ID J9VZ63_LENBU Unreviewed; 445 AA. AC J9VZ63; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 27-MAR-2024, entry version 67. DE RecName: Full=Xylose isomerase {ECO:0000256|ARBA:ARBA00018232, ECO:0000256|HAMAP-Rule:MF_00455}; DE EC=5.3.1.5 {ECO:0000256|ARBA:ARBA00011958, ECO:0000256|HAMAP-Rule:MF_00455}; GN Name=xylA {ECO:0000256|HAMAP-Rule:MF_00455, GN ECO:0000313|EMBL:AFR99528.1}; GN ORFNames=LBUCD034_0429 {ECO:0000313|EMBL:AFR99528.1}; OS Lentilactobacillus buchneri subsp. silagei CD034. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lentilactobacillus; Lentilactobacillus buchneri subsp. silagei. OX NCBI_TaxID=1071400 {ECO:0000313|EMBL:AFR99528.1, ECO:0000313|Proteomes:UP000007332}; RN [1] {ECO:0000313|EMBL:AFR99528.1, ECO:0000313|Proteomes:UP000007332} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CD034 {ECO:0000313|EMBL:AFR99528.1, RC ECO:0000313|Proteomes:UP000007332}; RX PubMed=22465289; DOI=10.1016/j.jbiotec.2012.03.007; RA Heinl S., Wibberg D., Eikmeyer F., Szczepanowski R., Blom J., Linke B., RA Goesmann A., Grabherr R., Schwab H., Puhler A., Schluter A.; RT "Insights into the completely annotated genome of Lactobacillus buchneri RT CD034, a strain isolated from stable grass silage."; RL J. Biotechnol. 161:153-166(2012). 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:0000256|ARBA:ARBA00033659, ECO:0000256|HAMAP- CC Rule:MF_00455, ECO:0000256|RuleBase:RU000609}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00455}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00455}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00455, CC ECO:0000256|RuleBase:RU000610}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00455, CC ECO:0000256|RuleBase:RU000610}. CC -!- SIMILARITY: Belongs to the xylose isomerase family. CC {ECO:0000256|ARBA:ARBA00005765, ECO:0000256|HAMAP-Rule:MF_00455, CC ECO:0000256|RuleBase:RU000609}. 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; CP003043; AFR99528.1; -; Genomic_DNA. DR RefSeq; WP_013727223.1; NC_018610.1. DR AlphaFoldDB; J9VZ63; -. DR STRING; 1071400.LBUCD034_0429; -. DR GeneID; 72461428; -. DR KEGG; lbn:LBUCD034_0429; -. DR PATRIC; fig|1071400.3.peg.422; -. DR eggNOG; COG2115; Bacteria. DR HOGENOM; CLU_037261_1_0_9; -. DR OrthoDB; 9763981at2; -. DR Proteomes; UP000007332; 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 {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP- KW Rule:MF_00455}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00455}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00455}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00455}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00455}; Reference proteome {ECO:0000313|Proteomes:UP000007332}; KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP- KW Rule:MF_00455}. FT ACT_SITE 100 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT ACT_SITE 103 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 231 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 267 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 267 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 270 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 295 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 306 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 308 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 339 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" SQ SEQUENCE 445 AA; 50266 MW; 52DEC5B25A793D73 CRC64; MSYWNVDKIK YVGTGEKKSG LGFQYYNPDE VVGGKKMRDW LRFAVAYWHT FDQRLVDPFG DGTAIRPYDK YTDPMDQALA KVDAAFEFYD KLGVDFLCFH DRDLAPEGDT LRETNRNLDK VVDKIVENQK TSGMKVLWNT SNLFTNPRFV EGAGTSPYAD IFAYSAAQLK HSLEIGKRVG SENYVFWGGR EGYESLWNTD MKREQEHAAK LFHMAKDYAN EIGFDAQMLL EPKPKEPTTH QYDFDAATTI AFMKEYGLDK DFKLNLEGNH ANLAGHTYQH EIRVAREAGL LGSLDANQGD KLIGWDIDEY PSNLYETTAA MTEVVENGSI GPRGGLNFDA KPRRSSFEPN DLFYGHIVGM DSFAAGLRVA VAMKNDGVLD DIVKNRYSSF DSGIGADIES GKASMADLEN YSLDKTQKDL RDATHSDHLE EIKDTINHYI IQTLK //