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Chain A, Dihydroorotate dehydrogenase (quinone)

PDB: 1F76_A

Identical Proteins FASTA Graphics 

LOCUS       1F76_A                   336 aa            linear   BCT 01-DEC-2020
DEFINITION  Chain A, Dihydroorotate dehydrogenase (quinone).
ACCESSION   1F76_A
VERSION     1F76_A
DBSOURCE    pdb: molecule 1F76, chain A, release Mar 12, 2014;
            deposition: Jun 26, 2000;
            class: Oxidoreductase;
            source: Mmdb_id: 20764, Pdb_id 1: 1F76;
            Exp. method: X-Ray Diffraction.
KEYWORDS    .
SOURCE      Escherichia coli K-12
  ORGANISM  Escherichia coli K-12
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 336)
  AUTHORS   Bjornberg,O., Jensen,K.F., Gruner,A.-C., Ottosen,M., Sore,P.,
            Rowland,P., Norager,S. and Larsen,S.
  TITLE     The Dihydroorotate Dehydrogenases Of Escherichia Co Lactococcus
            Lactis Represent Two Distinct Families Enzyme
  JOURNAL   Flavins And Flavoproteins,Proc.13th Int.Symp., 607 (1999)
REFERENCE   2  (residues 1 to 336)
  AUTHORS   Palfey,B., Bjornberg,O. and Jensen,K.F.
  TITLE     Reduction Reactions Of Two Dihydroorotate Dehydroge
  JOURNAL   Flavins And Flavoproteins,Proc.13th Int.Symp., 615 (1999)
REFERENCE   3  (residues 1 to 336)
  AUTHORS   Bjornberg,O., Gruner,A.C., Roepstorff,P. and Jensen,K.F.
  TITLE     The activity of Escherichia coli dihydroorotate dehydrogenase is
            dependent on a conserved loop identified by sequence homology,
            mutagenesis, and limited proteolysis
  JOURNAL   Biochemistry 38 (10), 2899-2908 (1999)
   PUBMED   10074342
REFERENCE   4  (residues 1 to 336)
  AUTHORS   Rowland,P., Norager,S., Jensen,K.F. and Larsen,S.
  TITLE     Crystallization and preliminary X-ray studies of
            membrane-associated Escherichia coli dihydroorotate dehydrogenase
  JOURNAL   Acta Crystallogr. D Biol. Crystallogr. 56 (PT 5), 659-661 (2000)
   PUBMED   10771442
REFERENCE   5  (residues 1 to 336)
  AUTHORS   Norager,S., Jensen,K.F., Bjornberg,O. and Larsen,S.
  TITLE     E. coli dihydroorotate dehydrogenase reveals structural and
            functional distinctions between different classes of dihydroorotate
            dehydrogenases
  JOURNAL   Structure 10 (9), 1211-1223 (2002)
   PUBMED   12220493
REFERENCE   6  (residues 1 to 336)
  AUTHORS   Norager,S., Jensen,K.F., Bjornberg,O. and Larsen,S.
  TITLE     Direct Submission
  JOURNAL   Submitted (26-JUN-2000)
COMMENT     Escherichia Coli Dihydroorotate Dehydrogenase.
FEATURES             Location/Qualifiers
     source          1..336
                     /organism="Escherichia coli K-12"
                     /db_xref="taxon:83333"
     NonStdRes       1
                     /non_std_residue="MSE NH3+"
     Het             bond(1)
                     /heterogen="(ORO,1002)"
     Region          2..336
                     /region_name="PRK05286"
                     /note="quinone-dependent dihydroorotate dehydrogenase"
                     /db_xref="CDD:235388"
     SecStr          3..11
                     /sec_str_type="helix"
                     /note="helix 1"
     SecStr          15..29
                     /sec_str_type="helix"
                     /note="helix 2"
     SecStr          46..50
                     /sec_str_type="sheet"
                     /note="strand 1"
     NonStdRes       50
                     /non_std_residue="MSE"
     SecStr          51..55
                     /sec_str_type="sheet"
                     /note="strand 2"
     SecStr          57..63
                     /sec_str_type="sheet"
                     /note="strand 3"
     SecStr          70..77
                     /sec_str_type="helix"
                     /note="helix 3"
     NonStdRes       77
                     /non_std_residue="MSE"
     SecStr          80..85
                     /sec_str_type="sheet"
                     /note="strand 4"
     SecStr          89..94
                     /sec_str_type="sheet"
                     /note="strand 5"
     SecStr          99..104
                     /sec_str_type="sheet"
                     /note="strand 6"
     SecStr          107..112
                     /sec_str_type="sheet"
                     /note="strand 7"
     NonStdRes       113
                     /non_std_residue="MSE"
     SecStr          115..120
                     /sec_str_type="sheet"
                     /note="strand 8"
     SecStr          121..129
                     /sec_str_type="helix"
                     /note="helix 4"
     SecStr          134..141
                     /sec_str_type="sheet"
                     /note="strand 9"
     SecStr          153..162
                     /sec_str_type="helix"
                     /note="helix 5"
     NonStdRes       159
                     /non_std_residue="MSE"
     SecStr          167..172
                     /sec_str_type="sheet"
                     /note="strand 10"
     SecStr          188..208
                     /sec_str_type="helix"
                     /note="helix 6"
     NonStdRes       207
                     /non_std_residue="MSE"
     SecStr          213..218
                     /sec_str_type="sheet"
                     /note="strand 11"
     SecStr          224..237
                     /sec_str_type="helix"
                     /note="helix 7"
     SecStr          240..244
                     /sec_str_type="sheet"
                     /note="strand 12"
     NonStdRes       257
                     /non_std_residue="MSE"
     SecStr          264..269
                     /sec_str_type="sheet"
                     /note="strand 13"
     SecStr          272..286
                     /sec_str_type="helix"
                     /note="helix 8"
     SecStr          290..295
                     /sec_str_type="sheet"
                     /note="strand 14"
     SecStr          301..310
                     /sec_str_type="helix"
                     /note="helix 9"
     SecStr          313..317
                     /sec_str_type="sheet"
                     /note="strand 15"
     SecStr          327..335
                     /sec_str_type="helix"
                     /note="helix 10"
ORIGIN      
        1 xyypfvrkal fqldperahe ftfqqlrrit gtpfealvrq kvpakpvncx gltfknplgl
       61 aagldkdgec idalgaxgfg sieigtvtpr pqpgndkprl frlvdaegli nrxgfnnlgv
      121 dnlvenvkka hydgvlgini gknkdtpveq gkddylicxe kiyayagyia inisspntpg
      181 lrtlqygeal ddlltaiknk qndlqaxhhk yvpiavkiap dlseeeliqv adslvrhnid
      241 gviatnttld rslvqgxknc dqtgglsgrp lqlksteiir rlslelngrl piigvggids
      301 viaarekiaa gaslvqiysg fifkgpplik eivthi
//
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