ID A0A2V5IMS3_9MICC Unreviewed; 1217 AA.
AC A0A2V5IMS3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=CVS30_13335 {ECO:0000313|EMBL:PYI37908.1};
OS Arthrobacter psychrolactophilus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=92442 {ECO:0000313|EMBL:PYI37908.1, ECO:0000313|Proteomes:UP000247980};
RN [1] {ECO:0000313|EMBL:PYI37908.1, ECO:0000313|Proteomes:UP000247980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|EMBL:PYI37908.1,
RC ECO:0000313|Proteomes:UP000247980};
RA Liu Q., Xin Y.-H.;
RT "Genetic diversity of glacier-inhabiting Cryobacterium bacteria in China
RT and description of Cryobacterium mengkeensis sp. nov. and Arthrobacter
RT glacialis sp. nov.";
RL Submitted (MAY-2018) 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=ATP + D-maltose = ADP + alpha-maltose 1-phosphate + H(+);
CC Xref=Rhea:RHEA:31915, ChEBI:CHEBI:15378, ChEBI:CHEBI:17306,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:63576, ChEBI:CHEBI:456216;
CC EC=2.7.1.175; Evidence={ECO:0000256|ARBA:ARBA00001537};
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|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_00685}.
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000256|ARBA:ARBA00006219}.
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:PYI37908.1}.
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DR EMBL; QJVC01000015; PYI37908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5IMS3; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000247980; 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; 3.90.1200.10; -; 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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR040999; Mak_N_cap.
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 Pfam; PF18085; Mak_N_cap; 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.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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|HAMAP-Rule:MF_00685,
KW ECO:0000313|EMBL:PYI37908.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000247980};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 744..1095
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 896
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
FT ACT_SITE 949
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
SQ SEQUENCE 1217 AA; 134526 MW; 1759ACF91B191D87 CRC64;
MSDALLTLIA EWLPQQRWYP RKGDAGHGAR LTIAERHELP SPDPAVTLLV LLLRVDFPSL
TSPPYDVGQR LTLHVPLSFH RDSTAVPSNS EASAGAVGTG GVLGTLEEFD GWPDGRVHDG
LADLVFLRAW LSMALGVPQG AADEVQIWRN PELVGGAEDT LSDIRALGAE QSNTSIVFRY
EDRPLIAKFF RILQSGAHPE VEIGRALATV SGKGKFSQVP TLQVVAQQGS SGAVLCVIHN
FIEGAQDGWE RALATAGVSE DFTAHAELIG GALAQVHANL RESMGAHWAE KAETQAFVEV
MAARLEHAWD VARPAVGPYD QKFESIVQRL RHIDRLPQFQ RIHGDLHLGQ LVLRESAPTP
EWFILDFEGE PLRSLYERGQ ADIVIRDLAG MLRSFDYAGA QAAGTGAITR NEGAEWARKS
SDAFILGYEN GSGERTSRNS PLFMALWLDK ALYEVVYELQ NRPTWTWVPV KAVRDLFESM
ESGVDMGLNE MAPLAVNAGV LARISEGSYY APHSVLGAHL DSDGKVTVRA LRHLAESVQL
VTAQGVIPMT HEYGGIWVAV IPAQEADHVP DYRLDVRYAD GVHRTDDPYR YLPTVGELDM
HLIAEGRHET LWTVLGAHVR HYHSELGDVS GVSFTVWAPA VQAVRVIGEF NDWDGRSNAM
RSLGNSGLWE LFIPGVSAGA RYKFEILTES GSWLEKADPM AYGTEVPPLT ASRVVDSSYS
FKDDDWMAKR ATIDPHNSPM SVYEVHLGSW RPGLSYEELA TELVEYVRDL GFTHVELMPV
SEHPFGGSWG YQVTSYYAPT SRFGHPDQFR FLVDSLHQAG IGVIMDWVPA HFPKDEWALA
QFNGGAQYEH ANPQLGEHPD WGTLIFDFGR NEVRNFLVAN ALYWIEEFHI DGLRVDAVAS
MLYLDYSRED GAWSPNRFGG RENLEAISFL QEMNATVYRR NPGVVTIAEE STAFPGVTAP
TSEGGLGFGI KWNMGWMHDS LTYMSEDPVN RGWHHNQITF SLAYAFTENF LLPISHDEVV
HGKGSLLRKM PGDRWQQLAN LRAYLAFQWA HPGKQLIFMG TEFGQEAEWS EAHGLDWWLA
ENPGHSAIQK LVKDLNHNYT SITALSELDN TSEGFTWLNG GDTANNVVSF VRWDKAGKPL
VCIVNFAGVA YEGYRIGIPA AGVWSEALNT DLAIYGGSGV SNTGTLTAEP LPWDGQENSL
RLRVPPLGAL YLTLADS
//
