LOCUS ACR72075.1 478 aa PRT BCT 25-AUG-2017 DEFINITION [Eubacterium] eligens ATCC 27750 starch synthase protein. ACCESSION CP001104-1029 PROTEIN_ID ACR72075.1 SOURCE [Eubacterium] eligens ATCC 27750 ORGANISM [Eubacterium] eligens ATCC 27750 Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae; Lachnospira. REFERENCE 1 (bases 1 to 2144190) AUTHORS Mahowald,M.A., Rey,F.E., Seedorf,H., Turnbaugh,P.J., Fulton,R.S., Wollam,A., Shah,N., Wang,C., Magrini,V., Wilson,R.K., Cantarel,B.L., Coutinho,P.M., Henrissat,B., Crock,L.W., Russell,A., Verberkmoes,N.C., Hettich,R.L. and Gordon,J.I. TITLE Characterizing a model human gut microbiota composed of members of its two dominant bacterial phyla JOURNAL Proc. Natl. Acad. Sci. U.S.A. 106 (14), 5859-5864 (2009) PUBMED 19321416 REFERENCE 2 (bases 1 to 2144190) AUTHORS Mahowald,M.A., Henrissat,B., Coutinho,P.M., Cantarel,B.L., Wollam,A., Fulton,R.S., Fulton,L.A., Wilson,R.K. and Gordon,J.I. TITLE Genomic and transcriptional studies of human gut bacteria suggest mutualistic relationship between model Bacteroidetes and Firmicutes JOURNAL Unpublished REFERENCE 3 (bases 1 to 2144190) AUTHORS Mahowald,M.A., Henrissat,B., Coutinho,P.M., Cantarel,B.L., Wollam,A., Fulton,R.S., Fulton,L.A., Wilson,R.K. and Gordon,J.I. TITLE Direct Submission JOURNAL Submitted (03-JUN-2008) Center for Genome Sciences, Washington University in St. Louis, 4444 Forest Park Ave., St. Louis, MO 63108, USA COMMENT This genome was sequenced by the Genome Sequencing Center, Washington University School of Medicine, Washington University in St. Louis. Source DNA is available from Jeffrey I. Gordon, jgordon@wustl.edu. FEATURES Qualifiers source /organism="[Eubacterium] eligens ATCC 27750" /mol_type="genomic DNA" /strain="ATCC 27750" /culture_collection="ATCC:27750" /type_material="type strain of Eubacterium eligens" /db_xref="taxon:515620" protein /locus_tag="EUBELI_01075" /note="Psort-B: Unknown cell location; COG0297 Glycogen synthase; HMMPfam:IPR001296; HMMPfam:IPR013534; HMMTigr:IPR011835; K00703 starch synthase" /transl_table=11 BEGIN 1 MKNVLLIASE AVPFIKTGGL ADVAGSLPKY FDKTKFDVRV MIPKYTCIPW EYREKMVYKT 61 HFYIDLAWRT QYVGVFELEW NGVTFYFIDN EFYFGGNKPY SWIHEDIEKF AFFSKAALSA 121 LPVLGFRPDI IHCNDWQTGL IPVYLKERFS QGEFYQGIKS IMTIHNLKFQ GIWDLKKVKD 181 ITGLPDEYFT SDKLEAYDDA NYLKGGIVYA DRVTTVSETY AEEIKTPFYG ENLDGLMRAR 241 SNVLSGIVNG IDYDEYNPET DKRIPNNYNQ VTFRKEKWKN KVALQKELGL TEDKGKFMIG 301 LVSRLTDQKG LDLVAYVMDQ LCAEDVQFVV LGTGEERYEN MFRHYDWKYN DRVSANIYYS 361 EDMSHKIYAA CDAFLMPSLF EPCGLSQLMS LRYGTVPIVR ETGGLKDTVE PYNEYEGKGT 421 GFSFANYNAH EMLGIVNYAK DVYYNHKREW NKIVDRGMKT DFSWNSSARK YEELYNSL //