ID PGK1_PIG Reviewed; 417 AA. AC Q7SIB7; Q6B6L7; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 124. DE RecName: Full=Phosphoglycerate kinase 1; DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P00558}; DE EC=2.7.2.3 {ECO:0000250|UniProtKB:P00558}; GN Name=PGK1; 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]. RC TISSUE=Skeletal muscle; RA Xu D.Q., Xiong Y.Z.; RT "Molecular cloning and characterization of porcine PGK1."; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007744|PDB:1HDI} RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 5-417 IN COMPLEX WITH SUBSTRATE RP AND AMP, AND COFACTOR. RX PubMed=11178909; DOI=10.1006/jmbi.2000.4294; RA Szilagyi A.N., Ghosh M., Garman E., Vas M.; RT "A 1.8 A resolution structure of pig muscle 3-phosphoglycerate kinase with RT bound MgADP and 3-phosphoglycerate in open conformation: new insight into RT the role of the nucleotide in domain closure."; RL J. Mol. Biol. 306:499-511(2001). RN [3] {ECO:0007744|PDB:1KF0} RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND COFACTOR. RX PubMed=12102622; DOI=10.1021/bi020210j; RA Kovari Z., Flachner B., Naray-Szabo G., Vas M.; RT "Crystallographic and thiol-reactivity studies on the complex of pig muscle RT phosphoglycerate kinase with ATP analogues: correlation between nucleotide RT binding mode and helix flexibility."; RL Biochemistry 41:8796-8806(2002). RN [4] {ECO:0007744|PDB:1VJC, ECO:0007744|PDB:1VJD} RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ATP. RX PubMed=15035615; DOI=10.1021/bi035022n; RA Flachner B., Kovari Z., Varga A., Gugolya Z., Vonderviszt F., RA Naray-Szabo G., Vas M.; RT "Role of phosphate chain mobility of MgATP in completing the 3- RT phosphoglycerate kinase catalytic site: binding, kinetic, and RT crystallographic studies with ATP and MgATP."; RL Biochemistry 43:3436-3449(2004). CC -!- FUNCTION: Catalyzes one of the two ATP producing reactions in the CC glycolytic pathway via the reversible conversion of 1,3- CC diphosphoglycerate to 3-phosphoglycerate. Both L- and D- forms of CC purine and pyrimidine nucleotides can be used as substrates, but the CC activity is much lower on pyrimidines. In addition to its role as a CC glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha CC cofactor protein (primer recognition protein). Acts as a protein kinase CC when localized to the mitochondrion where it phosphorylates pyruvate CC dehydrogenase kinase PDK1 to inhibit pyruvate dehydrogenase complex CC activity and suppress the formation of acetyl-coenzyme A from pyruvate, CC and consequently inhibit oxidative phosphorylation and promote CC glycolysis. May play a role in sperm motility. CC {ECO:0000250|UniProtKB:P00558}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl CC phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3; CC Evidence={ECO:0000250|UniProtKB:P00558}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14802; CC Evidence={ECO:0000250|UniProtKB:P00558}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14803; CC Evidence={ECO:0000250|UniProtKB:P00558}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000250|UniProtKB:P00558}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:11178909, ECO:0000269|PubMed:12102622}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 2/5. {ECO:0000250|UniProtKB:P00558}. CC -!- SUBUNIT: Monomer (PubMed:11178909, PubMed:15035615). Interacts with CC kinase MAPK1/ERK2; the interaction is direct, occurs under hypoxic CC conditions, and promotes its interaction with PIN1. Interacts with CC peptidyl-prolyl cis-trans isomerase PIN1; the interaction is direct, CC occurs under hypoxic conditions, and targets the protein to the CC mitochondrion by promoting interactions with the TOM complex. Interacts CC with mitochondrial circRNA mcPGK1 (via its 2nd stem-loop); the CC interaction is direct and targets the protein to the mitochondrion by CC promoting interactions with the TOM complex. Interacts with pyruvate CC dehydrogenase kinase PDK1; the interaction is direct, occurs under CC hypoxic conditions and leads to PDK1-mediated inhibition of pyruvate CC dehydrogenase complex activity (By similarity). CC {ECO:0000250|UniProtKB:P00558, ECO:0000269|PubMed:11178909, CC ECO:0000269|PubMed:15035615}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P00558}. Mitochondrion matrix CC {ECO:0000250|UniProtKB:P00558}. Note=Hypoxic conditions promote CC mitochondrial targeting. Targeted to the mitochondrion following CC phosphorylation by MAPK1/ERK2, cis-trans isomerization by PIN1, and CC binding to mitochondrial circRNA mcPGK1. CC {ECO:0000250|UniProtKB:P00558}. CC -!- PTM: Phosphorylated at Ser-203 by MAPK1/ERK2 under hypoxic conditions, CC which promotes its mitochondrial targeting. CC {ECO:0000250|UniProtKB:P00558}. CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=Ref.3; Type=Miscellaneous discrepancy; Note=The sequence shown in PDB entry 1KF0 is a tentative sequence based on the electron density. It differs from that shown in 14 positions.; Evidence={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; AY677198; AAT77773.1; -; mRNA. DR RefSeq; NP_001093402.1; NM_001099932.2. DR PDB; 1HDI; X-ray; 1.80 A; A=5-417. DR PDB; 1KF0; X-ray; 2.50 A; A=2-417. DR PDB; 1VJC; X-ray; 2.10 A; A=2-417. DR PDB; 1VJD; X-ray; 1.90 A; A=2-417. DR AlphaFoldDB; Q7SIB7; -. DR MDposit; Q7SIB7; -. DR SMR; Q7SIB7; -. DR FunCoup; Q7SIB7; 727. DR STRING; 9823.ENSSSCP00000013238; -. DR PaxDb; 9823-ENSSSCP00000013238; -. DR PeptideAtlas; Q7SIB7; -. DR GeneID; 407608; -. DR KEGG; ssc:407608; -. DR CTD; 5230; -. DR eggNOG; KOG1367; Eukaryota. DR InParanoid; Q7SIB7; -. DR OrthoDB; 275353at2759; -. DR BRENDA; 2.7.2.3; 6170. DR SABIO-RK; Q7SIB7; -. DR UniPathway; UPA00109; UER00185. DR EvolutionaryTrace; Q7SIB7; -. DR Proteomes; UP000008227; Unplaced. