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Database: UniProt
Entry: A0A101F6C1_9FIRM
LinkDB: A0A101F6C1_9FIRM
Original site: A0A101F6C1_9FIRM 
ID   A0A101F6C1_9FIRM        Unreviewed;       621 AA.
AC   A0A101F6C1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=starch synthase {ECO:0000256|ARBA:ARBA00012588};
DE            EC=2.4.1.21 {ECO:0000256|ARBA:ARBA00012588};
DE   Flags: Fragment;
GN   ORFNames=XD63_1455 {ECO:0000313|EMBL:KUK31277.1};
OS   Thermoanaerobacterales bacterium 50_218.
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales.
OX   NCBI_TaxID=1635288 {ECO:0000313|EMBL:KUK31277.1, ECO:0000313|Proteomes:UP000053634};
RN   [1] {ECO:0000313|Proteomes:UP000053634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-
CC         alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA-
CC         COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001478};
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:KUK31277.1}.
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DR   EMBL; LGFL01000052; KUK31277.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101F6C1; -.
DR   Proteomes; UP000053634; 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   Gene3D; 1.20.1430.10; Families 57/38 glycoside transferase, middle domain; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 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   InterPro; IPR013534; Starch_synth_cat_dom.
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; PF08323; Glyco_transf_5; 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};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          7..394
FT                   /note="Glycoside hydrolase family 57 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03065"
FT   DOMAIN          427..527
FT                   /note="1,4-alpha-glucan branching enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09210"
FT   DOMAIN          548..606
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   ACT_SITE        188
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         240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         407
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   BINDING         467
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR640042-2"
FT   NON_TER         621
FT                   /evidence="ECO:0000313|EMBL:KUK31277.1"
SQ   SEQUENCE   621 AA;  71474 MW;  300C5AE65365B2F1 CRC64;
     MSSGYLALVL HAHLPYVRHP ECQTAVAERW LWEALTESYI PLLQTFFRLA DEKIPFRITL
     SLSPPLISML GDPLLQDRYW KHLHLSLELG AKEIARNKGN PQLKNLAEFY LERLEGIKKF
     YEEWGHDLIS AFRRLHRTGH IEVITTAATH GYLPLMVTEE ARKAQIAISV ESFEKWFGFS
     PKGFWLPECG YKPGIEKILG EFGIKYFIVE THGILHASPP PKDGVYAPLL TSSGVAAFGR
     DPDSSRQVWS SREGYPGDFC YREFYRDIGY ELDYDYLAPY LPGDGVRVDT GFKYYRITGP
     GEEKQYYDPH LAMEKVRVHA GHFLFAREKQ IEHLSSHLSP KKPIIVAPYD AELFGHWWFE
     GPLWLGELIR RIPLQQTFSL TTPSDYLEEA RNKGWQLQQA ELPESSWGLG GYHEVWLGPA
     NDWIYRHLHL AEKRMVELAK SYPDSYGLQR RALNQAAREL LLAQSSDWAF IMHAGTVVEY
     ARQRVNDHLG RFTLLYHQIR NNDLDQEMLE FIEWLDPIFP CLDYRVYADK IKKSAKNEVL
     VPRSSKGRVL VLTWEFPPRS IGGLSRHVAG LTQALAEAGE AVDVIAPWVP GAPTFSQNGL
     LRVHRVRVDA EDIHDFLDWV F
//
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