ID C6LEN4_9FIRM Unreviewed; 835 AA.
AC C6LEN4;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=1,4-alpha-glucan branching enzyme GlgB {ECO:0000256|HAMAP-Rule:MF_00685};
DE EC=2.4.1.18 {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=Alpha-(1->4)-glucan branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE AltName: Full=Glycogen branching enzyme {ECO:0000256|HAMAP-Rule:MF_00685};
DE Short=BE {ECO:0000256|HAMAP-Rule:MF_00685};
GN Name=glgB {ECO:0000256|HAMAP-Rule:MF_00685,
GN ECO:0000313|EMBL:EET61017.1};
GN ORFNames=BRYFOR_07084 {ECO:0000313|EMBL:EET61017.1};
OS Marvinbryantia formatexigens DSM 14469.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Marvinbryantia.
OX NCBI_TaxID=478749 {ECO:0000313|EMBL:EET61017.1, ECO:0000313|Proteomes:UP000005561};
RN [1] {ECO:0000313|EMBL:EET61017.1, ECO:0000313|Proteomes:UP000005561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14469 {ECO:0000313|EMBL:EET61017.1,
RC ECO:0000313|Proteomes:UP000005561};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages
CC in glycogen by scission of a 1,4-alpha-linked oligosaccharide from
CC growing alpha-1,4-glucan chains and the subsequent attachment of the
CC oligosaccharide to the alpha-1,6 position.
CC {ECO:0000256|ARBA:ARBA00002953, ECO:0000256|HAMAP-Rule:MF_00685}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00685};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|HAMAP-Rule:MF_00685}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00685}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000, ECO:0000256|HAMAP-
CC Rule:MF_00685}.
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:EET61017.1}.
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DR EMBL; ACCL02000008; EET61017.1; -; Genomic_DNA.
DR RefSeq; WP_006861877.1; NZ_CP102268.1.
DR AlphaFoldDB; C6LEN4; -.
DR STRING; 168384.SAMN05660368_00309; -.
DR eggNOG; COG0296; Bacteria.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000005561; Unassembled WGS sequence.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR CDD; cd11322; AmyAc_Glg_BE; 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; 2.
DR HAMAP; MF_00685; GlgB; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR037439; Branching_enzy.
DR InterPro; IPR006407; GlgB.
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 NCBIfam; TIGR01515; branching_enzym; 1.
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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600, ECO:0000256|HAMAP-
KW Rule:MF_00685};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_00685}; Reference proteome {ECO:0000313|Proteomes:UP000005561};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00685}.
FT DOMAIN 255..616
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 692..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 412
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT ECO:0000256|PIRSR:PIRSR000463-1"
FT ACT_SITE 465
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00685,
FT ECO:0000256|PIRSR:PIRSR000463-1"
SQ SEQUENCE 835 AA; 95105 MW; DD1BCC6CF3E93212 CRC64;
MGEDKLYDLM DWAQIEALIY SEEDNPHAIL GPHLTDDGVL IQAFIPTADR IMVQITGKKE
SYEMTMEDEA GFFAVLIPGD KIPKYTLYVI FDNGTSLEYI DPYAFEPVLT KQETAKFNAG
ICYDIYEKMG AHPMTVQGIK GIHFAVWAPN AVRVSLVGDF NLWDGRRLPM RRLWDSGIFE
IFVPGISVGE MYKYEIKAQG NITYLKADPY ANAAQLRPDT ASIVADLTQF QWTDDAWMKQ
RKKTDSKKKP MAIYEMHLAS WKKPEDRDFY NYRELAPMIA EYVKEMGYTH IELLPVMEHP
FDGSWGYQVT GYYAPTARYG TPEDFMYFMN YMHEAGIGVI LDWVPAHFPR DTFGLAAFDG
TCLYEHLDPR QGSHPHWGTL IYNYGRPEVK NFLIANALFW ADKYHADGIR MDAVASMLYL
DYGKNDGEWV ANIYGGNENL EAVEFLKHLN SVFKKRKDGA ILIAEESTAW PKITGALDDG
GLGFDYKWNM GWMNDFIGYM SLDPIYRASN HGGLTFSMIY AYSEDFILTL SHDEVVHGKC
SLINKMPGET EQKFANLRAA YGYMMAHPGK KLLFMGQEFA QYKEWNETKG LDWEDLEQEP
NRQMRDYYKA LLEFYRTHPA LYELDYEPEG FTWINAINAN ENLLVFTRNT AKKDETLLIV
CNFSPLVYEN HKVGVPWPGK YKEIFNSDRT EFGGKGNLNP RVKQSKKEEA DGQENSITVK
IPPMGISIFS YAKADPKAAS NKAAREKKSA GEKKTKAVPK KVSLKEELMQ KMEAAKEPEA
AKPQKETVKQ PKAAAKQQKE SAGQPKAAAK QQKESAGQPK ETAKQQKPGQ QKKKG
//
