XYLA_ARTS7
ID XYLA_ARTS7 Reviewed; 395 AA.
AC P12070;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA;
OS Arthrobacter sp. (strain NRRL B3728).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=1669;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1854339; DOI=10.1042/bj2770263;
RA Loviny-Anderton T., Shaw P.C., Shin M.K., Hartley B.S.;
RT "D-xylose (D-glucose) isomerase from Arthrobacter strain N.R.R.L. B3728.
RT Gene cloning, sequence and expression.";
RL Biochem. J. 277:263-271(1991).
RN [2]
RP PROTEIN SEQUENCE OF 2-21, AND CHARACTERIZATION.
RX PubMed=1854338; DOI=10.1042/bj2770255;
RA Smith C.A., Rangarajan M., Hartley B.S.;
RT "D-xylose (D-glucose) isomerase from Arthrobacter strain N.R.R.L. B3728.
RT Purification and properties.";
RL Biochem. J. 277:255-261(1991).
RN [3]
RP ACTIVE SITES HIS-54 AND ASP-57.
RX PubMed=2319597; DOI=10.1016/0022-2836(90)90316-e;
RA Collyer C.A., Henrick K., Blow D.M.;
RT "Mechanism for aldose-ketose interconversion by D-xylose isomerase
RT involving ring opening followed by a 1,2-hydride shift.";
RL J. Mol. Biol. 212:211-235(1990).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=2769749; DOI=10.1016/0022-2836(89)90092-2;
RA Henrick K., Collyer C.A., Blow D.M.;
RT "Structures of D-xylose isomerase from Arthrobacter strain B3728 containing
RT the inhibitors xylitol and D-sorbitol at 2.5-A and 2.3-A resolution,
RT respectively.";
RL J. Mol. Biol. 208:129-157(1989).
RN [5]
RP COMPARISON OF X-RAY STRUCTURES.
RX PubMed=3508294; DOI=10.1093/protein/1.6.467;
RA Henrick K., Blow D.M., Carell H.L., Glusker J.P.;
RT "Comparison of backbone structures of glucose isomerase from Streptomyces
RT and Arthrobacter.";
RL Protein Eng. 1:467-469(1987).
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;
CC Note=Binds 2 magnesium 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; X59466; CAA42073.1; -; Genomic_DNA.
DR PIR; S16214; S16214.
DR PDB; 1DID; X-ray; 2.50 A; A/B=2-395.
DR PDB; 1DIE; X-ray; 2.50 A; A/B=2-395.
DR PDB; 1XLA; X-ray; 2.30 A; A/B=2-395.
DR PDB; 1XLB; X-ray; 2.50 A; A/B=2-395.
DR PDB; 1XLC; X-ray; 2.50 A; A/B=2-395.
DR PDB; 1XLD; X-ray; 2.50 A; A/B=2-395.
DR PDB; 1XLE; X-ray; 2.50 A; A/B=2-395.
DR PDB; 1XLF; X-ray; 2.50 A; A/B=2-395.
DR PDB; 1XLG; X-ray; 2.50 A; A/B=2-395.
DR PDB; 1XLH; X-ray; 2.50 A; A/B=2-395.
DR PDB; 1XLI; X-ray; 2.50 A; A/B=2-395.
DR PDB; 1XLJ; X-ray; 2.50 A; A/B=2-395.
DR PDB; 1XLK; X-ray; 2.50 A; A/B=2-395.
DR PDB; 1XLL; X-ray; 2.50 A; A/B=2-395.
DR PDB; 1XLM; X-ray; 2.40 A; A/B=2-395.
DR PDB; 4XIA; X-ray; 2.30 A; A/B=3-395.
DR PDB; 5XIA; X-ray; 2.50 A; A/B=3-395.
DR PDBsum; 1DID; -.
DR PDBsum; 1DIE; -.
DR PDBsum; 1XLA; -.
DR PDBsum; 1XLB; -.
DR PDBsum; 1XLC; -.
DR PDBsum; 1XLD; -.
DR PDBsum; 1XLE; -.
DR PDBsum; 1XLF; -.
DR PDBsum; 1XLG; -.
DR PDBsum; 1XLH; -.
DR PDBsum; 1XLI; -.
DR PDBsum; 1XLJ; -.
DR PDBsum; 1XLK; -.
DR PDBsum; 1XLL; -.
DR PDBsum; 1XLM; -.
DR PDBsum; 4XIA; -.
DR PDBsum; 5XIA; -.
DR AlphaFoldDB; P12070; -.
DR SMR; P12070; -.
DR DrugBank; DB02172; 2,5-Dideoxy-2,5-Imino-D-Glucitol.
DR DrugBank; DB03206; Duvoglustat.
DR DrugBank; DB11195; Xylitol.
DR SABIO-RK; P12070; -.
DR EvolutionaryTrace; P12070; -.
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; Cytoplasm;
KW Direct protein sequencing; Isomerase; Magnesium; Metal-binding;
KW Xylose metabolism.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1854338"
FT CHAIN 2..395
FT /note="Xylose isomerase"
FT /id="PRO_0000195760"
FT ACT_SITE 54
FT /evidence="ECO:0000269|PubMed:2319597"
FT ACT_SITE 57
FT /evidence="ECO:0000269|PubMed:2319597"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:1XLA"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:1XLA"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:1XLA"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1XLA"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 109..128
FT /evidence="ECO:0007829|PDB:1XLA"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1XLA"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 151..172
FT /evidence="ECO:0007829|PDB:1XLA"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:1XLA"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1XLA"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:1XLA"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 228..237
FT /evidence="ECO:0007829|PDB:1XLA"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:1XLA"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 302..328
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 330..338
FT /evidence="ECO:0007829|PDB:1XLA"
FT TURN 339..342
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 355..360
FT /evidence="ECO:0007829|PDB:1XLA"
FT TURN 362..367
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 370..373
FT /evidence="ECO:0007829|PDB:1XLA"
FT HELIX 380..391
FT /evidence="ECO:0007829|PDB:1XLA"
SQ SEQUENCE 395 AA; 43292 MW; EA7A21FC47726369 CRC64;
MSVQPTPADH FTFGLWTVGW TGADPFGVAT RKNLDPVEAV HKLAELGAYG ITFHDNDLIP
FDATEAEREK ILGDFNQALK DTGLKVPMVT TNLFSHPVFK DGGFTSNDRS IRRFALAKVL
HNIDLAAEMG AETFVMWGGR EGSEYDGSKD LAAALDRMRE GVDTAAGYIK DKGYNLRIAL
EPKPNEPRGD IFLPTVGHGL AFIEQLEHGD IVGLNPETGH EQMAGLNFTH GIAQALWAEK
LFHIDLNGQR GIKYDQDLVF GHGDLTSAFF TVDLLENGFP NGGPKYTGPR HFDYKPSRTD
GYDGVWDSAK ANMSMYLLLK ERALAFRADP EVQEAMKTSG VFELGETTLN AGESAADLMN
DSASFAGFDA EAAAERNFAF IRLNQLAIEH LLGSR
