XYLA_STRMR
ID XYLA_STRMR Reviewed; 388 AA.
AC P37031;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA;
OS Streptomyces murinus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=33900;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Luiten R.G.M., Quax W.J., Schuurhuizen P.W., Mrabet N.;
RT "Novel glucose isomerase enzymes and their use.";
RL Patent number EP0351029, 17-JAN-1990.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=15299450; DOI=10.1107/s0907444993009540;
RA Rasmussen H., la Cour T., Nyborg J., Schuelein M.;
RT "Structure determination of glucose isomerase from Streptomyces murinus at
RT 2.6-A resolution.";
RL Acta Crystallogr. D 50:124-131(1994).
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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
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DR EMBL; A10243; CAA00885.1; -; Unassigned_DNA.
DR PDB; 1DXI; X-ray; 2.60 A; A/B=1-388.
DR PDBsum; 1DXI; -.
DR AlphaFoldDB; P37031; -.
DR SMR; P37031; -.
DR EvolutionaryTrace; P37031; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 CHAIN 1..388
FT /note="Xylose isomerase"
FT /id="PRO_0000195801"
FT ACT_SITE 54
FT /evidence="ECO:0000250"
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 STRAND 11..14
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:1DXI"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:1DXI"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:1DXI"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1DXI"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 109..127
FT /evidence="ECO:0007829|PDB:1DXI"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:1DXI"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1DXI"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 151..171
FT /evidence="ECO:0007829|PDB:1DXI"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1DXI"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:1DXI"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:1DXI"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:1DXI"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:1DXI"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1DXI"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:1DXI"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:1DXI"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 296..320
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:1DXI"
FT TURN 354..359
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 362..366
FT /evidence="ECO:0007829|PDB:1DXI"
FT HELIX 372..378
FT /evidence="ECO:0007829|PDB:1DXI"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:1DXI"
SQ SEQUENCE 388 AA; 42772 MW; C995067BF6582A8F CRC64;
MSFQPTPEDR FTFGLWTVGW QGRDPFGDAT RPALDPVETV QRLAELGAYG VTFHDDDLIP
FGSSDTERES HIKRFRQALD ATGMTVPMAT TNLFTHPVFK DGGFTANDRD VRRYALRKTI
GNIDLAAELG AKTYVAWGGR EGAESGGAKD VRDALDRMKE AFDLLGEYVT AQGYDLRFAI
EPKPNEPRGD ILLPTVGHAL AFIERLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK
LFHIDLNGQS GIKYDQDLRF GAGDLRAAFW LVDLLETAGY EGPRHFDFKP PRTEDFDGVW
ASAAGCMRNY LILKDRAAAF RADPEVQEAL RAARLDQLAQ PTAADGLDAL LADRAAFEDF
DVDAAAARGM AFEHLDQLAM DHLLGARG
