ID D0YQJ9_9ACTO Unreviewed; 497 AA.
AC D0YQJ9;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
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:EEZ91869.1};
GN ORFNames=HMPREF0578_1114 {ECO:0000313|EMBL:EEZ91869.1};
OS Mobiluncus mulieris 28-1.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Mobiluncus.
OX NCBI_TaxID=596328 {ECO:0000313|EMBL:EEZ91869.1, ECO:0000313|Proteomes:UP000005581};
RN [1] {ECO:0000313|EMBL:EEZ91869.1, ECO:0000313|Proteomes:UP000005581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-1 {ECO:0000313|EMBL:EEZ91869.1,
RC ECO:0000313|Proteomes:UP000005581};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (NOV-2009) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEZ91869.1}.
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DR EMBL; ADBR01000020; EEZ91869.1; -; Genomic_DNA.
DR RefSeq; WP_004011883.1; NZ_ADBR01000020.1.
DR AlphaFoldDB; D0YQJ9; -.
DR eggNOG; COG1640; Bacteria.
DR Proteomes; UP000005581; Unassembled WGS sequence.
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:EEZ91869.1};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:EEZ91869.1}.
SQ SEQUENCE 497 AA; 55916 MW; 05BEA8064C52206E CRC64;
MGSRCAGVLL PVFSLPGFYG IGTIGQEARG FIDRLAAAGQ RIWQILPLCP PGYGASPYSS
HSTNAGNPWF IDLNSLVAKN WLAPHEIESL DWGDVPNRVN YAKVEQSSRK VLHLACARAG
KWVESPDFVA FHEANPWVTD YALFMALKTH FGGVSWLEWP QEFRNRQPEA LERARRELAK
EIEFHLFSQW VFESQWEDLH QYASSQGIQI LGDIPIYVSL DSVDTWVNPE LFQLGADKLP
SNVAGVPPDG FSATGQIWGN PLYDWPAHRR EDFAWWKERL RVQLRRVDLL RVDHFRGLES
YFAVPTGAKT AGAGHWEPGP GLEFFQAMEA ELGDLPLVLE DLGYMTEEVR QLREATGKPG
IQLIQFAFDS REPANYWPYE MPRNAVVYTG THDNDTLRGW FDSLSSADQE LARVYCAAQD
TALADLPRCF LTLAMTSVAD TCIIPVADYL GLGSEGRINT PSVANGNWEW KLDETTLGAI
PWTFIDQLTR ISGRYSE
//
