DPYD_PIG
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 03-AUG-2022, entry version 147.
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}.
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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 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 AlphaFoldDB; Q28943; -.
DR SMR; Q28943; -.
DR STRING; 9823.ENSSSCP00000007333; -.
DR PaxDb; Q28943; -.
DR PeptideAtlas; Q28943; -.
DR PRIDE; Q28943; -.
DR GeneID; 397109; -.
DR KEGG; ssc:397109; -.
DR CTD; 1806; -.
DR eggNOG; KOG1799; Eukaryota.
DR InParanoid; Q28943; -.
DR OrthoDB; 592753at2759; -.
DR BRENDA; 1.3.1.2; 6170.
DR UniPathway; UPA00131; -.
DR EvolutionaryTrace; Q28943; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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: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; IEA:InterPro.
DR GO; GO:0006212; P:uracil catabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.1060.10; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.50.50.60; -; 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.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR044512; DPYD.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR43073; PTHR43073; 1.
DR Pfam; PF01180; DHO_dh; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1.
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 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 STRAND 321..323
FT /evidence="ECO:0007829|PDB:7LJS"
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:7LJT"
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:1GT8"
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
