ID K7ADC1_9ALTE Unreviewed; 439 AA. AC K7ADC1; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 27-MAR-2024, entry version 68. DE RecName: Full=Xylose isomerase {ECO:0000256|ARBA:ARBA00011958, 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 ORFNames=C427_4907 {ECO:0000313|EMBL:AGH47006.1}; OS Paraglaciecola psychrophila 170. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Alteromonadaceae; Paraglaciecola. OX NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH47006.1, ECO:0000313|Proteomes:UP000011864}; RN [1] {ECO:0000313|EMBL:AGH47006.1, ECO:0000313|Proteomes:UP000011864} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=170 {ECO:0000313|EMBL:AGH47006.1, RC ECO:0000313|Proteomes:UP000011864}; RX PubMed=23640379; RA Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.; RT "Complete Genome Sequence of Glaciecola psychrophila Strain 170T."; RL Genome Announc. 1:E00199-13(2013). 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; CP003837; AGH47006.1; -; Genomic_DNA. DR RefSeq; WP_007643107.1; NZ_BAES01000095.1. DR AlphaFoldDB; K7ADC1; -. DR STRING; 1129794.C427_4907; -. DR KEGG; gps:C427_4907; -. DR PATRIC; fig|1129794.4.peg.4891; -. DR eggNOG; COG2115; Bacteria. DR HOGENOM; CLU_037261_1_0_6; -. DR OrthoDB; 9763981at2; -. DR Proteomes; UP000011864; 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:UP000011864}; KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP- KW Rule:MF_00455}. FT ACT_SITE 101 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT ACT_SITE 104 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 232 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 268 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 268 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 271 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 296 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 307 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 309 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 439 AA; 49229 MW; DEFA1A04110BD272 CRC64; MTTYFDAIPN IQFEGAESDS PLAFHHYNAN EVVLGKTMSE HLRFAACYWH NFCWDGADVF GQGTFNRPWL KPCDPMQMAI QKADVAFEFF SKLNIPYYCF HDIDVAPEGD SIHDYVNNFS TMVDVLEQKQ SETGLRLLWG TANLFSNPRF AAGGASNPNP DVFSYGATQV FHAMNATKRL GGENYVLWGG REGYESLLNT DLRQEREQLG RFFTMVAEHK HKIGFKGALL IEPKPQEPTK HQYDYDTASV YGFLKQYGLE QEFKVNIEAN HATLAGHSFH HEIATAISLG IFGSIDANRG DPQNGWDTDQ FPTAVDELSL VMYEILKSGG FTTGGLNFDC KLRRQSSDPA DLFHGHIGGM DHMALALKKA AAILENDFIA DKLSQRYEGW GQHFGQSILN GQQNLESLAS HTLSNSLQPK HVSGQQEMME NKVNRVLFG //