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB. DR GO; GO:0043531; F:ADP binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB. DR GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB. DR GO; GO:0106310; F:protein serine kinase activity; ISS:UniProtKB. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR CDD; cd00318; Phosphoglycerate_kinase; 1. DR FunFam; 3.40.50.1260:FF:000019; Phosphoglycerate kinase 1; 1. DR FunFam; 3.40.50.1260:FF:000031; Phosphoglycerate kinase 1; 1. DR Gene3D; 3.40.50.1260; Phosphoglycerate kinase, N-terminal domain; 3. DR HAMAP; MF_00145; Phosphoglyc_kinase; 1. DR InterPro; IPR001576; Phosphoglycerate_kinase. DR InterPro; IPR015911; Phosphoglycerate_kinase_CS. DR InterPro; IPR015824; Phosphoglycerate_kinase_N. DR InterPro; IPR036043; Phosphoglycerate_kinase_sf. DR PANTHER; PTHR11406; PHOSPHOGLYCERATE KINASE; 1. DR PANTHER; PTHR11406:SF14; PHOSPHOGLYCERATE KINASE 1; 1. DR Pfam; PF00162; PGK; 1. DR PIRSF; PIRSF000724; Pgk; 1. DR PRINTS; PR00477; PHGLYCKINASE. DR SUPFAM; SSF53748; Phosphoglycerate kinase; 1. DR PROSITE; PS00111; PGLYCERATE_KINASE; 1. DR PDBsum; 1HDI; -. DR PDBsum; 1KF0; -. DR PDBsum; 1VJC; -. DR PDBsum; 1VJD; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; Glycolysis; KW Hydroxylation; Kinase; Magnesium; Metal-binding; Mitochondrion; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P00558" FT CHAIN 2..417 FT /note="Phosphoglycerate kinase 1" FT /id="PRO_0000145837" FT REGION 38..43 FT /note="Mitochondrial targeting region exposed following FT cis-trans isomerization by PIN1 and recognized by the TOM FT complex for mitochondrial translocation of the protein" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 23 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 24 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000269|PubMed:12102622, FT ECO:0007744|PDB:1KF0" FT BINDING 25 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 26 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000269|PubMed:11178909, FT ECO:0000269|PubMed:12102622, ECO:0007744|PDB:1HDI, FT ECO:0007744|PDB:1KF0" FT BINDING 38 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 39 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000269|PubMed:11178909, FT ECO:0000269|PubMed:12102622, ECO:0007744|PDB:1HDI, FT ECO:0007744|PDB:1KF0" FT BINDING 62 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 63 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000269|PubMed:12102622, FT ECO:0007744|PDB:1KF0" FT BINDING 65 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 66 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000269|PubMed:11178909, FT ECO:0007744|PDB:1HDI" FT BINDING 122 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 123 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000269|PubMed:11178909, FT ECO:0000269|PubMed:12102622, ECO:0007744|PDB:1HDI, FT ECO:0007744|PDB:1KF0" FT BINDING 170 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 171 FT /ligand="(2R)-3-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58272" FT /evidence="ECO:0000269|PubMed:11178909, FT ECO:0000269|PubMed:12102622, ECO:0007744|PDB:1HDI, FT ECO:0007744|PDB:1KF0" FT BINDING 214 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 214 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 215 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000269|PubMed:11178909, FT ECO:0007744|PDB:1HDI" FT BINDING 215 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:15035615, FT ECO:0007744|PDB:1VJC, ECO:0007744|PDB:1VJD" FT BINDING 215 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 216 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000269|PubMed:11178909, FT ECO:0007744|PDB:1HDI" FT BINDING 218 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 219 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 219 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:12102622, FT ECO:0007744|PDB:1KF0" FT BINDING 220 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000269|PubMed:11178909, FT ECO:0007744|PDB:1HDI" FT BINDING 220 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:15035615, FT ECO:0007744|PDB:1VJC, ECO:0007744|PDB:1VJD" FT BINDING 238 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 238 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 239 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000269|PubMed:11178909, FT ECO:0007744|PDB:1HDI" FT BINDING 239 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:15035615, FT ECO:0007744|PDB:1VJC, ECO:0007744|PDB:1VJD" FT BINDING 313 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000269|PubMed:11178909, FT ECO:0007744|PDB:1HDI" FT BINDING 313 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:15035615, FT ECO:0007744|PDB:1VJC, ECO:0007744|PDB:1VJD" FT BINDING 338 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 340 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 343 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 343 FT /ligand="CDP" FT /ligand_id="ChEBI:CHEBI:58069" FT /evidence="ECO:0000250|UniProtKB:P00558" FT BINDING 344 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000269|PubMed:11178909, FT ECO:0007744|PDB:1HDI" FT BINDING 344 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:15035615, FT ECO:0007744|PDB:1VJC, ECO:0007744|PDB:1VJD" FT BINDING 375 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:15035615, FT ECO:0007744|PDB:1VJD" FT BINDING 375 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:11178909, FT ECO:0007744|PDB:1HDI" FT BINDING 376 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:15035615, FT ECO:0007744|PDB:1VJD" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 6 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P09411" FT MOD_RES 11 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 48 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 48 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09411" FT MOD_RES 75 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 76 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P09411" FT MOD_RES 86 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 91 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P09411" FT MOD_RES 97 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 97 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 131 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 131 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000250" FT MOD_RES 146 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 191 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P09411" FT MOD_RES 196 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 199 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 203 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 216 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 220 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 267 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 291 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 323 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P00558" FT MOD_RES 361 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P09411" FT HELIX 3..5 FT /evidence="ECO:0007829|PDB:1VJD" FT HELIX 9..11 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 18..22 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 29..35 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 38..52 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 56..61 FT /evidence="ECO:0007829|PDB:1HDI" FT TURN 73..75 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 79..89 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:1VJC" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 102..109 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 115..118 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 122..124 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 126..129 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 139..141 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 144..156 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 159..163 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 166..168 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 174..177 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 188..201 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 206..212 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 218..220 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 221..228 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 232..236 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 238..240 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 241..244 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 245..249 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 262..264 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 266..276 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 279..281 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 285..293 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 298..302 FT /evidence="ECO:0007829|PDB:1HDI" FT TURN 303..305 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 312..316 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 318..330 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 332..338 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 346..348 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 350..364 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 368..371 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 375..382 FT /evidence="ECO:0007829|PDB:1HDI" FT TURN 386..388 FT /evidence="ECO:0007829|PDB:1HDI" FT STRAND 389..392 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 396..403 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 406..408 FT /evidence="ECO:0007829|PDB:1HDI" FT HELIX 409..412 FT /evidence="ECO:0007829|PDB:1HDI" SQ SEQUENCE 417 AA; 44559 MW; B014E769058C1135 CRC64; MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAIPSIKFC LDNGAKSVVL MSHLGRPDGI PMPDKYSLEP VAVELKSLPG KDVLFLKDCV GPEVEKACAD PAAGSVILLE NLRFHVEEEG KGKDASGSKV KADPAKIEAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN LPKKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM AFTFLKVLNN MEIGTSLFDE EGSKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKIGQ ATVASGIPAG WMGLDCGPES SKKYSEAVAR AKQIVWNGPV GVFEWEAFAQ GTKALMDEVV KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNV //