ID D2Q8G2_BIFDB Unreviewed; 816 AA.
AC D2Q8G2;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=GlgX2 Glycogen operon protein glgX {ECO:0000313|EMBL:ADB09098.1};
DE EC=2.4.1.18 {ECO:0000313|EMBL:ADB09098.1};
GN Name=glgX2 {ECO:0000313|EMBL:ADB09098.1};
GN OrderedLocusNames=BDP_0421 {ECO:0000313|EMBL:ADB09098.1};
OS Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / Bd1).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB09098.1, ECO:0000313|Proteomes:UP000008693};
RN [1] {ECO:0000313|EMBL:ADB09098.1, ECO:0000313|Proteomes:UP000008693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC {ECO:0000313|Proteomes:UP000008693};
RX PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., Bottacini F.,
RA Canchaya C., Claesson M.J., He F., Mantzourani M., Mulas L., Ferrarini A.,
RA Gao B., Delledonne M., Henrissat B., Coutinho P., Oggioni M., Gupta R.S.,
RA Zhang Z., Beighton D., Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT adaptation to the human oral cavity.";
RL PLoS Genet. 5:E1000785-E1000785(2009).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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DR EMBL; CP001750; ADB09098.1; -; Genomic_DNA.
DR RefSeq; WP_012901877.1; NC_013714.1.
DR AlphaFoldDB; D2Q8G2; -.
DR STRING; 401473.BDP_0421; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; bde:BDP_0421; -.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_011725_1_1_11; -.
DR Proteomes; UP000008693; 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:0004133; F:glycogen debranching enzyme activity; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005980; P:glycogen catabolic process; IEA:InterPro.
DR CDD; cd11326; AmyAc_Glg_debranch; 1.
DR CDD; cd02856; E_set_GDE_Isoamylase_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; 1.
DR InterPro; IPR044505; GlgX_Isoamylase_N_E_set.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR011837; Glycogen_debranch_GlgX.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR NCBIfam; TIGR02100; glgX_debranch; 1.
DR PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR PANTHER; PTHR43002:SF1; ISOAMYLASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00128; Alpha-amylase; 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:0000313|EMBL:ADB09098.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008693};
KW Transferase {ECO:0000313|EMBL:ADB09098.1}.
FT DOMAIN 212..642
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 535..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 92001 MW; B8D423CE1E7B819F CRC64;
MRNPPLHRYA TRPGLYFTDD GGADAVVRSE TADQVWFCVL EPLDQPSAFY AEAVRLFNEP
DISFIEQAQS QKICTRRIPS LNLRETLFMM DGPNYGLWYV HIPKAWDGMH YGYRVNGPWD
PNHGVSFNPY KLLLDPYAKG IDGSMKLNPG AFAYACEIMN GKVKGSPFGP MSTVDSLGHM
PVSVAIDDRD ANKHEGEPSH PHVAWSKTII YELHVKGFTA NAPWLPKELR GTYAGLAHPS
TLSYLQDLGV TSIELMPIQA KQPELFLQER GRTNYWGYST LGYFAPEPSY ATRAAQEAGA
AAVRKEVIDM VRALHEAGFE VIMDVVYNHT CESGPEGPTI CWRGLDNLSY YRRNKEKISR
LYDTTGCGNT LDFTNTHVVT FAVDSLRYWA KRIGIDGFRF DLAATLARLD GDFTSYHPFL
YALRSDMLLG NLKMIMEPWD VGPGGWRTGQ FGIPFAEWND RFRDTTRKFW LTDVKRNRGG
ESGVVTMQEM ATRLCGSADL FATDPGRGST ASVNYVACHD GFTMADLTRY RHKHNERNGE
DNRDGTNDNH SVNFGYEGPS DDPIIIQQRE RAMANMLGML LLSLGTPMLL SGDEFGNSQN
GNNNAYMQDN PTTWLDWDWL YSTEQTPELK QFDLVSRLIA LRKSRDLYDH EDFFTRLSKI
GLLKRSDRVH WFLPSGHAPH DADWTNPAVR TFAMQLLSPD GSSLMILING SDEISRFHLP
ADKEWEMVWS SAEVSGEYPG QGTSVDRVAE LNEESENKPA GRFSDHLHRL NMMYWHADVN
DGAVPEDIYD AEGADDPTLW TIPALSISVM RQISAD
//