XYLA_STRRU
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 03-AUG-2022, entry version 152.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA;
OS Streptomyces rubiginosus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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}.
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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; 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; 8XIA; -.
DR PDBsum; 9XIA; -.
DR AlphaFoldDB; P24300; -.
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 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 Pfam; PF01261; AP_endonuc_2; 1.
DR PRINTS; PR00688; XYLOSISMRASE.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR02631; xylA_Arthro; 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
