ID   Q2LRL5_SYNAS            Unreviewed;       511 AA.
AC   Q2LRL5;
DT   21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   21-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=starch synthase {ECO:0000256|ARBA:ARBA00012588};
DE            EC=2.4.1.21 {ECO:0000256|ARBA:ARBA00012588};
GN   ORFNames=SYN_00877 {ECO:0000313|EMBL:ABC76724.1};
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC76724.1, ECO:0000313|Proteomes:UP000001933};
RN   [1] {ECO:0000313|EMBL:ABC76724.1, ECO:0000313|Proteomes:UP000001933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB {ECO:0000313|EMBL:ABC76724.1,
RC   ECO:0000313|Proteomes:UP000001933};
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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};
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DR   EMBL; CP000252; ABC76724.1; -; Genomic_DNA.
DR   RefSeq; WP_011416757.1; NC_007759.1.
DR   AlphaFoldDB; Q2LRL5; -.
DR   STRING; 56780.SYN_00877; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   KEGG; sat:SYN_00877; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_18_5_7; -.
DR   InParanoid; Q2LRL5; -.
DR   OrthoDB; 9808590at2; -.
DR   Proteomes; UP000001933; Chromosome.
DR   GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009011; F:starch synthase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR013534; Starch_synth_cat_dom.
DR   PANTHER; PTHR45825; GRANULE-BOUND STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR   PANTHER; PTHR45825:SF11; STARCH SYNTHASE 1, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR   Pfam; PF08323; Glyco_transf_5; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:ABC76724.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001933};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABC76724.1}.
FT   DOMAIN          39..234
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
SQ   SEQUENCE   511 AA;  57099 MW;  807C3CD13DCEBEEF CRC64;
     MVAIKSSKTT PRTAVLLITP ETGRLPEGMC DLARFISGKS GGLGEVVTAL CEGLTARGIN
     CHLATLNLKK RFQQEGNMDE SEWRKIRYQI DPERIHLVSS SIFADLPSAY AGDVTLNAAE
     FQKQLINHVI KTVSAQNCGK LILHTHDWMA GGPVTAYAKS RKIPVLHTVH NVFTRNVPVP
     MYLGVDLEQL DHDLYYSEEK GERCIDCQAT AIKSATLVNL VGHRFLEEIV DDYFMDRAII
     PDSVRQEIKA KKAFESALTV LNCPSLNMYP ESCSFLHRNF GADDDVLQAK KDNLVEFQRR
     TGLNVDPEAI LLYWPSRLDP CQKGVELIEE IALKFVIEHG DVQIAVIGDG VGGDRTHEEI
     MGRIACASQG KICYHRFNEE LSMLGFASAS DVFGASLYEP CGQIDQLGNL FGATATNRDT
     GGYHDKIREL KLKIDGAPED SGNGFLFHDY DVGGLWYGLH KCVEFHRRPA EVRASQIKRI
     MKETRATYKL DRMIDEYIKI YERLNGGMPL A
//