ID XYLA_STRRU Reviewed; 388 AA. AC P24300; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 159. DE RecName: Full=Xylose isomerase; DE EC=5.3.1.5; GN Name=xylA; OS Streptomyces rubiginosus. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces; Streptomyces pseudogriseolus group. OX NCBI_TaxID=1929; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1657868; DOI=10.1128/jb.173.21.6849-6858.1991; RA Wong H.C., Ting Y., Lin H.C., Reichert F., Myambo K., Watt K.W., Toy P.L., RA Drummond R.J.; RT "Genetic organization and regulation of the xylose degradation genes in RT Streptomyces rubiginosus."; RL J. Bacteriol. 173:6849-6858(1991). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX PubMed=2734296; DOI=10.1073/pnas.86.12.4440; RA Carrell H.L., Glusker J.P., Burger V., Manfre F., Tritsch D., RA Biellmann J.-F.; RT "X-ray analysis of D-xylose isomerase at 1.9 A: native enzyme in complex RT with substrate and with a mechanism-designed inactivator."; RL Proc. Natl. Acad. Sci. U.S.A. 86:4440-4444(1989). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). RX PubMed=2006134; DOI=10.1002/prot.340090302; RA Whitlow M., Howard A.J., Finzel B.C., Poulos T.L., Winborne E., RA Gilliland G.L.; RT "A metal-mediated hydride shift mechanism for xylose isomerase based on the RT 1.6 A Streptomyces rubiginosus structures with xylitol and D-xylose."; RL Proteins 9:153-173(1991). CC -!- FUNCTION: Involved in D-xylose catabolism. CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-xylose = alpha-D-xylulofuranose; Xref=Rhea:RHEA:22816, CC ChEBI:CHEBI:28518, ChEBI:CHEBI:188998; EC=5.3.1.5; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homotetramer. CC -!- INTERACTION: CC P24300; P24300: xylA; NbExp=4; IntAct=EBI-15859851, EBI-15859851; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}. CC -!- CAUTION: According to the crystallographic study residue 40 could be CC Gln. {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; M73789; AAA26838.1; -; Genomic_DNA. DR PIR; B41339; B41339. DR PDB; 1GW9; X-ray; 1.55 A; A=1-387. DR PDB; 1MNZ; X-ray; 0.99 A; A=1-388. DR PDB; 1O1H; X-ray; 1.40 A; A/B=2-388. DR PDB; 1OAD; X-ray; 1.50 A; A/B=2-388. DR PDB; 1XIB; X-ray; 1.60 A; A=1-388. DR PDB; 1XIC; X-ray; 1.60 A; A=1-388. DR PDB; 1XID; X-ray; 1.70 A; A=1-388. DR PDB; 1XIE; X-ray; 1.70 A; A=1-388. DR PDB; 1XIF; X-ray; 1.60 A; A=1-388. DR PDB; 1XIG; X-ray; 1.70 A; A=1-388. DR PDB; 1XIH; X-ray; 1.70 A; A=1-388. DR PDB; 1XII; X-ray; 1.70 A; A=1-388. DR PDB; 1XIJ; X-ray; 1.70 A; A=1-388. DR PDB; 1XIS; X-ray; 1.60 A; A=2-388. DR PDB; 2G4J; X-ray; 1.85 A; A=2-388. DR PDB; 2GLK; X-ray; 0.94 A; A=1-388. DR PDB; 2GUB; X-ray; 1.80 A; A=1-388. DR PDB; 2GVE; Neutron; 2.20 A; A=1-388. DR PDB; 2XIS; X-ray; 1.71 A; A=2-388. DR PDB; 3CWH; Neutron; 2.20 A; A=1-388. DR PDB; 3GNX; X-ray; 2.00 A; A/E=2-388. DR PDB; 3KBJ; X-ray; 2.00 A; A=1-388. DR PDB; 3KBM; X-ray; 2.00 A; A=1-388. DR PDB; 3KBN; X-ray; 1.53 A; A=1-388. DR PDB; 3KBS; X-ray; 1.80 A; A=1-388. DR PDB; 3KBV; X-ray; 1.80 A; A=1-388. DR PDB; 3KBW; X-ray; 1.60 A; A=1-388. DR PDB; 3KCJ; Other; 1.80 A; A=1-388. DR PDB; 3KCL; Other; 2.00 A; A=1-388. DR PDB; 3KCO; Other; 1.80 A; A=1-388. DR PDB; 3N4A; X-ray; 1.94 A; A=2-388. DR PDB; 3QYS; X-ray; 1.85 A; A=1-388. DR PDB; 3QZA; Other; 2.00 A; A=1-388. DR PDB; 3U3H; X-ray; 0.97 A; A=1-388. DR PDB; 3XIS; X-ray; 1.60 A; A=2-388. DR PDB; 4A8I; X-ray; 0.95 A; A=1-388. DR PDB; 4A8L; X-ray; 1.35 A; A=1-388. DR PDB; 4A8N; X-ray; 1.20 A; A=1-388. DR PDB; 4A8R; X-ray; 1.42 A; A=1-388. DR PDB; 4DUO; X-ray; 2.00 A; A=1-388. DR PDB; 4DVO; Other; 2.00 A; A=1-388. DR PDB; 4E3V; X-ray; 1.50 A; A=1-388. DR PDB; 4J4K; X-ray; 1.90 A; A=1-388. DR PDB; 4LNC; Other; 2.19 A; A=1-388. DR PDB; 4QDP; Other; 2.00 A; A=1-388. DR PDB; 4QDW; Other; 1.80 A; A=1-388. DR PDB; 4QE1; X-ray; 1.55 A; A=1-388. DR PDB; 4QE4; X-ray; 1.70 A; A=1-388. DR PDB; 4QE5; X-ray; 1.56 A; A=1-388. DR PDB; 4QEE; X-ray; 1.60 A; A=1-388. DR PDB; 4QEH; X-ray; 1.55 A; A=1-388. DR PDB; 4US6; X-ray; 1.20 A; A/B=1-388. DR PDB; 4W4Q; X-ray; 2.00 A; A=1-388. DR PDB; 4XIS; X-ray; 1.60 A; A=2-388. DR PDB; 4ZB0; X-ray; 2.00 A; A/B=2-388. DR PDB; 4ZB2; X-ray; 2.00 A; A=1-388. DR PDB; 4ZB5; X-ray; 2.00 A; A=1-387. DR PDB; 4ZBC; X-ray; 2.00 A; A/B=1-387. DR PDB; 5AVH; X-ray; 0.90 A; A=2-387. DR PDB; 5AVN; X-ray; 1.03 A; A/B=2-388. DR PDB; 5I7G; X-ray; 1.21 A; A=1-388. DR PDB; 5VR0; X-ray; 1.70 A; A=1-388. DR PDB; 5Y4I; X-ray; 1.91 A; A=1-388. DR PDB; 5Y4J; X-ray; 1.40 A; A=3-386. DR PDB; 5ZYC; X-ray; 1.75 A; A=1-388. DR PDB; 5ZYD; X-ray; 1.40 A; A=1-388. DR PDB; 5ZYE; X-ray; 1.40 A; A=1-388. DR PDB; 6IRK; X-ray; 1.75 A; A=1-388. DR PDB; 6KCA; X-ray; 1.90 A; A=1-388. DR PDB; 6KCC; X-ray; 2.00 A; A=1-388. DR PDB; 6KD2; X-ray; 1.70 A; A=1-388. DR PDB; 6LL2; X-ray; 1.75 A; A=1-388. DR PDB; 6OQZ; X-ray; 1.60 A; A=2-387. DR PDB; 6QNC; X-ray; 1.90 A; A=1-388. DR PDB; 6QND; X-ray; 2.00 A; A=1-388. DR PDB; 6QNH; X-ray; 1.85 A; A=1-388. DR PDB; 6QNI; X-ray; 1.85 A; A=1-388. DR PDB; 6QNJ; X-ray; 1.85 A; A=1-388. DR PDB; 6QRR; X-ray; 1.10 A; A=1-388. DR PDB; 6QRS; X-ray; 1.17 A; A=1-388. DR PDB; 6QRT; X-ray; 1.17 A; A=1-388. DR PDB; 6QRU; X-ray; 1.17 A; A=1-388. DR PDB; 6QRV; X-ray; 1.17 A; A=1-388. DR PDB; 6QRW; X-ray; 1.17 A; A=1-388. DR PDB; 6QRX; X-ray; 1.17 A; A=1-388. DR PDB; 6QRY; X-ray; 1.17 A; A=1-388. DR PDB; 6QUF; X-ray; 1.19 A; A=1-388. DR PDB; 6QUK; X-ray; 1.58 A; A/B=1-388. DR PDB; 6RND; X-ray; 1.70 A; A=1-388. DR PDB; 