ID F3UUL2_STRSA Unreviewed; 503 AA.
AC F3UUL2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
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:EGJ41474.1};
GN ORFNames=HMPREF9380_0200 {ECO:0000313|EMBL:EGJ41474.1};
OS Streptococcus sanguinis SK49.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=888808 {ECO:0000313|EMBL:EGJ41474.1, ECO:0000313|Proteomes:UP000006459};
RN [1] {ECO:0000313|EMBL:EGJ41474.1, ECO:0000313|Proteomes:UP000006459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK49 {ECO:0000313|EMBL:EGJ41474.1,
RC ECO:0000313|Proteomes:UP000006459};
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 (MAR-2011) 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:EGJ41474.1}.
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DR EMBL; AFFO01000002; EGJ41474.1; -; Genomic_DNA.
DR RefSeq; WP_002931828.1; NZ_GL890985.1.
DR AlphaFoldDB; F3UUL2; -.
DR PATRIC; fig|888808.3.peg.194; -.
DR eggNOG; COG1640; Bacteria.
DR HOGENOM; CLU_014132_1_0_9; -.
DR Proteomes; UP000006459; 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:EGJ41474.1};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:EGJ41474.1}.
SQ SEQUENCE 503 AA; 57849 MW; 5EF4AB72CDE2FD58 CRC64;
MKKRQSGVLM HISSLPGKYG IGSFGQSAYD FVDFLVRTKQ RYWQILPLGT TSYGDSPYQS
FSAFAGNTYF IDFDILIEEG LLDEADVKGA DFGDDPKKVD YAKIFDARRP IMEKAVARFL
KADDLSDYES FVEQNAAWLE VFAEYMAIKE HFDNLAWTEW PDEAIRRRDA ASLASYREKL
ADKLTYHRVT QYLFFKQWLR LKAYANEHHI EIVGDMPIYV AADSADVWAQ PHFFKTDAVG
KPTCVAGCPP DEFSETGQLW GNPIYDWEAM DKDGYAWWIE RLRESFKIYD IVRIDHFRGF
ESYWEVPAGS ETSASGKWVK GPDYKLFAAV KEALGDLNII AEDLGFMTDE VIELRERTGF
PGMKILQFAF NPDDESIDSP HQAPNNSVMY TGTHDNNTVL GWYKDEIDDA TRQYMAQYTN
RKEYETVPHA MLRTIFASVS FMAIATMQDL LELDSAARMN YPSTIGGNWT WRMTAEELNP
IVEGELYSLT KTYRRMNTDL INE
//
