LOCUS       1SI8_A                   484 aa            linear   BCT 01-FEB-2013
DEFINITION  Chain A, Crystal Structure Of E. Faecalis Catalase.
ACCESSION   1SI8_A
VERSION     1SI8_A
DBSOURCE    pdb: molecule 1SI8, chain 65, release Jan 25, 2013;
            deposition: Feb 28, 2004;
            class: Oxidoreductase;
            source: Mmdb_id: 27431, Pdb_id 1: 1SI8;
            Exp. method: X-Ray Diffraction.
KEYWORDS    .
SOURCE      Enterococcus faecalis V583
  ORGANISM  Enterococcus faecalis V583
            Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
            Enterococcus.
REFERENCE   1  (residues 1 to 484)
  AUTHORS   Frankenberg,L., Brugna,M. and Hederstedt,L.
  TITLE     Enterococcus faecalis heme-dependent catalase
  JOURNAL   J. Bacteriol. 184 (22), 6351-6356 (2002)
   PUBMED   12399505
REFERENCE   2  (residues 1 to 484)
  AUTHORS   Hakansson,K.O., Brugna,M. and Tasse,L.
  TITLE     The three-dimensional structure of catalase from Enterococcus
            faecalis
  JOURNAL   Acta Crystallogr. D Biol. Crystallogr. 60 (PT 8), 1374-1380 (2004)
   PUBMED   15272159
REFERENCE   3  (residues 1 to 484)
  AUTHORS   Hakansson,K.O., Brugna,M. and Tasse,L.
  TITLE     Direct Submission
  JOURNAL   Submitted (28-FEB-2004)
COMMENT     1 Catalase.
FEATURES             Location/Qualifiers
     source          1..484
                     /organism="Enterococcus faecalis V583"
                     /db_xref="taxon:226185"
     Region          1..475
                     /region_name="KatE"
                     /note="Catalase [Inorganic ion transport and metabolism];
                     COG0753"
                     /db_xref="CDD:223824"
     SecStr          21..24
                     /sec_str_type="sheet"
                     /note="strand 1"
     SecStr          27..30
                     /sec_str_type="sheet"
                     /note="strand 2"
     SecStr          34..45
                     /sec_str_type="helix"
                     /note="helix 1"
     Region          47..474
                     /region_name="catalase_clade_3"
                     /note="Clade 3 of the heme-binding enzyme catalase;
                     cd08156"
                     /db_xref="CDD:163712"
     Site            order(47,52,100..101,120..121,136..140,142,145,151..156,
                     160,163,227,230,233..234,238,241..242,245,268..269,274,
                     276,302,304..305,307,310,317..318,326,328,331,334..336,
                     339..340,343..345,347..348,350..353,357,361..362,364,367,
                     369..371,380..385,444..445,447,450,454)
                     /site_type="other"
                     /note="tetramer interface [polypeptide binding]"
                     /db_xref="CDD:163712"
     Region          51..484
                     /region_name="Domain 1"
                     /note="NCBI Domains"
     Site            order(54,93,127,132,140,333,337)
                     /site_type="other"
                     /note="heme binding pocket [chemical binding]"
                     /db_xref="CDD:163712"
     SecStr          56..61
                     /sec_str_type="sheet"
                     /note="strand 3"
     SecStr          62..66
                     /sec_str_type="sheet"
                     /note="strand 4"
     SecStr          67..70
                     /sec_str_type="sheet"
                     /note="strand 5"
     SecStr          80..83
                     /sec_str_type="sheet"
                     /note="strand 6"
     SecStr          84..89
                     /sec_str_type="sheet"
                     /note="strand 7"
     SecStr          90..95
                     /sec_str_type="sheet"
                     /note="strand 8"
     SecStr          108..118
                     /sec_str_type="sheet"
                     /note="strand 9"
     SecStr          119..128
                     /sec_str_type="sheet"
                     /note="strand 10"
     Site            order(130,173,177,180,182,192,214,216,281..284,419,
                     422..423)
                     /site_type="other"
                     /note="NADPH binding site [chemical binding]"
                     /db_xref="CDD:163712"
     SecStr          140..147
                     /sec_str_type="helix"
                     /note="helix 2"
     SecStr          158..167
                     /sec_str_type="helix"
                     /note="helix 3"
     SecStr          172..179
                     /sec_str_type="helix"
                     /note="helix 4"
     SecStr          191..195
                     /sec_str_type="sheet"
                     /note="strand 11"
     SecStr          198..204
                     /sec_str_type="sheet"
                     /note="strand 12"
     SecStr          206..218
                     /sec_str_type="sheet"
                     /note="strand 13"
     SecStr          226..235
                     /sec_str_type="helix"
                     /note="helix 5"
     SecStr          239..250
                     /sec_str_type="helix"
                     /note="helix 6"
     SecStr          253..265
                     /sec_str_type="sheet"
                     /note="strand 14"
     SecStr          289..299
                     /sec_str_type="sheet"
                     /note="strand 15"
     SecStr          321..324
                     /sec_str_type="sheet"
                     /note="strand 16"
     SecStr          327..334
                     /sec_str_type="helix"
                     /note="helix 7"
     SecStr          337..344
                     /sec_str_type="helix"
                     /note="helix 8"
     Het             bond(337)
                     /heterogen="(HEM,1003 )"
     SecStr          418..426
                     /sec_str_type="helix"
                     /note="helix 9"
     SecStr          429..443
                     /sec_str_type="helix"
                     /note="helix 10"
     SecStr          449..462
                     /sec_str_type="helix"
                     /note="helix 11"
     SecStr          463..475
                     /sec_str_type="helix"
                     /note="helix 12"
ORIGIN      
        1 mknqhlttsq gspvgdnqns ltagefgpvl iqdvhllekl ahfnrervpe rvvhakgaga
       61 hgifkvsqsm aqytkadfls evgketplfa rfstvagelg ssdtlrdprg falkfytdeg
      121 nydlvgnntp iffirdaikf pdfihsqkrn prthlkspea vwdfwshspe slhqvtilms
      181 drgiplsfrh mhgfgshtfk wvnaagevff vkyhfktnqg iknlesqlae eiagknpdfh
      241 iedlhnaien qefpswtlsv qiipyadalt mketlfdvtk tvsqkeypli evgtmtlnrn
      301 penyfaeveq vtfspgnfvp gieaspdkll qgrlfaygda hrhrvgansh qlpinqakap
      361 vnnyqkdgnm rfnngnsein yepnsytetp kedptakiss fevegnvgny synqdhftqa
      421 nalynllpse ekenlinnia aslgqvknqe iiarqidlft rvnpeygarv aqaikqqahh
      481 hhhh
//