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Database: UniProt
Entry: A0A1M7Z7P8_9BACT
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ID   A0A1M7Z7P8_9BACT        Unreviewed;       671 AA.
AC   A0A1M7Z7P8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, 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=SAMN04488108_1043 {ECO:0000313|EMBL:SHO60810.1};
OS   Algoriphagus zhangzhouensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=1073327 {ECO:0000313|EMBL:SHO60810.1, ECO:0000313|Proteomes:UP000184609};
RN   [1] {ECO:0000313|Proteomes:UP000184609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25035 {ECO:0000313|Proteomes:UP000184609};
RA   Varghese N., Submissions S.;
RL   Submitted (DEC-2016) 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}.
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DR   EMBL; FRXN01000001; SHO60810.1; -; Genomic_DNA.
DR   RefSeq; WP_073570657.1; NZ_SORH01000001.1.
DR   AlphaFoldDB; A0A1M7Z7P8; -.
DR   STRING; 1073327.SAMN04488108_1043; -.
DR   OrthoDB; 9761875at2; -.
DR   Proteomes; UP000184609; 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   Reference proteome {ECO:0000313|Proteomes:UP000184609};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          184..565
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        338
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT   ACT_SITE        391
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ   SEQUENCE   671 AA;  78159 MW;  DAE9073B4FA578A5 CRC64;
     MSKKNIPVLI KDEPWLEGFE KAVQARIDRF HSAKFHIENE FGSILEFANF HQYYGVHYEP
     IRKGWTYREW APAAQQLYLM GDFNNWDRYS HPLKKNRRGD WEIFLPYHDY KDSFIHESKI
     KVHVVGENGS ALDRIPAYIT RVVQDEASHD FSGQLWFPET PYEWKDQNFD PTASTQMPLI
     YECHVGMALE KEGVGTYHEF TQEILPRIKA GGYNAIQLMA VMEHPYYGSF GYHVSNFFAP
     SSRFGTPEEL KALIDTAHSM GIAVIMDIVH SHAVKNVNEG LNEFDGSNHQ YFHPGERGYH
     EGWDSKLFDY GKWEVQQFLL SNIRYWLDEF HFDGFRFDGA TSMLYKHHGH AGFESAESYF
     NEGVDEDAVL YFQLANTVIH EVKPKAISIA EEVSGMPGLC RQVDDGGLGF DFRLAMGIPD
     FWIKTLKHKK DEEWDMFEIW HELTNRPAKE KSIAYAESHD QALVGDKSIA FWLMDKEMYF
     SMSVLQQNLT IDRGISLHKM IRLITLTLGG EGYLNFIGNE FGHPEWVDFP REGNNWSYQY
     ARRQWSLVDT EHLRYQQLNE WDKEIIGLAN NYKIPASPPA IQLYLDPDKK ILAYQRADLI
     FIFSFHPTES YFGYPIPLPE GGEYKIILES DEKRFGGFER LDMDINYSTD EKSNIHVYLP
     NRAAMVLKKI N
//
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