XYLA_THETU
ID XYLA_THETU Reviewed; 439 AA.
AC P19148;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA;
OS Thermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Thermoanaerobacterium.
OX NCBI_TaxID=33950;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33743 / DSM 2229 / 4B;
RX PubMed=2229064; DOI=10.1016/s0021-9258(17)30628-2;
RA Lee C.Y., Bagdasarian M., Meng M.H., Zeikus J.G.;
RT "Catalytic mechanism of xylose (glucose) isomerase from Clostridium
RT thermosulfurogenes. Characterization of the structural gene and function of
RT active site histidine.";
RL J. Biol. Chem. 265:19082-19090(1990).
RN [2]
RP PROTEIN SEQUENCE OF 1-7.
RX PubMed=1996956; DOI=10.1042/bj2730565;
RA Lee C.Y., Zeikus J.G.;
RT "Purification and characterization of thermostable glucose isomerase from
RT Clostridium thermosulfurogenes and Thermoanaerobacter strain B6A.";
RL Biochem. J. 273:565-571(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC STRAIN=ATCC 33743 / DSM 2229 / 4B;
RA Gallay O., Chopra R., Conti E., Brick P., Jackson R., Hartley B.,
RA Vieille C., Zeikus J.G., Blow D.;
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=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Note=Binds 2 cobalt 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; J05650; AAA23285.1; -; Genomic_DNA.
DR PIR; A36598; ISCLXM.
DR PDB; 1A0C; X-ray; 2.50 A; A/B/C/D=2-439.
DR PDBsum; 1A0C; -.
DR AlphaFoldDB; P19148; -.
DR SMR; P19148; -.
DR SABIO-RK; P19148; -.
DR EvolutionaryTrace; P19148; -.
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; Cobalt; Cytoplasm;
KW Direct protein sequencing; Isomerase; Metal-binding; Xylose metabolism.
FT CHAIN 1..439
FT /note="Xylose isomerase"
FT /id="PRO_0000195817"
FT ACT_SITE 101
FT ACT_SITE 104
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT BINDING 268
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT BINDING 268
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT BINDING 271
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT BINDING 296
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT BINDING 307
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT BINDING 309
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT BINDING 339
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT MUTAGEN 101
FT /note="H->F: Abolishes activity."
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:1A0C"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 75..93
FT /evidence="ECO:0007829|PDB:1A0C"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 112..130
FT /evidence="ECO:0007829|PDB:1A0C"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:1A0C"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 160..179
FT /evidence="ECO:0007829|PDB:1A0C"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:1A0C"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 202..222
FT /evidence="ECO:0007829|PDB:1A0C"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:1A0C"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:1A0C"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:1A0C"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 269..274
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:1A0C"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:1A0C"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 315..327
FT /evidence="ECO:0007829|PDB:1A0C"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 350..375
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 393..399
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 405..414
FT /evidence="ECO:0007829|PDB:1A0C"
FT HELIX 425..436
FT /evidence="ECO:0007829|PDB:1A0C"
SQ SEQUENCE 439 AA; 50475 MW; 55A227DBDD0EECB9 CRC64;
MNKYFENVSK IKYEGPKSNN PYSFKFYNPE EVIDGKTMEE HLRFSIAYWH TFTADGTDQF
GKATMQRPWN HYTDPMDIAK ARVEAAFEFF DKINAPYFCF HDRDIAPEGD TLRETNKNLD
TIVAMIKDYL KTSKTKVLWG TANLFSNPRF VHGASTSCNA DVFAYSAAQV KKALEITKEL
GGENYVFWGG REGYETLLNT DMEFELDNFA RFLHMAVDYA KEIGFEGQFL IEPKPKEPTK
HQYDFDVANV LAFLRKYDLD KYFKVNIEAN HATLAFHDFQ HELRYARING VLGSIDANTG
DMLLGWDTDQ FPTDIRMTTL AMYEVIKMGG FDKGGLNFDA KVRRASFEPE DLFLGHIAGM
DAFAKGFKVA YKLVKDRVFD KFIEERYASY KDGIGADIVS GKADFRSLEK YALERSQIVN
KSGRQELLES ILNQYLFAE