6RNF; X-ray; 1.70 A; A=1-388. DR PDB; 6VRS; EM; 2.70 A; A/B/C/D=1-388. DR PDB; 6YBO; X-ray; 1.06 A; A=1-388. DR PDB; 6YBR; X-ray; 1.20 A; A=1-388. DR PDB; 7BJZ; X-ray; 2.13 A; A/B=1-388. DR PDB; 7BVL; X-ray; 2.00 A; A=1-388. DR PDB; 7BVN; X-ray; 2.00 A; A=1-388. DR PDB; 7CJO; X-ray; 1.40 A; A/B=1-388. DR PDB; 7CJP; X-ray; 1.50 A; A/B=1-388. DR PDB; 7CK0; X-ray; 1.80 A; A=1-388. DR PDB; 7CVK; X-ray; 1.70 A; A=1-388. DR PDB; 7CVM; X-ray; 2.00 A; A=1-388. DR PDB; 7DFJ; X-ray; 1.50 A; A=1-388. DR PDB; 7DFK; X-ray; 1.40 A; A=1-388. DR PDB; 7DMM; X-ray; 0.99 A; A=2-387. DR PDB; 7E03; X-ray; 1.60 A; A=1-388. DR PDB; 7NJG; X-ray; 1.90 A; A=1-388. DR PDB; 8AW8; X-ray; 1.63 A; A/B=1-388. DR PDB; 8AW9; X-ray; 1.62 A; A/B=1-388. DR PDB; 8AWB; X-ray; 2.30 A; A=1-388. DR PDB; 8AWC; X-ray; 1.75 A; A=1-388. DR PDB; 8AWD; X-ray; 1.85 A; A=1-388. DR PDB; 8AWE; X-ray; 1.70 A; A=1-388. DR PDB; 8AWF; X-ray; 1.61 A; A/B=1-388. DR PDB; 8AWS; X-ray; 2.26 A; A=1-388. DR PDB; 8AWU; X-ray; 1.47 A; A=1-388. DR PDB; 8AWV; X-ray; 2.08 A; A=1-388. DR PDB; 8AWX; X-ray; 1.96 A; A=1-388. DR PDB; 8AWY; X-ray; 1.60 A; A=1-388. DR PDB; 8WDG; X-ray; 0.99 A; A=3-387. DR PDB; 8WDH; X-ray; 1.70 A; A=3-387. DR PDB; 8XIA; X-ray; 1.90 A; A=1-388. DR PDB; 9XIA; X-ray; 1.90 A; A=1-388. DR PDBsum; 1GW9; -. DR PDBsum; 1MNZ; -. DR PDBsum; 1O1H; -. DR PDBsum; 1OAD; -. DR PDBsum; 1XIB; -. DR PDBsum; 1XIC; -. DR PDBsum; 1XID; -. DR PDBsum; 1XIE; -. DR PDBsum; 1XIF; -. DR PDBsum; 1XIG; -. DR PDBsum; 1XIH; -. DR PDBsum; 1XII; -. DR PDBsum; 1XIJ; -. DR PDBsum; 1XIS; -. DR PDBsum; 2G4J; -. DR PDBsum; 2GLK; -. DR PDBsum; 2GUB; -. DR PDBsum; 2GVE; -. DR PDBsum; 2XIS; -. DR PDBsum; 3CWH; -. DR PDBsum; 3GNX; -. DR PDBsum; 3KBJ; -. DR PDBsum; 3KBM; -. DR PDBsum; 3KBN; -. DR PDBsum; 3KBS; -. DR PDBsum; 3KBV; -. DR PDBsum; 3KBW; -. DR PDBsum; 3KCJ; -. DR PDBsum; 3KCL; -. DR PDBsum; 3KCO; -. DR PDBsum; 3N4A; -. DR PDBsum; 3QYS; -. DR PDBsum; 3QZA; -. DR PDBsum; 3U3H; -. DR PDBsum; 3XIS; -. DR PDBsum; 4A8I; -. DR PDBsum; 4A8L; -. DR PDBsum; 4A8N; -. DR PDBsum; 4A8R; -. DR PDBsum; 4DUO; -. DR PDBsum; 4DVO; -. DR PDBsum; 4E3V; -. DR PDBsum; 4J4K; -. DR PDBsum; 4LNC; -. DR PDBsum; 4QDP; -. DR PDBsum; 4QDW; -. DR PDBsum; 4QE1; -. DR PDBsum; 4QE4; -. DR PDBsum; 4QE5; -. DR PDBsum; 4QEE; -. DR PDBsum; 4QEH; -. DR PDBsum; 4US6; -. DR PDBsum; 4W4Q; -. DR PDBsum; 4XIS; -. DR PDBsum; 4ZB0; -. DR PDBsum; 4ZB2; -. DR PDBsum; 4ZB5; -. DR PDBsum; 4ZBC; -. DR PDBsum; 5AVH; -. DR PDBsum; 5AVN; -. DR PDBsum; 5I7G; -. DR PDBsum; 5VR0; -. DR PDBsum; 5Y4I; -. DR PDBsum; 5Y4J; -. DR PDBsum; 5ZYC; -. DR PDBsum; 5ZYD; -. DR PDBsum; 5ZYE; -. DR PDBsum; 6IRK; -. DR PDBsum; 6KCA; -. DR PDBsum; 6KCC; -. DR PDBsum; 6KD2; -. DR PDBsum; 6LL2; -. DR PDBsum; 