ID A0A444YPD7_ARAHY Unreviewed; 890 AA.
AC A0A444YPD7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN ORFNames=Ahy_B06g083189 {ECO:0000313|EMBL:RYR03820.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR03820.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR03820.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR03820.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004727}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Plastid, amyloplast
CC {ECO:0000256|ARBA:ARBA00004602}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RYR03820.1}.
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DR EMBL; SDMP01000016; RYR03820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444YPD7; -.
DR STRING; 3818.A0A444YPD7; -.
DR OrthoDB; 96at2759; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000289738; Chromosome b06.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
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 GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd11321; AmyAc_bac_euk_BE; 1.
DR CDD; cd02854; E_set_GBE_euk_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; 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: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 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 Amyloplast {ECO:0000256|ARBA:ARBA00023234};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Plastid {ECO:0000256|ARBA:ARBA00023234};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 352..712
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 54..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 495
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 550
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 890 AA; 101555 MW; E7BFD227A95AC7C6 CRC64;
MVYTVSGIRF PSVPSLQKSS QLSFHDRRSA SFSFLLNRNS FSRKSLAVKC SHDSDLSSST
VAESDKVLIP QGHDNSSTTT DEVEAPDITS EDPQKIQELT MKGEKIDYEA VSTDKDDKDG
QGHVLSSHVD VDTNTQAENT SVSINKKVKV ESEEARPKII APPGTGHKIY EIDPSLQAHR
AHLDFRYGQY KRLHEEINKY EGGLDAFSRG YEKFGFTRSA TGITYREWAP GATSAALIGD
FNNWNPNADV MTRNEFGVWE IFLPNNVDGS LPIPHGSRVK IRMETPSGIK DSIPAWIKFS
VQAPGEIPYN GIYYDPPEEE KYVFKYPQPK RPKSLRIYES HVGMSSSEPK INTYVNFRDE
VLPRIKRLGY NAVQIMAIQE HSYYASFGYH VTNFFAPSSR FGTPDDLKSL IDKAHELGLL
VLMDIVHSHA SNNTLDGLNM FDGTDTHYFH GGSRGYHWMW DSRLFNYGSW EVLRYLLSNA
RWWLEEYKFD GFRFDGVTSM MYTHHGLGVG FTGNYNEYFG FATDVDAVVY LMLVNDVIHG
LFPEAITIGE DVSGMPTFCL PTQDGGVGFD YRLHMAIADK WIEILKKKDE DWEMGDIVHS
LTNRRWLEKC VAYAESHDQA LVGDKTIAFW LMDKDMYDFM ALDRPSTPLI DRGIALHKMI
RLITMGLGGE GYLNFMGNEF GHPEWIDFPR GDQHLPTGAV IPGNNYSYDK CRRRFDLGDA
DYLRYRGMQE FDQAMQHLEE RFGFMTSEHQ YISRKHEGDK VIVFERGKLV FVFNFHWYNS
YSDYRVGCLN PGKYKIVLDS DDPLFGGFNR LNPTAEYFTS DGWYDDRPRS FLVYAPSRTA
VVYALADEAE PEPKLKPVEV LVMEPELEPE PKQVLESESK PEPVEAEVEP
//
