ID   DPYD_PIG                Reviewed;        1025 AA.
AC   Q28943;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Dihydropyrimidine dehydrogenase [NADP(+)] {ECO:0000305};
DE            Short=DHPDHase;
DE            Short=DPD;
DE            EC=1.3.1.2 {ECO:0000269|PubMed:20831907, ECO:0000269|PubMed:8083224, ECO:0000269|PubMed:9860876};
DE   AltName: Full=Dihydrothymine dehydrogenase;
DE   AltName: Full=Dihydrouracil dehydrogenase;
DE   Flags: Precursor;
GN   Name=DPYD;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CATALYTIC
RP   ACTIVITY.
RC   TISSUE=Liver;
RX   PubMed=8083224; DOI=10.1016/s0021-9258(17)31638-1;
RA   Yokota H., Fernandez-Salguero P., Furuya H., Lin K., McBride O.W.,
RA   Podschun B., Schnackerz K.D., Gonzalez F.J.;
RT   "cDNA cloning and chromosome mapping of human dihydropyrimidine
RT   dehydrogenase, an enzyme associated with 5-fluorouracil toxicity and
RT   congenital thymine uraciluria.";
RL   J. Biol. Chem. 269:23192-23196(1994).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND MUTAGENESIS OF
RP   CYS-671.
RX   PubMed=9860876; DOI=10.1021/bi9815997;
RA   Rosenbaum K., Jahnke K., Curti B., Hagen W.R., Schnackerz K.D.,
RA   Vanoni M.A.;
RT   "Porcine recombinant dihydropyrimidine dehydrogenase: comparison of the
RT   spectroscopic and catalytic properties of the wild-type and C671A mutant
RT   enzymes.";
RL   Biochemistry 37:17598-17609(1998).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF CYS-126;
RP   GLN-156; ARG-235 AND SER-670.
RX   PubMed=20831907; DOI=10.1016/j.bbapap.2010.08.014;
RA   Lohkamp B., Voevodskaya N., Lindqvist Y., Dobritzsch D.;
RT   "Insights into the mechanism of dihydropyrimidine dehydrogenase from site-
RT   directed mutagenesis targeting the active site loop and redox cofactor
RT   coordination.";
RL   Biochim. Biophys. Acta 1804:2198-2206(2010).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEXES WITH 5-FLUOROURACIL;
RP   FAD; FMN; 4FE-4S IRON-SULFUR CLUSTER AND NADP, FUNCTION, SUBUNIT, AND
RP   COFACTOR.
RX   PubMed=11179210; DOI=10.1093/emboj/20.4.650;
RA   Dobritzsch D., Schneider G., Schnackerz K.D., Lindqvist Y.;
RT   "Crystal structure of dihydropyrimidine dehydrogenase, a major determinant
RT   of the pharmacokinetics of the anti-cancer drug 5-fluorouracil.";
RL   EMBO J. 20:650-660(2001).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH 5-IODOURACIL; FAD;
RP   FMN; 4FE-4S IRON-SULFUR CLUSTER AND NADP, COFACTOR, AND ACTIVE SITE.
RX   PubMed=11796730; DOI=10.1074/jbc.m111877200;
RA   Dobritzsch D., Ricagno S., Schneider G., Schnackerz K.D., Lindqvist Y.;
RT   "Crystal structure of the productive ternary complex of dihydropyrimidine
RT   dehydrogenase with NADPH and 5-iodouracil. Implications for mechanism of
RT   inhibition and electron transfer.";
RL   J. Biol. Chem. 277:13155-13166(2002).
