ID H5Y3T4_9FIRM Unreviewed; 1178 AA.
AC H5Y3T4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
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 ORFNames=DesyoDRAFT_2243 {ECO:0000313|EMBL:EHQ89328.1};
OS Desulfosporosinus youngiae DSM 17734.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=768710 {ECO:0000313|EMBL:EHQ89328.1, ECO:0000313|Proteomes:UP000005104};
RN [1] {ECO:0000313|EMBL:EHQ89328.1, ECO:0000313|Proteomes:UP000005104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17734 {ECO:0000313|EMBL:EHQ89328.1,
RC ECO:0000313|Proteomes:UP000005104};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Land M.L., Hauser L., Pester M.,
RA Spring S., Ollivier B., Rattei T., Klenk H.-P., Wagner M., Loy A.,
RA Woyke T.J.;
RT "The Noncontiguous Finished genome of Desulfosporosinus youngiae DSM
RT 17734.";
RL Submitted (NOV-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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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DR EMBL; CM001441; EHQ89328.1; -; Genomic_DNA.
DR RefSeq; WP_007782944.1; NZ_CM001441.1.
DR AlphaFoldDB; H5Y3T4; -.
DR STRING; 768710.DesyoDRAFT_2243; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG1640; Bacteria.
DR eggNOG; COG3280; Bacteria.
DR HOGENOM; CLU_007997_2_0_9; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000005104; 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:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11338; AmyAc_CMD; 1.
DR CDD; cd02857; E_set_CDase_PDE_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004185; Glyco_hydro_13_lg-like_dom.
DR InterPro; IPR003385; Glyco_hydro_77.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR045857; O16G_dom_2.
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; PF00128; Alpha-amylase; 1.
DR Pfam; PF02446; Glyco_hydro_77; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF81296; E set domains; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361207};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU361207};
KW Reference proteome {ECO:0000313|Proteomes:UP000005104};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:EHQ89328.1}.
FT DOMAIN 154..562
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1178 AA; 135314 MW; 34411D4AD2ACD79E CRC64;
MKFEAYHNSH DVFYRNPFGA VNCGQRIIFR LSTVSSEPIE ACLLRLWETD HETTSLMQKT
VGKRSYDSAS KKMPGEESGQ DESYEVEYQV PGIPGLIWYY FIIKAGSQTY YYGNNSHRLG
GEGCLWEQEP PAYQITVHKP TAVPEWYKRG VIYQVFVDRF FNPLHNRFSC CPKKNALLHA
NWSDQPVYIK DEQGRVTDWD FFGGTLQGIM EKLPYFQELG ISILYFNPIF EAASNHKYDT
ANYLKIDPMY GDDLVFADLI STAKQYGISI ILDGVFSHTG SDSIYFNKYG SYPGAGAYQS
ADSPYYTWYK FKGNREEYES WWGVDDLPEV NEMDSSYRQF IYGPENSVIQ KWQSLGVAGW
RLDVADELPD EFIQELRQRI KSLNPDAVLI GEVWEDASNK ISYDKPRRYL LGDELDGTMN
YPFRDSFLRF ILGRSDAGDL HNEVMSLFEN YPRENFYAAM NLMGSHDTIR ILTLLGEAPP
EQSLTKSQQR TFRLSAAARK LAVQRLKLLS LVQMIFPGVP SIYYGDEAGV EGYADPYNRG
TYPWGREDKE ILAWYRRLVR MHAEFEVLQT GDFSSLSLEA DVYGFRRVGD DEEICVLINR
HGEEAKTVDL KERLKLESSS FVIDLINGEK LFTETLSALS VNALSGRALL IKKNRPPALQ
LQPSCGVLLH ISSLPSAWGL GDLGQEAYDF VDFLAESGHS IWQVLPLNPA GAGDCPYQSE
SVLAGNPLFI SLDHLIYEGL LDLTETRAKY DQLIRIGLRE SLLKEGFKEL KRDLLYEAYQ
LFGEQIKSDN RSFKDSDYLS QENYAKFKKK HKKWLEDYAL FRALKDHFGD APWFAWDTEI
ALRKPEALAK YSYLLREEVG FAEFLQYTFF YQWDKLKIYA MSKGIKMMGD LPHFVAADSC
DVWVNRNLFK LDERGRAAQI AGVPPDYFSK TGQLWGNPVY NWDAHAATEY AWWKMRLEFG
LEQFEYIRLD HFRGFEAFWA VDANEKTAEK GRWIKGPGKR FFESILAAFG KCPFIVEDLG
VITTEVNTLK EMFGFPGIKV HQFTPLKEVA KTETNFVYYT GTHDNNTLLG WYKKKDSSGE
DSPDSTSLQN GRIDQQDILL QACRESIEEV YLSQAVWVIL PMQDILGLGE EARMNVPGTI
HGNWKWQLDK DYNSDELKGW LRTLAEKAKR LEGGSRRG
//