XYLA_STRAL
ID XYLA_STRAL Reviewed; 391 AA.
AC P24299;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA;
OS Streptomyces albus G.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1962;
RN [1]
RP CRYSTALLIZATION.
RX PubMed=2651156; DOI=10.1016/0014-5793(89)81227-x;
RA Dauter Z., Dauter M., Hemker J., Witzel H., Wilson K.S.;
RT "Crystallisation and preliminary analysis of glucose isomerase from
RT Streptomyces albus.";
RL FEBS Lett. 247:1-8(1989).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=2085424; DOI=10.1107/s0108768190008059;
RA Dauter Z., Terry H., Witzel H., Wilson K.S.;
RT "Refinement of glucose isomerase from Streptomyces albus at 1.65 A with
RT data from an imaging plate.";
RL Acta Crystallogr. B 46:833-845(1990).
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;
CC Note=Binds 2 magnesium ions per subunit.;
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
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DR PDB; 6XIA; X-ray; 1.65 A; A=2-388.
DR PDBsum; 6XIA; -.
DR AlphaFoldDB; P24299; -.
DR SMR; P24299; -.
DR EvolutionaryTrace; P24299; -.
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 INIT_MET 1
FT /note="Removed"
FT CHAIN 2..391
FT /note="Xylose isomerase"
FT /id="PRO_0000195795"
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 HELIX 7..9
FT /evidence="ECO:0007829|PDB:6XIA"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:6XIA"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:6XIA"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6XIA"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 109..128
FT /evidence="ECO:0007829|PDB:6XIA"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:6XIA"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 151..172
FT /evidence="ECO:0007829|PDB:6XIA"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:6XIA"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:6XIA"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6XIA"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:6XIA"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:6XIA"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:6XIA"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 296..322
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 347..352
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:6XIA"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 362..367
FT /evidence="ECO:0007829|PDB:6XIA"
FT HELIX 372..384
FT /evidence="ECO:0007829|PDB:6XIA"
SQ SEQUENCE 391 AA; 43421 MW; 405A909694713812 CRC64;
MNYQPTPEDR FTFGLWTVGW EGRDPFGDAT RTALDPVESV RRLAELGAHG VTFHDDDLIP
FGSSDSERYE 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 DHLLGARGAA A
