ID XYLA_RHIE6 Reviewed; 436 AA.
AC B3Q0R5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Xylose isomerase {ECO:0000255|HAMAP-Rule:MF_00455};
DE EC=5.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00455};
GN Name=xylA {ECO:0000255|HAMAP-Rule:MF_00455};
GN OrderedLocusNames=RHECIAT_CH0003919;
OS Rhizobium etli (strain CIAT 652).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652;
RX PubMed=20048063; DOI=10.1128/aem.02039-09;
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P., Fernandez J.L.,
RA Hernandez Gonzalez I.L., Diaz R., Flores M., Palacios R., Mora J.,
RA Davila G.;
RT "Conserved symbiotic plasmid DNA sequences in the multireplicon pangenomic
RT structure of Rhizobium etli.";
RL Appl. Environ. Microbiol. 76:1604-1614(2010).
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00455};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00455};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00455};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00455}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00455}.
CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000255|HAMAP-
CC Rule:MF_00455}.
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DR EMBL; CP001074; ACE92856.1; -; Genomic_DNA.
DR AlphaFoldDB; B3Q0R5; -.
DR SMR; B3Q0R5; -.
DR KEGG; rec:RHECIAT_CH0003919; -.
DR eggNOG; COG2115; Bacteria.
DR HOGENOM; CLU_037261_1_0_5; -.
DR Proteomes; UP000008817; Chromosome.
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 Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR HAMAP; MF_00455; Xylose_isom_A; 1.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013452; Xylose_isom_bac.
DR InterPro; IPR001998; Xylose_isomerase.
DR NCBIfam; TIGR02630; xylose_isom_A; 1.
DR PANTHER; PTHR48320; -; 1.
DR PANTHER; PTHR48320:SF1; XYLOSE ISOMERASE; 1.
DR PRINTS; PR00688; XYLOSISMRASE.
DR SUPFAM; SSF51658; Xylose isomerase-like; 1.
DR PROSITE; PS51415; XYLOSE_ISOMERASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium; Metal-binding;
KW Xylose metabolism.
FT CHAIN 1..436
FT /note="Xylose isomerase"
FT /id="PRO_1000200299"
FT ACT_SITE 100
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT ACT_SITE 103
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 338
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
SQ SEQUENCE 436 AA; 48956 MW; 00D119CEC7EEDE4B CRC64;
MSTGFFGDIQ KIKYEGPDST NPLAFRHYQP DEIVLGKRME DHLRFAVAYW HTFTWPGGDP
FGGQTFLRPW FEDTMKAAKL KADVAFEFFS LLGAPYYCFH DADVRPEGRN FAENTKNLNE
IVDYFAEKQA ATGTKLLWGT ANLFSNRRYM SGAATNPDPD VFAFAAATVK TCIDATQKLG
GENYVLWGGR EGYETLLNTD LKRELDQLGR FLNLVVEYKH KIGFKGTILI EPKPQEPTKH
QYDYDVATVY GFLKKHGVEN EVKVNIEQGH AILAGHSFEH ELALANALGI FGSIDMNRND
YQSGWDTDQF PNNVPEMALA YYHVLAGGGF KTGGTNFDAK LRRQSLDPAD LLIGHIGGMD
CCARGLKAAA KMIEDKALSQ PLADRYAGWE SAEAQKLFRG EYSLDEITNW VESHDVNPQP
KSGKQELLEN VVNRYV
//