LOCUS       YP_003419475             401 aa            linear   CON 10-JUN-2013
DEFINITION  aminotransferase, class I or II [Sulfolobus islandicus L.D.8.5].
ACCESSION   YP_003419475
VERSION     YP_003419475.1  GI:284997708
DBLINK      Project: 43679
            BioProject: PRJNA43679
DBSOURCE    REFSEQ: accession NC_013769.1
KEYWORDS    .
SOURCE      Sulfolobus islandicus L.D.8.5
  ORGANISM  Sulfolobus islandicus L.D.8.5
            Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
            Sulfolobus.
REFERENCE   1  (residues 1 to 401)
  AUTHORS   Reno,M.L., Held,N.L., Fields,C.J., Burke,P.V. and Whitaker,R.J.
  CONSRTM   US DOE Joint Genome Institute
  TITLE     Contemporary genome evolution in thermophilic Archaea
  JOURNAL   Unpublished
REFERENCE   2  (residues 1 to 401)
  CONSRTM   NCBI Genome Project
  TITLE     Direct Submission
  JOURNAL   Submitted (27-JAN-2010) National Center for Biotechnology
            Information, NIH, Bethesda, MD 20894, USA
REFERENCE   3  (residues 1 to 401)
  AUTHORS   Copeland,A., Lucas,S., Lapidus,A., Glavina del Rio,T., Dalin,E.,
            Tice,H., Pitluck,S., Bruce,D., Goodwin,L., Land,M., Whitaker,R.J.
            and Richardson,P.
  CONSRTM   US DOE Joint Genome Institute
  TITLE     Direct Submission
  JOURNAL   Submitted (03-SEP-2009) US DOE Joint Genome Institute, 2800
            Mitchell Drive B100, Walnut Creek, CA 94598-1698, USA
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence is identical to ADB87105.
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..401
                     /organism="Sulfolobus islandicus L.D.8.5"
                     /strain="L.D.8.5"
                     /db_xref="taxon:425944"
     Protein         1..401
                     /product="aminotransferase, class I or II"
                     /calculated_mol_wt=45577
     Region          5..398
                     /region_name="PRK05764"
                     /note="aspartate aminotransferase; Provisional"
                     /db_xref="CDD:235596"
     Region          38..392
                     /region_name="AAT_like"
                     /note="Aspartate aminotransferase family. This family
                     belongs to pyridoxal phosphate (PLP)-dependent aspartate
                     aminotransferase superfamily (fold I). Pyridoxal phosphate
                     combines with an alpha-amino acid to form a compound
                     called a Schiff base or aldimine...; cd00609"
                     /db_xref="CDD:99734"
     Site            order(103..105,129,180,211,238,240..241,249)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99734"
     Site            order(106,139,204,247..249,278,281)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99734"
     Site            241
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99734"
     CDS             1..401
                     /locus_tag="LD85_1437"
                     /coded_by="complement(NC_013769.1:1269119..1270324)"
                     /transl_table=11
                     /db_xref="GeneID:8761256"
CONTIG      join(WP_012713677.1:1..401)
ORIGIN      
        1 mvslldfnen msqvtgettl lykeiarnve ktkkikiidf gigqpdlptf krirdaakea
       61 ldqgftfyts afgidelrek iaqylntryg advrkeeviv tpgakpalfl vfilyinpgd
      121 evilpdpsfy syaevvkllg gkpiytnlkw skegfsidvd dlqskiskrt kmivfnnphn
      181 ptgtlfspnd vkkivdisrd nkiillsdei ydnfvyegkm rstledsdwr dfliyvngfs
      241 ktfsmtgwrl gyivakreii qkmgvlaani ytaptsfvqk aavkafdtfd evnemvklfk
      301 krrdvmydql ikvkgievsk pngafymfpn agkllkisgl dvksfairli eekgvvtipg
      361 evfplnigke flrlsfavne eviregvqki refaeqmmns r
//