CC   -!- FUNCTION: Involved in pyrimidine base degradation. Catalyzes the
CC       reduction of uracil and thymine. {ECO:0000269|PubMed:11179210,
CC       ECO:0000269|PubMed:20831907, ECO:0000269|PubMed:9860876}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrouracil + NADP(+) = H(+) + NADPH + uracil;
CC         Xref=Rhea:RHEA:18093, ChEBI:CHEBI:15378, ChEBI:CHEBI:15901,
CC         ChEBI:CHEBI:17568, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.2;
CC         Evidence={ECO:0000269|PubMed:20831907, ECO:0000269|PubMed:8083224,
CC         ECO:0000269|PubMed:9860876};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18095;
CC         Evidence={ECO:0000269|PubMed:8083224};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-dihydrothymine + NADP(+) = H(+) + NADPH + thymine;
CC         Xref=Rhea:RHEA:58284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17821,
CC         ChEBI:CHEBI:27468, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.2;
CC         Evidence={ECO:0000269|PubMed:8083224};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58286;
CC         Evidence={ECO:0000305|PubMed:8083224};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC       Note=Binds 2 FAD. {ECO:0000269|PubMed:11796730};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC       Note=Binds 2 FMN. {ECO:0000269|PubMed:11796730};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 4 [4Fe-4S] clusters. Contains approximately 16 iron atoms
CC       per subunit. {ECO:0000269|PubMed:11796730};
CC   -!- ACTIVITY REGULATION: Inactivated by 5-iodouracil.
CC       {ECO:0000269|PubMed:11796730}.
CC   -!- PATHWAY: Amino-acid biosynthesis; beta-alanine biosynthesis.
CC       {ECO:0000305|PubMed:8083224}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11179210,
CC       ECO:0000269|PubMed:11796730, ECO:0000269|PubMed:9860876}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC       {ECO:0000305}.
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; U09179; AAA57475.1; -; mRNA.
DR   PIR; B54718; B54718.
DR   RefSeq; NP_999209.1; NM_214044.2.
DR   PDB; 1GT8; X-ray; 3.30 A; A/B/C/D=1-1025.
DR   PDB; 1GTE; X-ray; 1.65 A; A/B/C/D=1-1025.
DR   PDB; 1GTH; X-ray; 2.25 A; A/B/C/D=1-1025.
DR   PDB; 1H7W; X-ray; 1.90 A; A/B/C/D=1-1025.
DR   PDB; 1H7X; X-ray; 2.01 A; A/B/C/D=1-1025.
DR   PDB; 7LJS; X-ray; 2.00 A; A/B/C/D=1-1025.
DR   PDB; 7LJT; X-ray; 1.98 A; A/B/C/D=1-1025.
DR   PDB; 7LJU; X-ray; 1.87 A; A/B/C/D=1-1025.
DR   PDB; 7M31; X-ray; 1.69 A; A/B/C/D=1-1025.
DR   PDB; 7M32; X-ray; 1.82 A; A/B/C/D=1-1025.
DR   PDB; 8F5W; X-ray; 1.97 A; A/B/C/D=1-1025.
DR   PDB; 8F61; X-ray; 2.14 A; A/B/C/D=1-1025.
DR   PDB; 8F6N; X-ray; 2.12 A; A/B/C/D=1-1018.
DR   PDBsum; 1GT8; -.
DR   PDBsum; 1GTE; -.
DR   PDBsum; 1GTH; -.
DR   PDBsum; 1H7W; -.
DR   PDBsum; 1H7X; -.
DR   PDBsum; 7LJS; -.
DR   PDBsum; 7LJT; -.
DR   PDBsum; 7LJU; -.
DR   PDBsum; 7M31; -.
DR   PDBsum; 7M32; -.
DR   PDBsum; 8F5W; -.
DR   PDBsum; 8F61; -.
DR   PDBsum; 8F6N; -.
DR   AlphaFoldDB; Q28943; -.
DR   SMR; Q28943; -.
DR   STRING; 9823.ENSSSCP00000007333; -.
DR   PaxDb; 9823-ENSSSCP00000007333; -.
DR   PeptideAtlas; Q28943; -.
DR   GeneID; 397109; -.
DR   KEGG; ssc:397109; -.
DR   CTD; 1806; -.
DR   eggNOG; KOG1799; Eukaryota.
DR   InParanoid; Q28943; -.
DR   OrthoDB; 1211169at2759; -.
DR   BRENDA; 1.3.1.2; 6170.
DR   UniPathway; UPA00131; -.
DR   EvolutionaryTrace; Q28943; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0017113; F:dihydropyrimidine dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR   GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0002058; F:uracil binding; IBA:GO_Central.
