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Database: UniProt
Entry: A0A0M0BUF9_9ARCH
LinkDB: A0A0M0BUF9_9ARCH
Original site: A0A0M0BUF9_9ARCH 
ID   A0A0M0BUF9_9ARCH        Unreviewed;       669 AA.
AC   A0A0M0BUF9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE            EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN   ORFNames=AC479_07885 {ECO:0000313|EMBL:KON32099.1};
OS   miscellaneous Crenarchaeota group-6 archaeon AD8-1.
OC   Archaea; Candidatus Bathyarchaeota; Candidatus Bathyarchaeia.
OX   NCBI_TaxID=1685126 {ECO:0000313|EMBL:KON32099.1, ECO:0000313|Proteomes:UP000037259};
RN   [1] {ECO:0000313|EMBL:KON32099.1, ECO:0000313|Proteomes:UP000037259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD8-1 {ECO:0000313|EMBL:KON32099.1};
RA   Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA   Teske A.P.;
RT   "New insights into the roles of widespread benthic archaea in carbon and
RT   nitrogen cycling.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a
CC         primary hydroxy group in a similar glucan chain.; EC=2.4.1.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00000826};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC       subfamily. {ECO:0000256|ARBA:ARBA00009000}.
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:KON32099.1}.
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DR   EMBL; LFWW01000066; KON32099.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0BUF9; -.
DR   STRING; 1685126.AC479_07885; -.
DR   PATRIC; fig|1685126.3.peg.642; -.
DR   Proteomes; UP000037259; Unassembled WGS sequence.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0102752; F:1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis); IEA:UniProtKB-EC.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR   CDD; cd11321; AmyAc_bac_euk_BE; 1.
DR   CDD; cd02854; E_set_GBE_euk_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR037439; Branching_enzy.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
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   PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR   PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF02922; CBM_48; 1.
DR   PIRSF; PIRSF000463; GlgB; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          173..538
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   669 AA;  78175 MW;  813F89BC33AE7782 CRC64;
     MRLEDRLSRL LKSDLALMPF SDQIRHRLEL IEKTEKVLTQ SKMSLADFAS GHEYFGLHFS
     KDEWIFREWA PNATEIFIIG DMSNWQERKD FSLQKINNGV WEIHLDPYQL AHGDLYRLSV
     RWTGGRGDRI PAYARRVVQD PKTLIFNAQV WSPKPYQWKI KGIQFKEAPI IYEAHVGMSQ
     EEEKIGTFKE FTNKVLPRIV DAGYNTIQLM AIQEHPYYAS FGYQVSSFFA PSSRFGTPED
     LKELIDLAHS QGLRVFMDLI HSHAASNEVE GLSCFDGTPF QYFHEGPRGK HRAWDSCCFD
     YNKPEVLHFL LSNCRYWLDE YRFDGFRFDG VTSMIYLQHG LGRIFTSYND YFDGSVDEEA
     LTYLALANKM IHNIYPNATT IAEDVSGMPG LAVSSSNGGF GFDYRFAMGI PDYWIRLIKD
     YKDEEWPIGH LWYELTNRRK DEKTISYAES HDQALVGDQT LIFRLIGQDM YEHMQINDYN
     LRVARGIALH KMIRMITLAT AGHGYLNFMG NEFGHPDWID FPRQGNNWSY KYARRQWHLV
     DDHKLKYHLL AKFDQDLITL AKEHDLFSTS NIQLLHEDST NKIIIFQRKN LIFIFNFHPQ
     QSYQNYQFHA PPGKYHMLID SDATKYGGHG RLIPKQTHLT ITKKTKTKIE YVLSLYLPSR
     SAFVLYSIK
//
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