3GZS7_9CORY
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ID   A0A0G3GZS7_9CORY        Unreviewed;       715 AA.
AC   A0A0G3GZS7;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
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:AKK06639.1};
GN   ORFNames=CMUST_11640 {ECO:0000313|EMBL:AKK06639.1};
OS   Corynebacterium mustelae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=571915 {ECO:0000313|EMBL:AKK06639.1, ECO:0000313|Proteomes:UP000035199};
RN   [1] {ECO:0000313|EMBL:AKK06639.1, ECO:0000313|Proteomes:UP000035199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45274 {ECO:0000313|EMBL:AKK06639.1,
RC   ECO:0000313|Proteomes:UP000035199};
RX   PubMed=26358597;
RA   Ruckert C., Eimer J., Winkler A., Tauch A.;
RT   "Complete Genome Sequence of the Type Strain Corynebacterium mustelae DSM
RT   45274, Isolated from Various Tissues of a Male Ferret with Lethal Sepsis.";
RL   Genome Announc. 3:e01012-15(2015).
RN   [2] {ECO:0000313|Proteomes:UP000035199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45274 {ECO:0000313|Proteomes:UP000035199};
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete genome sequence of Corynebacterium mustelae DSM 45274, isolated
RT   from various tissues of a male ferret with lethal sepsis.";
RL   Submitted (MAY-2015) 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; CP011542; AKK06639.1; -; Genomic_DNA.
DR   RefSeq; WP_047262628.1; NZ_CP011542.1.
DR   AlphaFoldDB; A0A0G3GZS7; -.
DR   STRING; 571915.CMUST_11640; -.
DR   KEGG; cmv:CMUST_11640; -.
DR   PATRIC; fig|571915.4.peg.2486; -.
DR   OrthoDB; 9811841at2; -.
DR   Proteomes; UP000035199; 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   InterPro; IPR048458; MalQ_N.
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   Pfam; PF21226; MalQ_N; 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:AKK06639.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035199};
KW   Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:AKK06639.1}.
FT   DOMAIN          72..164
FT                   /note="MalQ N-terminal beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF21226"
SQ   SEQUENCE   715 AA;  78907 MW;  89A379E905252857 CRC64;
     MGYQETLREL AGAHAISTSY TGFGGNTIDV SDDTLIKTLR ALGVDLGTEE FPSEETLNEA
     LNIRHDSEFR RPLPRCIVTT DATTHAFNVH VHDGAPAELT ITFEDGNVTE VTNQLENWTP
     ARTIDDITWG EATFELPAGL PQGWHTITLV SDGVTDSCTL IVTPARLSTT DTYINSPVAG
     VMAQMYSVRS EKSWGIGDFN DLGFLGETIA KEGAGDFLLI NPMHAAEPFP PIEDSPYLPT
     TRRFTNPIYI RVEDIPEMEL LDENTRSDID DIAAEFAANN RDSENIERNP IYEAKLQVLR
     EIFLAGRDET REQQFRDFIH QEGDGLAEFA SWCAQRDLNE QTGHGNHAAV PEVEELTEFY
     MWLQWICDSQ LAAAQARCIE AGMKIGIMAD LAVGVHPGGA DAENLAAVLA PDASVGAPPD
     SYNQHGQDWS QPPWHPEKLA EVGYKPWRDM LRTVLRHSGG IRVDHVLGLF RLFWIPRMQH
     PSTGTYVNYD FHALVGILAL EAERAGAVVI GEDLGTFEPW VQDVLAGYGI MGTNILWFES
     SPHHGGARRK EEYRTAALAS VTTHDLPPTA GYLEGEHIAL RERLGLLITD AEQDIAEDLA
     WQAQVLNRVL EQGGFDGEDF EMDTFEGRAR NERGDTDVLV AATHRFIAHT PAALSCTALV
     DMVGDRKVQN QPGTTKDLYP NWCVPLSDAE GNVVLIEDLA SNPLFKKIAA AGKRP
//
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