6OQZ; -. DR PDBsum; 6QNC; -. DR PDBsum; 6QND; -. DR PDBsum; 6QNH; -. DR PDBsum; 6QNI; -. DR PDBsum; 6QNJ; -. DR PDBsum; 6QRR; -. DR PDBsum; 6QRS; -. DR PDBsum; 6QRT; -. DR PDBsum; 6QRU; -. DR PDBsum; 6QRV; -. DR PDBsum; 6QRW; -. DR PDBsum; 6QRX; -. DR PDBsum; 6QRY; -. DR PDBsum; 6QUF; -. DR PDBsum; 6QUK; -. DR PDBsum; 6RND; -. DR PDBsum; 6RNF; -. DR PDBsum; 6VRS; -. DR PDBsum; 6YBO; -. DR PDBsum; 6YBR; -. DR PDBsum; 7BJZ; -. DR PDBsum; 7BVL; -. DR PDBsum; 7BVN; -. DR PDBsum; 7CJO; -. DR PDBsum; 7CJP; -. DR PDBsum; 7CK0; -. DR PDBsum; 7CVK; -. DR PDBsum; 7CVM; -. DR PDBsum; 7DFJ; -. DR PDBsum; 7DFK; -. DR PDBsum; 7DMM; -. DR PDBsum; 7E03; -. DR PDBsum; 7NJG; -. DR PDBsum; 8AW8; -. DR PDBsum; 8AW9; -. DR PDBsum; 8AWB; -. DR PDBsum; 8AWC; -. DR PDBsum; 8AWD; -. DR PDBsum; 8AWE; -. DR PDBsum; 8AWF; -. DR PDBsum; 8AWS; -. DR PDBsum; 8AWU; -. DR PDBsum; 8AWV; -. DR PDBsum; 8AWX; -. DR PDBsum; 8AWY; -. DR PDBsum; 8WDG; -. DR PDBsum; 8WDH; -. DR PDBsum; 8XIA; -. DR PDBsum; 9XIA; -. DR AlphaFoldDB; P24300; -. DR EMDB; EMD-21371; -. DR SASBDB; P24300; -. DR SMR; P24300; -. DR DIP; DIP-58982N; -. DR DrugBank; DB03564; (4r)-2-Methylpentane-2,4-Diol. DR DrugBank; DB01881; 2-Methylpentane-1,2,4-Triol. DR DrugBank; DB00126; Ascorbic acid. DR DrugBank; DB02379; Beta-D-Glucose. DR DrugBank; DB03947; D-Xylulose. DR DrugBank; DB03911; L-Xylopyranose. DR DrugBank; DB11195; Xylitol. DR KEGG; ag:AAA26838; -. DR BRENDA; 5.3.1.5; 6089. DR EvolutionaryTrace; P24300; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009045; F:xylose isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1. DR HAMAP; MF_00455; Xylose_isom_A; 1. DR InterPro; IPR036237; Xyl_isomerase-like_sf. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR InterPro; IPR013453; XylA_actinobac. DR InterPro; IPR001998; Xylose_isomerase. DR NCBIfam; TIGR02631; xylA_Arthro; 1. DR PANTHER; PTHR12110; HYDROXYPYRUVATE ISOMERASE; 1. DR PANTHER; PTHR12110:SF59; XYLOSE ISOMERASE; 1. DR Pfam; PF01261; AP_endonuc_2; 1. DR PRINTS; PR00688; XYLOSISMRASE. DR SUPFAM; SSF51658; Xylose isomerase-like; 1. DR PROSITE; PS51415; XYLOSE_ISOMERASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium; KW Metal-binding; Xylose metabolism. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..388 FT /note="Xylose isomerase" FT /id="PRO_0000195805" FT ACT_SITE 54 FT ACT_SITE 57 FT /evidence="ECO:0000250" FT BINDING 181 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT BINDING 217 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT BINDING 217 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT BINDING 220 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT BINDING 245 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT BINDING 