ID U2L943_PORGN Unreviewed; 668 AA.
AC U2L943;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=HMPREF1989_01513 {ECO:0000313|EMBL:ERJ85964.1};
OS Porphyromonas gingivalis F0566.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1321822 {ECO:0000313|EMBL:ERJ85964.1, ECO:0000313|Proteomes:UP000016609};
RN [1] {ECO:0000313|EMBL:ERJ85964.1, ECO:0000313|Proteomes:UP000016609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0566 {ECO:0000313|EMBL:ERJ85964.1,
RC ECO:0000313|Proteomes:UP000016609};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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 -!- SIMILARITY: Belongs to the peptidase C25 family.
CC {ECO:0000256|ARBA:ARBA00006067}.
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:ERJ85964.1}.
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DR EMBL; AWVD01000112; ERJ85964.1; -; Genomic_DNA.
DR RefSeq; WP_021678949.1; NZ_KI260107.1.
DR AlphaFoldDB; U2L943; -.
DR PATRIC; fig|1321822.3.peg.1302; -.
DR HOGENOM; CLU_011131_2_2_10; -.
DR Proteomes; UP000016609; 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:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 191..535
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 668 AA; 78072 MW; BE7526B4DF87F589 CRC64;
MRIIEQDPWL RPYESVIESR LKYARKRETD LTGGRSGGLS DFANGHLYYG LHQDGDSWVI
REFAPEATAV YLIGELSRWR RLPQFRFAPV DEAGSWELRL PCRLLPHGSR YRLFFEWPGG
EGERIPAWCN RVEQDPETYL FYAQVWVPDT PYEMKHPHPN RKDEPLLIYE CHIGMSSEEE
KVSTYEEFRR NILPRIYKDG YNAIQLMAIQ EHPYYASFGY HVSSFFAPSS RFGTPEDLKR
LIDEAHALGL YVIMDLVHSH AVKNEVEGLG LYDGAHTLFF HEGNRGLHPA WDSYCFDYGK
DNVLHFLLSN CKYWLTEFGF DGFRFDGVTS MLYYSHGLGD RFDNYDSYYN GHQDGDAIAY
LILVNKLIHE LCPDAITIAE EVSGMPGLAL PLADGGYGFD YRLAMNIPDF WIKLIKEHRD
EDWNPGDIWY QLTNRRQEEK TISYAESHDQ ALVGDKTIIF RLIDADMYWY MNKQSCVHSV
DRGIALLKMI RLFTATTMNG GYLNFMGNEF GHPEWIDFPR EGNGWSYKYA RRQWSLADSP
FLRYAGLHLF DQDMIAMIRS VESFHKLPLR EYWLKREEQV ICYGRGDFFF VFNFHPERSY
SDYPIPLPAG KYSVVMSTDA RKYEGFGRVD EWVEHFTLPD GSKDRFTHEQ HLNLYLPARS
ALVLKLAE
//
