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Database: UniProt
Entry: P19148
LinkDB: P19148
Original site: P19148 
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   11-DEC-2019, entry version 111.
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;
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=D-xylose = D-xylulose; Xref=Rhea:RHEA:22816,
CC         ChEBI:CHEBI:17140, ChEBI:CHEBI:53455; 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}.
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   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   METAL           232
FT                   /note="Cobalt 1"
FT   METAL           268
FT                   /note="Cobalt 1"
FT   METAL           268
FT                   /note="Cobalt 2"
FT   METAL           271
FT                   /note="Cobalt 2"
FT   METAL           296
FT                   /note="Cobalt 1"
FT   METAL           307
FT                   /note="Cobalt 2"
FT   METAL           309
FT                   /note="Cobalt 2"
FT   METAL           339
FT                   /note="Cobalt 1"
FT   MUTAGEN         101
FT                   /note="H->F: Abolishes activity."
FT   STRAND          21..26
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           38..42
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   STRAND          44..47
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           48..52
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           68..71
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           75..93
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   STRAND          96..101
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           102..105
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           112..130
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   STRAND          136..141
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   STRAND          145..147
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           148..150
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           160..179
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   STRAND          183..187
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   STRAND          192..195
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           197..199
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           202..222
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   STRAND          227..231
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   STRAND          237..244
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           247..256
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   TURN            260..262
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   STRAND          263..268
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           269..274
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           279..288
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   STRAND          292..296
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   STRAND          304..306
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           315..327
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   STRAND          336..338
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           350..375
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           378..386
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           388..390
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           393..399
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           405..414
FT                   /evidence="ECO:0000244|PDB:1A0C"
FT   HELIX           425..436
FT                   /evidence="ECO:0000244|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
//
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