DR   GO; GO:0019483; P:beta-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006214; P:thymidine catabolic process; ISS:UniProtKB.
DR   GO; GO:0006210; P:thymine catabolic process; IBA:GO_Central.
DR   GO; GO:0006212; P:uracil catabolic process; ISS:UniProtKB.
DR   CDD; cd02940; DHPD_FMN; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005720; Dihydroorotate_DH_cat.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF01180; DHO_dh; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF14697; Fer4_21; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 2.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Acetylation; Cytoplasm; Direct protein sequencing;
KW   FAD; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding; NADP;
KW   Nucleotide-binding; Oxidoreductase; Reference proteome; Repeat.
FT   PROPEP          1..3
FT                   /id="PRO_0000021116"
FT   CHAIN           4..1025
FT                   /note="Dihydropyrimidine dehydrogenase [NADP(+)]"
FT                   /id="PRO_0000021117"
FT   DOMAIN          69..100
FT                   /note="4Fe-4S ferredoxin-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          944..976
FT                   /note="4Fe-4S ferredoxin-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   DOMAIN          978..1007
FT                   /note="4Fe-4S ferredoxin-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   ACT_SITE        671
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         79
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT   BINDING         82
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT   BINDING         87
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT   BINDING         91
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT   BINDING         129
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         130
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT   BINDING         136
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT   BINDING         140
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT   BINDING         156
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT   BINDING         194..198
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         218..226
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         235
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         261
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         340..343
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         364..365
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         371
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         437..439
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         480..489
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         481..487
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         550
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         574..575
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         609
FT                   /ligand="substrate"
FT   BINDING         668..670
FT                   /ligand="substrate"
FT   BINDING         709
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         736..737
FT                   /ligand="substrate"
FT   BINDING         767
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         793..795
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         816..817
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000269|PubMed:11796730"
FT   BINDING         953
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT   BINDING         956
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT   BINDING         959
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT   BINDING         963
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT   BINDING         986
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT   BINDING         989
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT   BINDING         992
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT   BINDING         996
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="4"
FT   MOD_RES         384
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12882"
FT   MUTAGEN         126
FT                   /note="C->A: No effect on enzyme activity. Reduced iron
FT                   content."
FT                   /evidence="ECO:0000269|PubMed:20831907"
FT   MUTAGEN         156
FT                   /note="Q->E: Loss of enzyme activity. Reduces iron
FT                   content."
FT                   /evidence="ECO:0000269|PubMed:20831907"
FT   MUTAGEN         235
FT                   /note="R->A,K: Loss of enzyme activity. Loss of FAD
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:20831907"
FT   MUTAGEN         670
FT                   /note="S->A: Strongly reduced affinity for uracil. Reduces
FT                   enzyme activity by 30%."
FT                   /evidence="ECO:0000269|PubMed:20831907"
FT   MUTAGEN         671
FT                   /note="C->A: Reduces catalytic activity by 99%."
FT                   /evidence="ECO:0000269|PubMed:9860876"
FT   MUTAGEN         673
FT                   /note="H->Q: Reduces activity by 50%."
