ID J4SFB3_9MYCO Unreviewed; 731 AA.
AC J4SFB3;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000256|HAMAP-Rule:MF_00685};
DE EC=2.4.1.18 {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE Short=BE {ECO:0000256|HAMAP-Rule:MF_00685};
GN Name=glgB {ECO:0000256|HAMAP-Rule:MF_00685};
GN ORFNames=MCOL_V217743 {ECO:0000313|EMBL:EJO87835.1};
OS Mycobacterium colombiense CECT 3035.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1041522 {ECO:0000313|EMBL:EJO87835.1, ECO:0000313|Proteomes:UP000006455};
RN [1] {ECO:0000313|EMBL:EJO87835.1, ECO:0000313|Proteomes:UP000006455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 3035 {ECO:0000313|EMBL:EJO87835.1,
RC ECO:0000313|Proteomes:UP000006455};
RX PubMed=21952541; DOI=10.1128/JB.05928-11;
RA Gonzalez-Perez M., Murcia M.I., Landsman D., Jordan I.K.,
RA Marino-Ramirez L.;
RT "Genome sequence of the Mycobacterium colombiense type strain, CECT 3035.";
RL J. Bacteriol. 193:5866-5867(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. {ECO:0000256|HAMAP-
CC Rule:MF_00685}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00685};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|HAMAP-Rule:MF_00685}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00685}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000, ECO:0000256|HAMAP-
CC Rule:MF_00685}.
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:EJO87835.1}.
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DR EMBL; AFVW02000005; EJO87835.1; -; Genomic_DNA.
DR RefSeq; WP_007773913.1; NZ_CP020821.1.
DR AlphaFoldDB; J4SFB3; -.
DR STRING; 1041522.GCA_002105755_02467; -.
DR GeneID; 31528914; -.
DR eggNOG; COG0296; Bacteria.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000006455; Unassembled WGS sequence.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR CDD; cd11322; AmyAc_Glg_BE; 1.
DR CDD; cd02855; E_set_GBE_prok_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; 2.
DR HAMAP; MF_00685; GlgB; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
DR InterPro; IPR006407; GlgB.
DR InterPro; IPR044143; GlgB_N_E_set_prok.
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 NCBIfam; TIGR01515; branching_enzym; 1.
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; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 259..611
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 411
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 464
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 731 AA; 81954 MW; A45669597ED6D8B0 CRC64;
MSQADQLART HLAPDPADLS RLIAGTHHNP HSILGAHEYG DHTVIRAYRP HAVEVVALVG
DDRFPMQHIE SGLFAVVLPF VNLIDYRLQI TYEGAEPYVV ADAYRFLPTL GEVDLHLFGE
GRHERLWEVL GAHPRSFTTA DGVVTGVSFA VWAPNAKGIN LIGEFNGWTG GEAPMRVLGS
SGVWELFWPG FPLDGLYKFR VHGADGVVTE RADPMAFATE VPPHTASRVT RSEYTWEDAD
WMTERAQRNP VFEPMSTYEV HLGSWRPGLN YRQLARELTD YVVEHGFTHV ELLPVAEHPF
AGSWGYQVTS YYAPTSRFGT PDEFRALVDA LHQAGIGVLV DWVPAHFPKD AWALGRFDGT
PLYEHSDPKR GEQLDWGTYV FDFGRREVRN FLVANALFWL EEFHIDGLRV DAVASMLYLD
YSRPEGGWTP NIYGGRENLE AVQFLQEMNA TVHKTAPGIV TIAEESTSWP GVTRPTTLGG
LGFSMKWNMG WMHDTLDYIS RDPIYRSFHH HEMTFSMLYA FSENYVLPIS HDEVVHGKGT
LWGRMPGNNH VKAAGLRSLL AYQWAHPGKQ LLFMGQEFGQ RAEWSEERGL DWWQLDEQGF
SNGVLRLVRD INDIYRSHPA LWSQDTVPDG YSWIDANDSG NNVLSFLRYG KDGSVMACVF
NFAGAEHGGY RLGLPSAGRW REVLNTDAAA YNGSGIGNMG GVDATEDPWH GRPASALLVL
PPTSALWLEP E
//
