ID A7HEX0_ANADF Unreviewed; 1217 AA.
AC A7HEX0;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 24-JAN-2024, entry version 109.
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 OrderedLocusNames=Anae109_3070 {ECO:0000313|EMBL:ABS27266.1};
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS27266.1, ECO:0000313|Proteomes:UP000006382};
RN [1] {ECO:0000313|EMBL:ABS27266.1, ECO:0000313|Proteomes:UP000006382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS27266.1,
RC ECO:0000313|Proteomes:UP000006382};
RX PubMed=25614562; DOI=10.1128/genomeA.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
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|HAMAP-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}.
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DR EMBL; CP000769; ABS27266.1; -; Genomic_DNA.
DR AlphaFoldDB; A7HEX0; -.
DR STRING; 404589.Anae109_3070; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; afw:Anae109_3070; -.
DR eggNOG; COG0296; Bacteria.
DR eggNOG; COG3281; Bacteria.
DR HOGENOM; CLU_269035_0_0_7; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000006382; Chromosome.
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; 1.
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 InterPro; IPR012811; TreS_maltokin_C_dom.
DR NCBIfam; TIGR01515; branching_enzym; 1.
DR NCBIfam; TIGR02457; TreS_Cterm; 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; 1.
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}; Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00685};
KW Reference proteome {ECO:0000313|Proteomes:UP000006382};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 733..1104
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 549..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 892
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
FT ACT_SITE 945
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685"
SQ SEQUENCE 1217 AA; 135115 MW; 9BC59B027EF083BB CRC64;
MDASLSRLTT TGPWDELLHG PGRAGLEAAL PPYLVGRRWF GGKARRIQRV ELLDAAPVGP
GPGASRLVFL RVSYGDSAPE VYSLPLAFAP GPWADRVHGA WPGSEVALLE AGGEQGVLYA
TDRDPAFSRA LLDAIAHGRT LKGRGGEIVA WSTRAFARRS EGVEELVPTP LGGEQSNTSI
RFGDRMILKL FRRTEAGPNP ELEVGAYLTE RAAFPNVPAV LGAVEYRPRG GEPHVLALLQ
AFVPNRGDAW EFTLAELSAF LDRAAGRAPP AAPAAALVEL AGVAPPPELR ALAAPSLDAA
ALLGRRTAEL HLALARGVDE EAFRPEPFSR EDRRRLHDGA RAQVRAALAL LRRRRDVLPP
EVRARAEAVL AREDELELGL RWVLDRPLTA LRTRTHGDFH LGQVLRTGGD YVVIDFEGEP
ARPMAERRAK ASPLRDVAGM VRSLHYAAHA GPARRAERPD AAPGEAAHAQ AWARVWYAWV
AASFLRAYLD AARGARFLPA GGELRELLAL YLTEKALYEL AYELNNRPDW VRLPLEGIAE
LLGAAEAGAR EREDALPTKG TREAPRAAAR EAREGGAPGA VLARGGPGEL DRHLWNEGTN
HRAYRTLGAH PQTIDGAAGT SFTVWAPNAE RVSVIGDFNG WDKERHPLRR IDDSGLWQGF
LPGVGKGAVY KYHLRSRERG YAVDKADPFG FMHETAPGTQ SIVWDLAYAW GDDAWMRARR
ERNGLASPMS VYEVHLGSWR RVPEEGNRPL TYRELAPLLA DHVAALGFTH VELLPVTEHP
FYGSWGYQTT GYFAPTSRYG TPQDFMFLVD TLHQRGIGVI LDWVPSHFPT DEHGLAYFDG
THLFEHADRR QGHHPDWDSF IFNYGRNEVR SFLLSSALFW LDAYHADGLR VDAVASMLYL
DYSRKHGEWI PNKYGGRENL EAIDFLRRFN EVVYAEYPDV QTIAEESTSW PMVSRPLYVG
GLGFGMKWDM GWMHDTLAYM GHDPVFRKFH HNEVTFRMMY AFSENFVLAL SHDEVVHGKR
SLLGRMPGDA WQKLANLRLL YAYQWAQSGK KLLFMGGELA QGQEWSHERS LDWHLLGIEG
HAGVRTWVED LNRLMRENPA LHVRDFEPAG FEWIDANDAE ASVLSFLRKG REGDPEILVV
LNFTPVARPN YRVGVPRGGF WREVLNSDAQ RYGGSGWGNL GGQEAAPVGA HGRLHSLSLT
LPPLGALFFR HEPAGER
//
