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Database: UniProt
Entry: Q2RH74_MOOTA
LinkDB: Q2RH74_MOOTA
Original site: Q2RH74_MOOTA 
ID   Q2RH74_MOOTA            Unreviewed;       528 AA.
AC   Q2RH74;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=(1->4)-alpha-D-glucan branching enzyme {ECO:0000313|EMBL:ABC20215.1};
GN   OrderedLocusNames=Moth_1915 {ECO:0000313|EMBL:ABC20215.1};
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX   NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC20215.1};
RN   [1] {ECO:0000313|EMBL:ABC20215.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC20215.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT   "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family.
CC       {ECO:0000256|ARBA:ARBA00006821, ECO:0000256|RuleBase:RU361196}.
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DR   EMBL; CP000232; ABC20215.1; -; Genomic_DNA.
DR   RefSeq; YP_430758.1; NC_007644.1.
DR   AlphaFoldDB; Q2RH74; -.
DR   STRING; 264732.Moth_1915; -.
DR   CAZy; GH57; Glycoside Hydrolase Family 57.
DR   EnsemblBacteria; ABC20215; ABC20215; Moth_1915.
DR   KEGG; mta:Moth_1915; -.
DR   PATRIC; fig|264732.11.peg.2073; -.
DR   eggNOG; COG1543; Bacteria.
DR   HOGENOM; CLU_008192_1_0_9; -.
DR   OrthoDB; 9803279at2; -.
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   Gene3D; 1.20.1430.10; Families 57/38 glycoside transferase, middle domain; 1.
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   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   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361196}.
FT   DOMAIN          7..394
FT                   /note="Glycoside hydrolase family 57 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03065"
FT   DOMAIN          425..525
FT                   /note="1,4-alpha-glucan branching enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09210"
FT   ACT_SITE        189
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT   ACT_SITE        350
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-1"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         405
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         465
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
SQ   SEQUENCE   528 AA;  61342 MW;  42262899F41EC50F CRC64;
     MPRGYVALVL HAHLPYVRDT EDDFSLAEKW YHEAVTETYI PLINICQRLN RDRVPYRITI
     SLSPPLVTMM ADPLVQEHYR RYLERLRELA AREVWRTRND PRFHLVARMY QDLFENTART
     YQTYGGNLIN AFRELQDSGK VELITCAATH GYLPLIGLQR EVVRAQVEVA VNNHRRLFGR
     PPAGLWLPEC AYNPGDDAIL RDYGLKYFFV DAHGLLYATP RPRYSIFAPV YTPAGVAAFG
     RDLESSEQVW SAQEGYPGDF DYREFYRDIG YDLDFEYIKP YIHPSGLRLD TGLKYYRITG
     KSGYKEPYVP EWASFKAHTH AGNFLFNREQ QINYLATYMD RPPLIICPYD AELFGHWWFE
     GPQWLESLFR QVAGLAPQPF SFITPSEYLE RFPVNQPATP CMSSWGNNGY NEVWLEDSNH
     WIYRHLHHAA AEMIRLANQH PTAGGILLRA LNQAARELLV AQSSDWAFIM KTGTMVEYAV
     SRTKKHLLNF WELTRGINKN DLDPAKVQAL EEANNIFPDI NYRIFASR
//
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