XYLA_STRDI
ID XYLA_STRDI Reviewed; 388 AA.
AC P50910;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA;
OS Streptomyces diastaticus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces diastaticus group.
OX NCBI_TaxID=1956;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=No. 7 / M1033;
RX PubMed=7803695;
RA Wang Y., Huang Z., Dai X., Liu J., Cui T., Niu L., Wang C., Xu X.;
RT "The sequence of xylose isomerase gene from Streptomyces diastaticus No. 7
RT M1033.";
RL Chin. J. Biotechnol. 10:97-103(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RC STRAIN=No. 7 / M1033;
RX PubMed=10666592; DOI=10.1107/s0907444999015097;
RA Zhu X., Teng M., Niu L., Xu C., Wang Y.;
RT "Structure of xylose isomerase from Streptomyces diastaticus no. 7 strain
RT M1033 at 1.85 A resolution.";
RL Acta Crystallogr. D 56:129-136(2000).
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=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; S73809; AAB32873.1; -; Genomic_DNA.
DR PIR; JC1031; JC1031.
DR PDB; 1CLK; X-ray; 1.90 A; A=2-388.
DR PDB; 1QT1; X-ray; 1.85 A; A/B=2-388.
DR PDBsum; 1CLK; -.
DR PDBsum; 1QT1; -.
DR AlphaFoldDB; P50910; -.
DR SMR; P50910; -.
DR PRIDE; P50910; -.
DR EvolutionaryTrace; P50910; -.
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 3D-structure; Carbohydrate metabolism; Cobalt; Cytoplasm; Isomerase;
KW Metal-binding; Xylose metabolism.
FT CHAIN 1..388
FT /note="Xylose isomerase"
FT /id="PRO_0000195799"
FT ACT_SITE 54
FT /evidence="ECO:0000250"
FT ACT_SITE 57
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT BINDING 217
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT BINDING 217
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT BINDING 220
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT BINDING 245
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT BINDING 255
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT BINDING 257
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="2"
FT BINDING 287
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /ligand_label="1"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:1QT1"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:1QT1"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:1QT1"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1QT1"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 109..129
FT /evidence="ECO:0007829|PDB:1QT1"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1QT1"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 151..172
FT /evidence="ECO:0007829|PDB:1QT1"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:1QT1"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:1QT1"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1QT1"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:1QT1"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:1QT1"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:1QT1"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 265..278
FT /evidence="ECO:0007829|PDB:1QT1"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 296..322
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:1QT1"
FT TURN 342..345
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:1QT1"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 362..367
FT /evidence="ECO:0007829|PDB:1QT1"
FT HELIX 372..384
FT /evidence="ECO:0007829|PDB:1QT1"
SQ SEQUENCE 388 AA; 42676 MW; EFB9DA125AB1DEB0 CRC64;
MSYQPTPEDK FTFGLWTVGW QGRDPFGDAT RGALDPAESV RRLAELGAHG VTFHDDDLIP
FGATDSERAE HIKRFRQGLD ETGMKVPMAT TNLFTHPVFK DGGFTANDRD VRRYAVRKTI
RNIDLAVELG AQTYVAWGGR EGAESGAAKD VRVALDRMKE AFDLLGEYVT SQGYDTPFAI
EPKPNEPRGD ILLPTIGHAL AFIDGLERPE LYGVNPEVGH EQMAGLNFPH GIAQALWAGK
LFHIDLNGQS GIKYDQDLRF GPGDLAAAFW LVDLLESAGY EGPRHFDFKP PRTEDFDGVW
ASAAGCMRNY LILKERAAAF RADPEVQEAL RAARLDELAQ PTAGDGLQAL LPDRSAFEDF
DPDAAAARGM AFERLDQLAM DHLLGARG
