ID A0A0Q9S9K8_9BACL Unreviewed; 944 AA.
AC A0A0Q9S9K8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Glycosyl transferase family 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASG93_09850 {ECO:0000313|EMBL:KRF21644.1};
OS Paenibacillus sp. Soil787.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF21644.1, ECO:0000313|Proteomes:UP000051948};
RN [1] {ECO:0000313|EMBL:KRF21644.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF21644.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF21644.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF21644.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family.
CC {ECO:0000256|ARBA:ARBA00006821, ECO:0000256|RuleBase:RU361196}.
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:KRF21644.1}.
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DR EMBL; LMSP01000023; KRF21644.1; -; Genomic_DNA.
DR RefSeq; WP_056835067.1; NZ_LMSP01000023.1.
DR AlphaFoldDB; A0A0Q9S9K8; -.
DR STRING; 1736411.ASG93_09850; -.
DR OrthoDB; 9803279at2; -.
DR Proteomes; UP000051948; Unassembled WGS sequence.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:InterPro.
DR GO; GO:0030979; P:alpha-glucan biosynthetic process; IEA:InterPro.
DR CDD; cd10792; GH57N_AmyC_like; 1.
DR CDD; cd03801; GT4_PimA-like; 1.
DR Gene3D; 1.20.1430.10; Families 57/38 glycoside transferase, middle domain; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR InterPro; IPR037090; 57_glycoside_trans_central.
DR InterPro; IPR015293; BE_C.
DR InterPro; IPR040042; Branching_enz_MT3115-like.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR004300; Glyco_hydro_57_N.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR PANTHER; PTHR41695; 1,4-ALPHA-GLUCAN BRANCHING ENZYME RV3031-RELATED; 1.
DR PANTHER; PTHR41695:SF1; 1,4-ALPHA-GLUCAN BRANCHING ENZYME RV3031-RELATED; 1.
DR Pfam; PF09210; BE_C; 1.
DR Pfam; PF03065; Glyco_hydro_57; 1.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361196}.
FT DOMAIN 16..384
FT /note="Glycoside hydrolase family 57 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03065"
FT DOMAIN 414..521
FT /note="1,4-alpha-glucan branching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09210"
FT DOMAIN 564..738
FT /note="Glycosyltransferase subfamily 4-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13439"
FT DOMAIN 753..909
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT ACT_SITE 197
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT ACT_SITE 340
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
SQ SEQUENCE 944 AA; 108953 MW; 56C7D3C9F563D128 CRC64;
MINRIKPKPE LKGYFVLVLH AHLPYIRHQK HNDNLEEQWF YQAMTETYLP LIEVMNRLTS
DKIDFRLTFS ITPTILSLFS NPYLQDNYHA YLSKLIGLAD KERVRLQKNP SFLPLAAHYA
ERFRELQKLY ESCKGNVIAT FKHYQDLGRI EIVTSAATHG FLPLMKTEEA IKAQIMTAVR
DYERYFDQKP RGIWLPECGY TPGIDRILKQ AGIQYFFTDS SAIAFASPQP ARELAAPLMT
PYGVTAFPRD PESTNQVWSA ENGYPGDFNY REYYSDIGQD TGFKYYRNTS KGSHKEPYQP
ELALEKAAEH ADHFLANRQK QAAHWERWLD RKPLIVSPYD AELFGHWWYE GPHFLERLCR
NMFLDQQTIK MITPSEYLEE YPAAAVGHLN ESSWGRNHSA EIWLQGHNDW IYRHLHQAEE
RMIELATKHE HLSRHGKLSA SVLKRALNQA AREFMLAQSS DWAFMMDAQS DVDHAIRRTK
DHLGCFHHLC DQVDREQVDE VLLTDLEEKD NCLPDIQFQD YVSIQQLSPI PTIPNLKEWK
ALLEETKHRP NVFMLTWEYP PKHVGGLSRA VHELSEALVA NEEIVHVITT SYEGAPSFEK
MNGVYVHRLP IHHSGDTHFY HWTFEMNLAM IDHLVRWKEN GGRIDLLHAH DWMVAHTARE
IKTSYGIPLV ATIHATEWGR NQGNLTSDLQ RKIHHLEWQL TYEANRVFVC SSYMKEEVGR
IFNLPSDKVS VHPNGIRTPK PNIKTMNRPD FVAKQDKVIF FIGRLVYEKG IQILLAALPK
IISQVPQAKL IIAGSGPMES ELRSQAAFLG DRVLFTGFVN DAYRTQLYQS TDVCVIPSLY
EPFGIVALEA MANRKPLVLS DTGGLAEIIR HGVDGYKALP GHVDSLAWHI TDMLLQPKQA
AKMADSAYQL LQQHYEWSHI AQNIQNEYQM LTHYQPAIQV HATI
//
