ID F9VG73_LACGL Unreviewed; 655 AA.
AC F9VG73;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN OrderedLocusNames=LCGL_1864 {ECO:0000313|EMBL:BAK61324.1};
OS Lactococcus garvieae (strain Lg2) (Enterococcus seriolicida).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=420890 {ECO:0000313|EMBL:BAK61324.1, ECO:0000313|Proteomes:UP000008520};
RN [1] {ECO:0000313|EMBL:BAK61324.1, ECO:0000313|Proteomes:UP000008520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lg2 {ECO:0000313|EMBL:BAK61324.1,
RC ECO:0000313|Proteomes:UP000008520};
RX PubMed=21829716; DOI=10.1371/journal.pone.0023184;
RA Morita H., Toh H., Oshima K., Yoshizaki M., Kawanishi M., Nakaya K.,
RA Suzuki T., Miyauchi E., Ishii Y., Tanabe S., Murakami M., Hattori M.;
RT "Complete genome sequence and comparative analysis of the fish pathogen
RT Lactococcus garvieae.";
RL PLoS ONE 6:E23184-E23184(2011).
CC -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages
CC in glycogen by scission of a 1,4-alpha-linked oligosaccharide from
CC growing alpha-1,4-glucan chains and the subsequent attachment of the
CC oligosaccharide to the alpha-1,6 position.
CC {ECO:0000256|ARBA:ARBA00002953}.
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; AP009333; BAK61324.1; -; Genomic_DNA.
DR AlphaFoldDB; F9VG73; -.
DR STRING; 420890.LCGL_1864; -.
DR KEGG; lgv:LCGL_1864; -.
DR PATRIC; fig|420890.5.peg.1837; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_011131_2_2_9; -.
DR Proteomes; UP000008520; Chromosome.
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 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:UP000008520};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 173..544
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 327
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 381
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 655 AA; 75644 MW; D0D04D07D6B3861C CRC64;
MMKRRFLRML NILQYDPYLE PYKADLSYRL FEFSRTKKRL LGMEGKLTDF ANGHKYFGFQ
QEKEYWTFRE WAPHAEKAFL VGDFNDWTDK HELKAAYGGI WEIAVPGALP LGSKVKVKLI
INGAEVYRVP SYALYAVQNE YLELDGVIVA PDYQFQHSSP LLEEEAPLIY EAHIGISSEE
HKINTYQEFT QDILPRIKAA GYNTIQLMAI MEHPLYASFG YQVSNFFAIS SRFGRPEDLM
ALIDTAHGMG LRVLLDVVHS HAVKNVGDGL NLFDGSSDQY FHQGARGEHA AWNTKLFNYG
KDEVIHFLLS NLKFWLETYH FDGFRFDGVT SMLYHHHGLG TSFDSYKKYF STDTDIEAVV
YLMLATELVH QVNPQATLIA EDMSAMPGMA LPISEGGIGF DYRLSMGVPD YWIKQFKEKS
DEELDLMQLW WELTTRRPGE KNIGYVESHD QALVGDKTLM MWLANEAIYD AMDIHSTSMV
VDRAIALHKI VRLITFSLAG EGYLNFMGNE FGHPEWLDFP REGNQDSFQH ARRQWSLAAK
ENLRYHYLLK FDHDMIALEK NYHFLKQSDS LQQYWIKNED KLLAYRKGSL LFVLNFHPTM
EKKLQLDVDN PPTFILDTDD QKYGGFGPRS SFSHQKETGK LELSLAARTA MVFQL
//
