XYLA_GEOSE
ID XYLA_GEOSE Reviewed; 441 AA.
AC P54273;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCIMB 12403 / LLD-R;
RA Jackson R., Brannigan J., Taylor M.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND SEQUENCE REVISION TO 248.
RC STRAIN=NCIMB 12403 / LLD-R;
RA Gallay O., Chopra R., Conti E., Brick P., Jackson R., Hartley B.,
RA Vieille C., Zeikus J.G., Blow D.;
RT "Crystal structures of class II xylose isomerases from two thermophiles and
RT a hyperthermophile.";
RL Submitted (NOV-1997) to the PDB data bank.
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Binds 2 manganese 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 EMBL; X98088; CAA66715.1; -; Genomic_DNA.
DR PDB; 1A0D; X-ray; 3.00 A; A/B/C/D=2-441.
DR PDBsum; 1A0D; -.
DR AlphaFoldDB; P54273; -.
DR SMR; P54273; -.
DR EvolutionaryTrace; P54273; -.
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; IPR013452; Xylose_isom_bac.
DR InterPro; IPR001998; Xylose_isomerase.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR PRINTS; PR00688; XYLOSISMRASE.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR02630; xylose_isom_A; 1.
DR PROSITE; PS51415; XYLOSE_ISOMERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase; Manganese;
KW Metal-binding; Xylose metabolism.
FT CHAIN 1..441
FT /note="Xylose isomerase"
FT /id="PRO_0000195766"
FT ACT_SITE 99
FT ACT_SITE 102
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT BINDING 266
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT BINDING 266
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 294
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT BINDING 305
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 307
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT BINDING 337
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT CONFLICT 248
FT /note="A -> R (in Ref. 1; CAA66715)"
FT /evidence="ECO:0000305"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:1A0D"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 73..91
FT /evidence="ECO:0007829|PDB:1A0D"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 110..128
FT /evidence="ECO:0007829|PDB:1A0D"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1A0D"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 158..178
FT /evidence="ECO:0007829|PDB:1A0D"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1A0D"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 200..220
FT /evidence="ECO:0007829|PDB:1A0D"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1A0D"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:1A0D"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 277..286
FT /evidence="ECO:0007829|PDB:1A0D"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:1A0D"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 313..325
FT /evidence="ECO:0007829|PDB:1A0D"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 348..373
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 376..384
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 391..398
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 403..411
FT /evidence="ECO:0007829|PDB:1A0D"
FT HELIX 423..435
FT /evidence="ECO:0007829|PDB:1A0D"
SQ SEQUENCE 441 AA; 50142 MW; 78BB39852919D017 CRC64;
MPYFDNISTI AYEGPASKNP LAFKFYNPEE KVGDKTMEEH LRFSVAYWHT FTGDGSDPFG
AGNMIRPWNK YSGMDLAKAR VEAAFEFFEK LNIPFFCFHD VDIAPEGETL KETYKNLDII
VDMIEEYMKT SKTKLLWNTA NLFTHPRFVH GAATSCNADV FAYAAAKVKK GLEIAKRLGA
ENYVFWGGRE GYETLLNTDM KLELDNLARF LHMAVDYAKE IGFDGQFLIE PKPKEPTKHQ
YDFDVATALA FLQTYGLKDY FKFNIEANHA TLAGHTFEHE LRVARIHGML GSVDANQGDM
LLGWDTDEFP TDLYSTTLAM YEILKNGGLG RGGLNFDAKV RRGSFEPEDL FYAHIAGMDS
FAVGLKVAHR LIEDRVFDEF IEERYKSYTE GIGREIVEGT ADFHKLEAHA LQLGEIQNQS
GRQERLKTLL NQYLLEVCAA R
