(data stored in SCRATCH zone)

SWISSPROT: GLGB_CHLAB

ID   GLGB_CHLAB              Reviewed;         721 AA.
AC   Q5L6K4;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   11-DEC-2019, entry version 94.
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=CAB262;
OS   Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=218497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27085 / S26/3;
RX   PubMed=15837807; DOI=10.1101/gr.3684805;
RA   Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA   Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA   Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA   Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT   "The Chlamydophila abortus genome sequence reveals an array of variable
RT   proteins that contribute to interspecies variation.";
RL   Genome Res. 15:629-640(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}.
DR   EMBL; CR848038; CAH63718.1; -; Genomic_DNA.
DR   RefSeq; WP_011096942.1; NC_004552.2.
DR   SMR; Q5L6K4; -.
DR   STRING; 218497.CAB262; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; CAH63718; CAH63718; CAB262.
DR   KEGG; cab:CAB262; -.
DR   eggNOG; ENOG4105C9C; Bacteria.
DR   eggNOG; COG0296; LUCA.
DR   HOGENOM; HOG000283037; -.
DR   KO; K00700; -.
DR   OMA; YEMHLGS; -.
DR   OrthoDB; 227746at2; -.
DR   BioCyc; CABO218497:G1GI1-286-MONOMER; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001012; 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   Gene3D; 2.60.40.10; -; 1.
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; 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;
DR   PRODOM; Q5L6K4.
DR   SWISS-2DPAGE; Q5L6K4.
KW   Carbohydrate metabolism; Glycogen biosynthesis; Glycogen metabolism;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..721
FT                   /note="1,4-alpha-glucan branching enzyme GlgB"
FT                   /id="PRO_0000260643"
FT   ACT_SITE        400
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
FT   ACT_SITE        453
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00685"
SQ   SEQUENCE   721 AA;  83023 MW;  5E4CBEFF46AF64A6 CRC64;
     MVERIVNSED VSLLVSGRQS NPHKFLGIVS ENSSQDRIIL FRPGAHSVVV ELQGNIAHAQ
     HHHSGIFSLT APKGTLPQDY RIYHQNGLLA HDPYAFPPLW GEVDSFLFHQ GTHYKIYECM
     GAIPYNVQGI SGVLFVVWAP HAQRVSVVGD FNFWNGLVNP LRKVSDLGVW ELFIPGLEEG
     TLYKWEIVSA SGEVLIKTDP YGKRFDVPPH APSRVVDSDR YTWHDAAWME KRKHRGDQPL
     AIYEVHVGSW QWHEGKPLGY RELAKKLAAY CKEMHYTHVE LLPVTEHPLN ESWGYQVTGY
     YAPTCRYGTP EDFQFFVDHL HRENIGVILD WVPGHFPTDG FALAHFDGEA LYESIENHEP
     LHPHWRTYTF DYRCNEVVNF LLGSALFWLD KMHIDGLRVD AVTSMLYLDY GRQEGEWSPN
     IYGGRENLQA IEFIKHLNSV VHREFPGVLT FAEESTDFPK VTQAVAQGGL GFDYKWNLGW
     MHDTFRYIQV DPLFRSYHHK DLTFSLWYAF NERYLLPLSH DEVVHGKGSL LQKMPGDTWT
     KFAHMRLLLS YHICQPGKKL LFMGGEFAQG KEWTPDSPLD WHLLDHPDHA YLHKCVARMN
     ALYCDLPYFW KGDGKQGSFR WVDFKDTENH VIAYYRFSGE DRSSALLCVH HFSSGYFPSY
     VLYCQDIHSC QLLFNSDDCC FGGSGKGNRQ PVLCLDQHVS WGIDIELPPL ATLIFHVDFV
     N
//

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