ID F5YLY9_TREPZ Unreviewed; 611 AA.
AC F5YLY9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Putative sucrose phosphorylase (Sucroseglucosyltransferase) {ECO:0000313|EMBL:AEF86931.1};
GN OrderedLocusNames=TREPR_1803 {ECO:0000313|EMBL:AEF86931.1};
OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF86931.1, ECO:0000313|Proteomes:UP000009223};
RN [1] {ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA Paulsen I.T.;
RT "Complete sequence of Treponema primitia strain ZAS-2.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF86931.1, ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RX PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT spirochete species in co-culture.";
RL ISME J. 5:1133-1142(2011).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001843; AEF86931.1; -; Genomic_DNA.
DR RefSeq; WP_015708330.1; NC_015578.1.
DR AlphaFoldDB; F5YLY9; -.
DR STRING; 545694.TREPR_1803; -.
DR KEGG; tpi:TREPR_1803; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_021358_0_0_12; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000009223; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11356; AmyAc_Sucrose_phosphorylase-like_1; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR033746; GGa_phosphorylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF214; GLUCOSYLGLYCERATE PHOSPHORYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009223};
KW Transferase {ECO:0000313|EMBL:AEF86931.1}.
FT DOMAIN 85..438
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 611 AA; 67112 MW; 8F8B545C662E80DD CRC64;
MGDNEKSEAL QNLLVFIYGD KPGRETHAKL LSILEGVEHG PGLQGFTHRD AFLISYGDML
APAGGDRGSA AEDPSGEAVA ELPGSALADT FPAETGLSWL GNFLERRNEG AFTYLHLLPF
HPYSSDDGFS VVDYREVDPR FGTWEDIAAL GKGFKLAFDF VVNHGSVKSP WFQGFLAGDK
RYEGWYTTRP KDYDYSAVTR PRTHPLLTPF TRKDGSEVYV WTTFSADQVD YDFSNPEVLL
EFIRIFLEFA KRGARIIRLD AIGYLWKEDG HPCIHHAKTH AVVKLFRAIA ETLGLDLLLL
TETNVPHLQN VAYFGTGDEA HMVYNFALPP LVLHSLLSAD SGPLRSWAKT LPPYSEKGWL
FLNYLASHDG VGLGPAKGLV DDAAFALSIE EAQRRGALVS YKATPEGPIP YELNCSYVSL
AAPPSLGSAE IRARAFLASQ GVLLSLAGLP AVYFHSWIGS EAWTEGPELL GYNRAINRER
PPIDRVDREL DDPHSLRSLI YRGIKGFLQF RKAEEAFSPE IPQRILDADG AVFAVLRGPV
GGFPAKAKAG SAGISSRYVL CAQNLGAKPA TLRLRENGIP LEGIAGEELA LAPWETRWIA
YGGGEKRELS T
//
