ID   XYLA_STRRO              Reviewed;         394 AA.
AC   P22857;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Xylose isomerase;
DE            EC=5.3.1.5;
GN   Name=xylA;
OS   Streptomyces rochei (Streptomyces parvullus).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces rochei group.
OX   NCBI_TaxID=1928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S-41;
RX   PubMed=1368583; DOI=10.1271/bbb1961.54.2469;
RA   Kikuchi T., Itoh Y., Kasumi T., Fukazawa C.;
RT   "Molecular cloning of the xylA gene encoding xylose isomerase from
RT   Streptomyces griseofuscus S-41: primary structure of the gene and its
RT   product.";
RL   Agric. Biol. Chem. 54:2469-2472(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; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
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DR   PIR; JN0086; ISSMXR.
DR   AlphaFoldDB; P22857; -.
DR   SMR; P22857; -.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium; Metal-binding;
KW   Xylose metabolism.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..394
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000195804"
FT   REGION          370..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        57
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   394 AA;  43644 MW;  EDF080CF957AAFCE CRC64;
     MSFQPTPEDK FTFGLWTVGW QGRDPFGDAT RPGLDPVETV QRLAELGAYG VTFHDDDLNP
     FGSSDTERES HIKRFRQALD ATGMTVPMAT TNLFTHPVFK DRFTANDRDV RAYAVRKTIR
     NIDLAAELGA KTYVAWGGRE GAESGGAKDV RDALDRMKEA FDLLGEYVTA QGYDLRFAIE
     PKPNEPRGDI LLPTVGHALA FIERLERPEL YGVNPEVGHE QMAGLNFPHG IAQALWAGKL
     FHIDLNGQSG IKYDQDCGSR RRPAGGVLVV DLLESAGYEG PRHFDFKPPR TEDFDGVWAS
     AEGCMRNYLI LKQPRPPSAP TRRCRRRASA PRVWTSWPSR PLADGLEALL ADRTAFEDFD
     VEAAAARGMV RTPRPAGDGP PAGRARLTVA PRKR