ID R0G308_9BRAS Unreviewed; 899 AA.
AC R0G308;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=CARUB_v10012936mg {ECO:0000313|EMBL:EOA29842.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA29842.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
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}.
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DR EMBL; KB870807; EOA29842.1; -; Genomic_DNA.
DR RefSeq; XP_006296944.1; XM_006296882.1.
DR AlphaFoldDB; R0G308; -.
DR STRING; 81985.R0G308; -.
DR GeneID; 17891099; -.
DR KEGG; crb:17891099; -.
DR eggNOG; KOG0470; Eukaryota.
DR OrthoDB; 349883at2759; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
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:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
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; 2.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
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:SF4; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME 3, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 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 Plastid {ECO:0000256|ARBA:ARBA00023234};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 420..763
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 47..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 103235 MW; 68EEA36F456F16EA CRC64;
MVSLSNQSRF CFHPNNLFVS DTRRLGISGV NFPRKIKVNI TCFAAERPRQ QKQKKKSQGQ
GTSDAEAGVD PVGFLSKLGI ADRIFAQFLR ERHKALKDLK DEILKRHFDF RDLASGFELL
GMHRHMEHRV DFMDWGPGAR YGAIIGDFNG WSPTENAARE GLFGHDDFGY WFIILEDKLR
EGEEPDELYF QQYNYVDDYD KGDSGVSAEE IFQKANDEYW EPGEDRFIKN RFEVPAKLYE
QLFGPNSPQT LEELGDIPDA ETRYKQYKEE HKNDPPSNLP SCDIIDNGQG KPYDIFNVVT
SPEWTKKFYE KKPPIPYWLE TRKGRKAWVK KYVPAVPHGS RYRLYFNTPD GPLERVPAWA
TYVQPEDEGK QAYAIHWEPS PESAYKWKNS KPEVPKSLRI YECHVGISGS EPKISSFEEF
TKKVLPHVKR AGYNAIQLIG IPEHKDYFTV GYRVTNFFAV SSRYGTPDDF KRLIDEAHGL
GILVFLDIVH SYAAADQMVG LSLFDGSNDC YFHYGKRGHH KHWGTRMFKY GDLDVLHFLI
SNLNWWITEY QVDGYQFHSL ASMIYTHNGF ASFDNELDDY CNQYVDRDAL MYLILANEIL
HVLHPNIITI AEDATYYPGL CEPVSQGGLG FDYYVNLSAS EMWVSLLDNV PDNEWSMSKI
VSTLVANKEY ADKMLSYAES HNQSISGGRS FAEILFGGVN NGSPGGLQLL DRGVSLHKMI
RLITFTIGGR AYLNFMGNEF GHPERVEFPT QSNNFSFSLA NRRWDLLESG VHRHLFSFDK
DLMDLDKSKG ILSRGLPSIH HVNDANMVIS FSRGPFLFIF NFHPSNAYEK YDVGIEEAGE
YTMILNSDEV KYGGQGLLTE DQYLQRSLSK RIDGQRNCLE VFLPSRTAQV YKLTRILRI
//