FT   HELIX           10..15
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   TURN            16..18
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           31..41
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           69..78
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           86..89
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           97..105
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           109..119
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           123..129
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           132..134
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           136..139
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           141..144
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:8F6N"
FT   HELIX           152..166
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           179..181
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           184..187
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          190..193
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           197..208
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          214..222
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           226..229
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   TURN            233..235
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           238..249
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   TURN            250..252
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          254..258
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           268..273
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          278..281
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           292..294
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   TURN            299..302
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          303..305
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           306..317
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   TURN            319..321
FT                   /evidence="ECO:0007829|PDB:8F5W"
FT   STRAND          322..324
FT                   /evidence="ECO:0007829|PDB:1H7X"
FT   STRAND          333..338
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           342..353
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          357..362
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           367..369
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           374..382
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          386..388
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          390..399
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          402..413
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          415..417
FT                   /evidence="ECO:0007829|PDB:8F5W"
FT   STRAND          419..430
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          432..436
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           445..450
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   TURN            451..453
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          460..462
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   TURN            466..468
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          476..478
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           481..483
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           489..510
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           527..530
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          535..537
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          540..548
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           552..554
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           557..566
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          569..572
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           579..581
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          590..592
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          601..603
FT                   /evidence="ECO:0007829|PDB:7LJT"
FT   STRAND          607..609
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           618..631
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          635..641
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           647..659
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          663..668
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           676..678
FT                   /evidence="ECO:0007829|PDB:7M31"
FT   HELIX           684..686
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           688..701
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          706..710
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           717..727
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          730..734
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          738..740
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          750..752
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   TURN            755..758
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          763..767
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           768..770
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           771..784
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          790..795
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           799..807
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          811..816
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           817..820
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           826..840
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           844..846
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          848..850
FT                   /evidence="ECO:0007829|PDB:1GT8"
FT   STRAND          858..860
FT                   /evidence="ECO:0007829|PDB:8F5W"
FT   TURN            869..873
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           880..899
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           921..924
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   TURN            925..928
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           929..931
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           935..937
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          940..942
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          944..948
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   TURN            950..952
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           958..966
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          971..973
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   TURN            975..977
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          980..982
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   HELIX           991..995
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   TURN            999..1001
FT                   /evidence="ECO:0007829|PDB:1GTE"
FT   STRAND          1002..1006
FT                   /evidence="ECO:0007829|PDB:1GTE"
SQ   SEQUENCE   1025 AA;  111424 MW;  B8D553AD862845D0 CRC64;
     MAPVLSKDVA DIESILALNP RTQSHAALHS TLAKKLDKKH WKRNPDKNCF HCEKLENNFG
     DIKHTTLGER GALREAMRCL KCADAPCQKS CPTHLDIKSF ITSISNKNYY GAAKMIFSDN
     PLGLTCGMVC PTSDLCVGGC NLYATEEGSI NIGGLQQFAS EVFKAMNIPQ IRNPCLPSQE
     KMPEAYSAKI ALLGAGPASI SCASFLARLG YSDITIFEKQ EYVGGLSTSE IPQFRLPYDV
     VNFEIELMKD LGVKIICGKS LSENEITLNT LKEEGYKAAF IGIGLPEPKT DDIFQGLTQD
     QGFYTSKDFL PLVAKSSKAG MCACHSPLPS IRGAVIVLGA GDTAFDCATS ALRCGARRVF
     LVFRKGFVNI RAVPEEVELA KEEKCEFLPF LSPRKVIVKG GRIVAVQFVR TEQDETGKWN
     EDEDQIVHLK ADVVISAFGS VLRDPKVKEA LSPIKFNRWD LPEVDPETMQ TSEPWVFAGG
     DIVGMANTTV ESVNDGKQAS WYIHKYIQAQ YGASVSAKPE LPLFYTPVDL VDISVEMAGL
     KFINPFGLAS AAPTTSSSMI RRAFEAGWGF ALTKTFSLDK DIVTNVSPRI VRGTTSGPMY
     GPGQSSFLNI ELISEKTAAY WCQSVTELKA DFPDNIVIAS IMCSYNKNDW MELSRKAEAS
     GADALELNLS CPHGMGERGM GLACGQDPEL VRNICRWVRQ AVQIPFFAKL TPNVTDIVSI
     ARAAKEGGAD GVTATNTVSG LMGLKADGTP WPAVGAGKRT TYGGVSGTAI RPIALRAVTT
     IARALPGFPI LATGGIDSAE SGLQFLHSGA SVLQVCSAVQ NQDFTVIQDY CTGLKALLYL
     KSIEELQGWD GQSPGTESHQ KGKPVPRIAE LMGKKLPNFG PYLEQRKKII AEEKMRLKEQ
     NAAFPPLERK PFIPKKPIPA IKDVIGKALQ YLGTFGELSN IEQVVAVIDE EMCINCGKCY
     MTCNDSGYQA IQFDPETHLP TVTDTCTGCT LCLSVCPIID CIRMVSRTTP YEPKRGLPLA
     VNPVC
//