XYLA_RHILW
ID XYLA_RHILW Reviewed; 436 AA.
AC B5ZQV6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
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}; OrderedLocusNames=Rleg2_3411;
OS Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395492;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2304;
RX PubMed=21304679; DOI=10.4056/sigs.44642;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT WSM2304, an effective microsymbiont of the South American clover Trifolium
RT polymorphum.";
RL Stand. Genomic Sci. 2:66-76(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001191; ACI56678.1; -; Genomic_DNA.
DR RefSeq; WP_012558995.1; NC_011369.1.
DR AlphaFoldDB; B5ZQV6; -.
DR SMR; B5ZQV6; -.
DR STRING; 395492.Rleg2_3411; -.
DR EnsemblBacteria; ACI56678; ACI56678; Rleg2_3411.
DR KEGG; rlt:Rleg2_3411; -.
DR eggNOG; COG2115; Bacteria.
DR HOGENOM; CLU_037261_1_0_5; -.
DR OMA; TLAMYEI; -.
DR OrthoDB; 481478at2; -.
DR Proteomes; UP000008330; 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 HAMAP; MF_00455; Xylose_isom_A; 1.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR InterPro; IPR013452; Xylose_isom_bac.
DR InterPro; IPR001998; Xylose_isomerase.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR PRINTS; PR00688; XYLOSISMRASE.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR02630; xylose_isom_A; 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_1000200300"
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; 49084 MW; 66BCA86B4EA44358 CRC64;
MSTGFFGDIQ KVKYEGPDST NPLAFRYYQP DEIVMGKRME DHLRFAVAYW HTFTWPGGDP
FGGQTFLRPW FEDTMKAAKL KADVAFEFFS LLGSPYYCFH DADVRPEGKN FAENTKNLNE
IVDYFAEKQA STGTKLLWGT ANLFSNRRYM SGAATNPDPD VFAFAAATVK TCIDATQKLG
GENYVLWGGR EGYETLLNTD LKRELDQLGR FLNLVVEYKH KIGYTGTILI EPKPQEPTKH
QYDYDVATVY GFLKKHGLEN EVKLNIEQGH AILAGHSFEH ELALANALGI FGSIDMNRND
YQSGWDTDQF PNNVPEMALA YYHVLAGGGF KTGGTNFDSK LRRQSLDPAD LLIGHIGGMD
CCARGLKAAA RMIEDKALSQ PLADRYAGWE SAEAQKLFRG EYSLDEITNW VETKDVNPQP
RSGKQELLEN VVNRYV