255 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT BINDING 257 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT BINDING 287 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT HELIX 7..9 FT /evidence="ECO:0007829|PDB:5AVH" FT STRAND 11..14 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 15..18 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 36..45 FT /evidence="ECO:0007829|PDB:5AVH" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 55..58 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 65..82 FT /evidence="ECO:0007829|PDB:5AVH" FT STRAND 85..90 FT /evidence="ECO:0007829|PDB:5AVH" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:5AVH" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:3CWH" FT HELIX 109..128 FT /evidence="ECO:0007829|PDB:5AVH" FT STRAND 132..136 FT /evidence="ECO:0007829|PDB:5AVH" FT STRAND 142..146 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 151..172 FT /evidence="ECO:0007829|PDB:5AVH" FT STRAND 177..180 FT /evidence="ECO:0007829|PDB:5AVH" FT STRAND 184..193 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 196..203 FT /evidence="ECO:0007829|PDB:5AVH" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 209..211 FT /evidence="ECO:0007829|PDB:5AVH" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 218..222 FT /evidence="ECO:0007829|PDB:5AVH" FT TURN 223..225 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 228..237 FT /evidence="ECO:0007829|PDB:5AVH" FT STRAND 244..246 FT /evidence="ECO:0007829|PDB:4J4K" FT STRAND 251..254 FT /evidence="ECO:0007829|PDB:5AVH" FT STRAND 262..264 FT /evidence="ECO:0007829|PDB:4ZBC" FT HELIX 265..277 FT /evidence="ECO:0007829|PDB:5AVH" FT STRAND 284..286 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 296..322 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 324..332 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 335..338 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 347..352 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 354..356 FT /evidence="ECO:0007829|PDB:5AVH" FT TURN 357..359 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 362..367 FT /evidence="ECO:0007829|PDB:5AVH" FT HELIX 372..384 FT /evidence="ECO:0007829|PDB:5AVH" SQ SEQUENCE 388 AA; 43227 MW; 4C675184B62C97FB CRC64; MNYQPTPEDR FTFGLWTVGW QGRDPFGDAT RRALDPVESV RRLAELGAHG VTFHDDDLIP FGSSDSEREE HVKRFRQALD DTGMKVPMAT TNLFTHPVFK DGGFTANDRD VRRYALRKTI RNIDLAVELG AETYVAWGGR EGAESGGAKD VRDALDRMKE AFDLLGEYVT SQGYDIRFAI EPKPNEPRGD ILLPTVGHAL AFIERLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK LFHIDLNGQN GIKYDQDLRF GAGDLRAAFW LVDLLESAGY SGPRHFDFKP PRTEDFDGVW ASAAGCMRNY LILKERAAAF RADPEVQEAL RASRLDELAR PTAADGLQAL LDDRSAFEEF DVDAAAARGM AFERLDQLAM DHLLGARG //