ID E0Q471_9STRE Unreviewed; 505 AA.
AC E0Q471;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:EFM34553.1};
GN ORFNames=HMPREF9189_1852 {ECO:0000313|EMBL:EFM34553.1};
OS Streptococcus sp. oral taxon 071 str. 73H25AP.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=864570 {ECO:0000313|EMBL:EFM34553.1, ECO:0000313|Proteomes:UP000005184};
RN [1] {ECO:0000313|EMBL:EFM34553.1, ECO:0000313|Proteomes:UP000005184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73H25AP {ECO:0000313|EMBL:EFM34553.1,
RC ECO:0000313|Proteomes:UP000005184};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (AUG-2010) 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:EFM34553.1}.
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DR EMBL; AEEP01000016; EFM34553.1; -; Genomic_DNA.
DR RefSeq; WP_000747313.1; NZ_GL397254.1.
DR AlphaFoldDB; E0Q471; -.
DR eggNOG; COG1640; Bacteria.
DR HOGENOM; CLU_014132_1_0_9; -.
DR Proteomes; UP000005184; 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:EFM34553.1};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:EFM34553.1}.
SQ SEQUENCE 505 AA; 58044 MW; DBCB06B20284B7F0 CRC64;
MKKRQSGVLM HISSLPGAYG IGSFGQTAYD FVDFLVRTKQ RYWQILPLGT TSYGDSPYQS
FSAFAGNTHF IDLDILVEQG LLEASDLEGV DFGSDASEVD YAKIYYARRP LLEKAVKRFL
EVGDVKDFEK FAQDNQSWLE LFAEYMAIKE HFDNLAWTEW PDADARARKA SALESYREKL
ADKLVYHRVT QYFFFQQWLK LKAYANDNHI EIVGDMPIYV AEDSSDMWAN PHLFKTDATG
KATCIAGCPP DEFSATGQLW GNPIYDWEAM DKDGYKWWIE RLRESFKIYD IVRIDHFRGF
ESYWEIPAGS DTAAPGKWVK GPGYKLFAAV KEELGELNII AEDLGFMTDE VIELRERTGF
PGMKILQFAF NPEDESIDSP HLAPANSVMY TGTHDNNTVL GWYRNEIDDP TREYMARYTN
RKEYETVPHA MLRTIFSSVS FMAIATMQDL LELDESARMN FPSTLGGNWS WRMTADQLTP
AVEETLLDLT TIYRRINENL VELKK
//
