GLGB_PHOPR
ID GLGB_PHOPR Reviewed; 716 AA.
AC Q6LHN1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000255|HAMAP-Rule:MF_00685};
DE EC=2.4.1.18 {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme {ECO:0000255|HAMAP-Rule:MF_00685};
DE Short=BE {ECO:0000255|HAMAP-Rule:MF_00685};
GN Name=glgB {ECO:0000255|HAMAP-Rule:MF_00685}; OrderedLocusNames=PBPRB1328;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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:0000255|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:0000255|HAMAP-Rule:MF_00685};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00685}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00685}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00685}.
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DR EMBL; CR378679; CAG23199.1; -; Genomic_DNA.
DR RefSeq; WP_011221380.1; NC_006371.1.
DR AlphaFoldDB; Q6LHN1; -.
DR SMR; Q6LHN1; -.
DR STRING; 298386.PBPRB1328; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; CAG23199; CAG23199; PBPRB1328.
DR KEGG; ppr:PBPRB1328; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_3_2_6; -.
DR OMA; FGMKWMM; -.
DR OrthoDB; 227746at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000000593; Chromosome 2.
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; cd02855; E_set_GBE_prok_N; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.1180; -; 1.
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 PANTHER; PTHR43651; PTHR43651; 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; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 2.
DR TIGRFAMs; TIGR01515; branching_enzym; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..716
FT /note="1,4-alpha-glucan branching enzyme GlgB"
FT /id="PRO_0000188725"
FT ACT_SITE 394
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT ACT_SITE 447
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ SEQUENCE 716 AA; 81846 MW; 77784870059256C2 CRC64;
MQLERAAFSD PFSFLGPQYQ SKGIALRVWM PGAVSMVVEI ENGEKFPLTR EDESGFVLIS
KMDLTAAVYK LHISWPTGEQ TIHDPYQFHG FMPSGDALVS PSKMHSEMGA QLISLNKGGQ
PISGVRFLTY APNASAVSVI GEFNAWDGRR HPMQRLDDGL WGLFIPDLED GTQYKFELKD
SSGNSLPHKA DPWGYSSEQY PSFTSIVYDQ SRYQWQDKAW QTRPVSVKHQ EALSFYELHA
GSWRRNEQGD FLTYRELAEQ LIPYLSEMGY THLELMPVSE HPFYGSWGYQ PIGLFSPTSR
FGTPDDFKYF VDQCHLAGIG VVLDWVPAHF PSDDHGLANF DGTALFNDPD PRRGWHQDWK
SYIYDYGRDH VRRFLISNAL FWLEHYHIDG LRVDAVASML YLDYSREHDQ WIPNHDGGNQ
NYDAISLLRW MNEEVYSHYP NAMTIAEEST AFSGVSRPTD MGGLGFGFKW NMGWMHDSLS
YIQEEPVHRK FHHNTITFPL IYAFSENYVL SLSHDEVVYG KGSLLDKMPG DEWQKSANLR
TYMGYMYGQP GKKLNFMGAE IAQSAEWSHD GQLEWHWLEY PRHNGMKKLV SDLNHLYQDL
PALHELDCSP EGFEWRVQDD AETSVLAHER FALNGDKVLV VSNFTPVPRE GYTLGVPAEG
EYEVLLNTDA EKYWGSGTPI QQTVKTQLLE KHGLAQSISL DLPPLSTVFL AFKQHA
