ID D5BGV9_ZUNPS Unreviewed; 601 AA.
AC D5BGV9;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 77.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN OrderedLocusNames=ZPR_2971 {ECO:0000313|EMBL:ADF53290.1};
OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS profunda).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zunongwangia.
OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF53290.1, ECO:0000313|Proteomes:UP000001654};
RN [1] {ECO:0000313|EMBL:ADF53290.1, ECO:0000313|Proteomes:UP000001654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC {ECO:0000313|Proteomes:UP000001654};
RX PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA Zhou B.C., Yu J., Zhang Y.Z.;
RT "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT to the deep-sea environment and ecological role in sedimentary organic
RT nitrogen degradation.";
RL BMC Genomics 11:247-247(2010).
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};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000}.
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DR EMBL; CP001650; ADF53290.1; -; Genomic_DNA.
DR RefSeq; WP_013072387.1; NC_014041.1.
DR AlphaFoldDB; D5BGV9; -.
DR STRING; 655815.ZPR_2971; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; zpr:ZPR_2971; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_004245_5_1_10; -.
DR OMA; TQIDHDY; -.
DR OrthoDB; 9761875at2; -.
DR Proteomes; UP000001654; 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: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:InterPro.
DR CDD; cd11325; AmyAc_GTHase; 1.
DR CDD; cd02855; E_set_GBE_prok_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; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
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; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF11; MALTO-OLIGOSYLTREHALOSE TREHALOHYDROLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 2.
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; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 129..487
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 289
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 333
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 601 AA; 68381 MW; 5A0284E2F1982D16 CRC64;
MMEENKLSYP IAPSDGMGAI PENDKTTFRV WAPNADKVSV TGDFNDWNPN DLPLEPEENG
YWAATTTKAK KGDQYKYHIE NGDISVYKND PYAFEVTNSD GNSIIRDLNF DWEEDNFQLP
PWNSLVIYEL HVGTFNRKNP DAVGTFQDVI EKLDYLKSLG INCIELLPVA EFAGGISWGY
NPAHPFAIEQ DYGGPEGLFQ LIKTAHQKGI GVIMDVVYNH LGPSDVDLWQ FDGWQENDKG
GIYFYNDHRS DTPWGDTRPD YGRPEVRQYF RDNALMWIEK YHCDGLRMDA TSYIRYEGGG
LGFDTEILEG IIMMRDINAE IRHKYPNTIT IAEDLKADNI ITAPTENGGI GYGTQWDMKF
VHPVREVLTA LNDDERDLQK IVDAIVYKYN DDVFNRVIYT ESHDEVANGK ARVPEEIQPG
DAESSFAKKR SILGLVLVMT SPGIPMIFQG QEFLEDGYFK DTEELNWDKL NRLEGIDQLS
ADLIKLRTGE TPGAEGLKGQ HTEIIHFNQE NKILAYKRTM DGAQPALIIL NFGNNDFEDY
GIGIEADKNW KIKFNSTWKG YDKDFSELPV EDIQKVHEES DQKEWTGKVN IPAYGALIYA
L
//