ID   XYLA_STRVO              Reviewed;         389 AA.
AC   P09033;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Xylose isomerase;
DE            EC=5.3.1.5;
GN   Name=xylA;
OS   Streptomyces violaceusniger.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=68280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RC   STRAIN=CBS 409-73;
RX   PubMed=3174453; DOI=10.1093/nar/16.19.9337;
RA   Drocourt D., Bejar S., Calmels T., Reynes J.-P., Tiraby G.;
RT   "Nucleotide sequence of the xylose isomerase gene from Streptomyces
RT   violaceoniger.";
RL   Nucleic Acids Res. 16:9337-9337(1988).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
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DR   EMBL; X12816; CAA31304.1; -; Genomic_DNA.
DR   EMBL; M36269; AAA26839.1; -; Genomic_DNA.
DR   PIR; S01436; ISSMXV.
DR   AlphaFoldDB; P09033; -.
DR   SMR; P09033; -.
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   Carbohydrate metabolism; Cytoplasm; Direct protein sequencing; Isomerase;
KW   Magnesium; Metal-binding; Xylose metabolism.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3174453"
FT   CHAIN           2..389
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000195808"
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                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   389 AA;  43144 MW;  7BCE4CE55BEE11B2 CRC64;
     MSFQPTPEDK FTFGLWTVGW QGRDPFGDAT RPALDPVETV QRLAELGAYG VTFHDDDLIP
     FGSSDTERES HIKRFRQALD ATGMTVPMAT TNLFTHPVFK DGGFTANDRD VRRYALRKTI
     RNIDLAAELG AKTYVAWGGR EGAESGGAKD VRDALDRMKE AFDLLGEYVT AQGYDLRFAI
     EPKPNEPRGD ILLPTVGHAL AFIERLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK
     LFHIDLNGQS GIKYDQDLRF GAGDLRAAFW LVDLLESAGY EGPRHFDFKP PRTEDFDGVW
     ASAEGCMRNY LILKERAAAF RADPEVQEAL RAARLDQLAQ PTAADGLEAL LADRTAFEDF
     DVEAAAARAA WPFERLDQLA MDHLLGARG