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Database: UniProt
Entry: H3K9X1_9FIRM
LinkDB: H3K9X1_9FIRM
Original site: H3K9X1_9FIRM 
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
//
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