ID A0A1H3DIJ0_9ACTN Unreviewed; 1003 AA.
AC A0A1H3DIJ0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05661080_00731 {ECO:0000313|EMBL:SDX66236.1};
OS Modestobacter sp. DSM 44400.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=1550230 {ECO:0000313|EMBL:SDX66236.1, ECO:0000313|Proteomes:UP000199500};
RN [1] {ECO:0000313|EMBL:SDX66236.1, ECO:0000313|Proteomes:UP000199500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44400 {ECO:0000313|EMBL:SDX66236.1,
RC ECO:0000313|Proteomes:UP000199500};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FNOZ01000003; SDX66236.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3DIJ0; -.
DR STRING; 1550230.SAMN05661080_00731; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000199500; 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; 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 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}; Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00685};
KW Reference proteome {ECO:0000313|Proteomes:UP000199500};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 504..845
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..162
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 656
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
FT ACT_SITE 709
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
SQ SEQUENCE 1003 AA; 107599 MW; 328B132ABD6BFF87 CRC64;
MTIDDASTPA PGGEPADKAE LMRRVEEITE SVRSDAATAD EPTAPQAAAA PARETAAKRA
PAVRKAAAKK ASPAAGEDAV GEDQAPAPAK KATKPAAAKK TAAAPVPDGD ASAPAKATKR
ARATKKVTAT PVVAPAPIAE PGNPSAPSAP QPEPPSRDPA EPSTPQAPAD GQQAGTGGSS
PAETASEPGD PGRTDTGPES ASGAVTTPGG SAPTPAATPA AAVPAGAEPA LAEPAGSGAP
SAAGVPTTTQ GREVSEEELR AVVEGRSYNP HGVLGTHQLP SGWAVRTLRP DAAAVTIVDQ
DGSRYDATQV HDGGVFEARL RGQPGDYRVE VTYPDAEGGT NTHVVDDPYR WLPTLGQLDQ
HLIREGRHEQ LWTVLGAHVR GFDTPGGHVE GVSFAVWAPN ARGVKVTGDF DYWEARAYPL
RSLGSSGVWE VFIPGVQVGT RYRFHVLGTD GQWVVKSDPM AFATEVPPSN ASVVTESAHV
WGDDEWMTQR AEGNWHQRPM SVYEVHAGSW RQGLSYRDMA DELVAYATDA GFTHLEFMPL
AEHPFGGSWG YQVTSYYAPT SRFGSPDDLR YLIDRAHQAG LGIIVDWVPG HFPKDEWALG
RFDGTALYEH GDPRRGEQPD WGTYVFDFGR SEVRNFLVAN ALFWCKEFHV DGIRVDAVAS
MLYLDYSRND GEWTPNVYGG RENLEAVAFL QEMNATLYRE IPGVVTIAEE STSWPGVTRA
THLGGLGFGF KWNMGWMHDS LAYMSKQPVH RSFHHNQLTF SLVYAFSENY VLPISHDEVV
YGKGSLLRKM PGDHWQQLAN LRAFLGYMWA HPGKQLLFMG SEFGQLSEWA ESRSLDWWHL
DDPAHSGVLR LVRDLNTVYK DTEALYSQDS DPAGFQWIDA NDAGGNTLSF LRYGADGQVL
ACVANFAGNP HQEYRIGLPR GGRWRELINT DFDGYGGSGV GNYGGVDAVA ESWHGQPYSA
TLTAPPLATV WLVHEGPDPD EAAADPEQAA GEASGGVEGL DIP
//
