ID E4RVU8_LEAB4 Unreviewed; 269 AA.
AC E4RVU8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=starch synthase {ECO:0000256|ARBA:ARBA00012588};
DE EC=2.4.1.21 {ECO:0000256|ARBA:ARBA00012588};
GN OrderedLocusNames=Lbys_3197 {ECO:0000313|EMBL:ADQ18858.1};
OS Leadbetterella byssophila (strain DSM 17132 / JCM 16389 / KACC 11308 / NBRC
OS 106382 / 4M15).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Leadbetterella.
OX NCBI_TaxID=649349 {ECO:0000313|EMBL:ADQ18858.1, ECO:0000313|Proteomes:UP000007435};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17132;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Teshima H., Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Leadbetterella byssophila DSM 17132.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ18858.1, ECO:0000313|Proteomes:UP000007435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17132 / JCM 16389 / KACC 11308 / NBRC 106382 / 4M15
RC {ECO:0000313|Proteomes:UP000007435};
RX PubMed=21475582; DOI=10.4056/sigs.1413518;
RA Abt B., Teshima H., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K.,
RA Pati A., Tapia R., Han C., Goodwin L., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Tindall B.J.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Leadbetterella byssophila type strain
RT (4M15).";
RL Stand. Genomic Sci. 4:2-12(2011).
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; CP002305; ADQ18858.1; -; Genomic_DNA.
DR RefSeq; WP_013409885.1; NC_014655.1.
DR AlphaFoldDB; E4RVU8; -.
DR STRING; 649349.Lbys_3197; -.
DR CAZy; GT5; Glycosyltransferase Family 5.
DR KEGG; lby:Lbys_3197; -.
DR eggNOG; COG0297; Bacteria.
DR HOGENOM; CLU_085315_0_0_10; -.
DR OrthoDB; 9808590at2; -.
DR Proteomes; UP000007435; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000007435};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..230
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
SQ SEQUENCE 269 AA; 31039 MW; A94B92D07295A7D4 CRC64;
MSKLRILYIS SEIDPFLETS KIASLLRKLP QEMQERGMEI RILIPRFGLI NERKHRLHEV
VRLSGINISI GEEEKPLIIK VASIPAAKLQ VYFLDNEDYF QRKTVFTDKA GTFYDDNDER
AIFFCKGALE TVKKLGWAPD VVHCTDWMTA LVPLYLKTTY KNDPIFKNTK TIFTVYNNSF
DHTFSDDMFP KVKMMDISDE NLANLRSRDF YGFIKIGCQY SDVVVKANPA LNEALSLALD
ETAQKQIHSY VDDENAADIF YNLYTELAD
//