ID H3K9X1_9FIRM Unreviewed; 1139 AA.
AC H3K9X1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
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=HMPREF9454_02044 {ECO:0000313|EMBL:EHR34538.1};
OS Megamonas funiformis YIT 11815.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Megamonas.
OX NCBI_TaxID=742816 {ECO:0000313|EMBL:EHR34538.1, ECO:0000313|Proteomes:UP000005963};
RN [1] {ECO:0000313|EMBL:EHR34538.1, ECO:0000313|Proteomes:UP000005963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11815 {ECO:0000313|EMBL:EHR34538.1,
RC ECO:0000313|Proteomes:UP000005963};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Megamonas funiformis YIT 11815.";
RL Submitted (JAN-2012) 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:EHR34538.1}.
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DR EMBL; ADMB01000088; EHR34538.1; -; Genomic_DNA.
DR RefSeq; WP_008539608.1; NZ_JH601092.1.
DR AlphaFoldDB; H3K9X1; -.
DR STRING; 437897.GCA_900128435_00919; -.
DR PATRIC; fig|742816.3.peg.1982; -.
DR HOGENOM; CLU_007997_0_1_9; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000005963; 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: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; 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361207};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU361207};
KW Transferase {ECO:0000256|RuleBase:RU361207, ECO:0000313|EMBL:EHR34538.1}.
FT DOMAIN 137..543
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1139 AA; 132204 MW; 3F19901F96C00A37 CRC64;
MIFHDSQNLY YRSPIGAVPT QSFVRLAIDV DLKDKVSLVR LHTWQETCGS IYYNLKKSSW
DEKHYFIDLD MPEDGCLVWY YFIIELVDGK LLYYGNNKAQ MGDIGQEALE VPPSYQITVF
KKDVKTPDWF KKAVMYQIFP DRFYRSGNNI PQKKHAVLHC DWNEPPMYYL DPDTKNVVTY
DYFGGNIQGI KEKLSYLKDL GISVIYFNPI FKSRANHHYD TADYHQVDPM FGTNEEFAQL
CSQAKEMGIR IILDGVFSHT GSDSIYFNRF GNFDSVGAYQ SKESPYYEWY DFKEYPCKYD
CWWGFTSMPN TKETTPSYMD FIIRSEDSVM NFWMDKGISG WRLDVIDELP QKFTRCFYQK
LKKLDKDAVI IGEVWEDASN KIAYNVHREY LCGYELDSAM NYPLRRIILD FILRNKSAQE
TEVSILNQHE NYPEENLYAM MNLLGSHDVE RILTLLGEAP SVENVPASVQ AKFKLDDAHL
RLAIARLKLA VVWQMTLPGV PSIYYGDEIG MQGYRDPHNR ASYKWDEADN NLRHFFTRMI
ALRNHRQVLQ TGWYIPVYAQ DDVLAYMRTT KLGKDRFGQK MDDDCILVVL NRHQEKTMTI
EIDVHGFCQR KLHEITNMYP DVEIIDNKAK IEIEPLTALV FEQEKENIEY ARKAGIIMHP
TSLPSDYGIG DLGKEAYNFV DWLVKAKQKI WQVLPLNPVG YGASPYQSPS AFAGNTMLIS
PEKLVEINLL EAKDIVLDYK ADVDKVDFVK VEAYKEKILT KAFANFVADA DYTAFCQQQS
YWLEDYALFM ALKKYYKNLP WYEWNLDIKL RKPQALESCR ISLAQDIAYA KFKQYIFFKQ
WQDLHAYANE RGIQIVGDVP IFPSHDSADV WVHQDLFNLN ADGTLKTAAG VPPDYFSEDG
QLWGNPHYLW KVMQRDDYSW WRKRIATLLN LVDIIRIDHF RGFEAYWEVS GMATNARVGK
WVKGPGKDLF DKIKEYLGDV PIIAEDLGVI TPEVEALKNS CNFPGMKVLQ FELYANKYHK
LNFISPKNSI VYTGTHDNNT TLGWLKEDIS PQDKAVLADL LEVKVDDNEA LLEELVKLAY
ASASKMAILP MQDVLKLDSN ARMNLPGTVG TNWGWRMQKD TLTDEKAMYL CSLVEKYNR
//