ID A0A2T5BYI2_9BACT Unreviewed; 670 AA.
AC A0A2T5BYI2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=C8N47_11915 {ECO:0000313|EMBL:PTN07302.1};
OS Mangrovibacterium marinum.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Mangrovibacterium.
OX NCBI_TaxID=1639118 {ECO:0000313|EMBL:PTN07302.1, ECO:0000313|Proteomes:UP000243525};
RN [1] {ECO:0000313|EMBL:PTN07302.1, ECO:0000313|Proteomes:UP000243525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28823 {ECO:0000313|EMBL:PTN07302.1,
RC ECO:0000313|Proteomes:UP000243525};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) 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 -!- 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:PTN07302.1}.
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DR EMBL; QAAD01000019; PTN07302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5BYI2; -.
DR OrthoDB; 9800174at2; -.
DR Proteomes; UP000243525; Unassembled WGS sequence.
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; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000243525};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 150..552
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 326
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 380
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 670 AA; 77624 MW; 45FD40D6D0205AE1 CRC64;
METLKLIEND PWLKVHSQVI LSRYQEAIQK ENELTQGQSL REFANGYNYY GLHRTDDQWI
FRDWAPNATA IYLIGECNHW AKEEAYRFQS VGNGNWELVL GHDQLKHGDL YAFHIEWDGG
QGTRIPAWVN RAVQDDTTKL FSAQVWGPEQ TYQWKNPDFS RGDDAPLVYE SHVGMAGEEE
RVHSYNEFRE QVLPRIKAAG YNTVQLMAVP EHPYYGSFGY HVSSFFAPSS RFGTPDELKA
LIDEAHGMGL AVIMDLVHSH AVKNENEGLG RYDGTRYQFF HDGGKGEHPA WDSYCFNYGK
NEVLHFLLSN IRWWLEEFKF DGFRFDGVTS MLYFDHGLGK AFTGYDDYYN ANVDVEATTY
FYLANKLIHE INPKALSIAE EMSGMPGLAS PLADGGLGFD YRMAMGVPDF WIKLIKEVAD
ENWDVGQIFY ELTSKRMDEK VVSYAESHDQ ALVGDKTIIF RLIDKEMYFS MRKDQPNMTV
DRGIALHKMI RLITAATAGG SYLNFMGNEF GHPEWIDFPR EGNNWSFKHA RRLWSIAEDK
ELRFHWLADF DREMIHWIQD HHVLNIPEVY HRFDNKGDQI LAFQRGDYLL VFNFNPVQSF
TGYGIPLEAS KWKILFDTDE DRFGGQGRID HSMTYYTKPS GGLTSQHYLN LYLPARTAMV
LKKQAFKRVR
//
