ID D2B0X8_STRRD Unreviewed; 383 AA. AC D2B0X8; DT 09-FEB-2010, integrated into UniProtKB/TrEMBL. DT 09-FEB-2010, sequence version 1. DT 27-MAR-2024, entry version 86. 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 OrderedLocusNames=Sros_0353 {ECO:0000313|EMBL:ACZ83385.1}; OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI OS 9100). OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales; OC Streptosporangiaceae; Streptosporangium. OX NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ83385.1, ECO:0000313|Proteomes:UP000002029}; RN [1] {ECO:0000313|EMBL:ACZ83385.1, ECO:0000313|Proteomes:UP000002029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100 RC {ECO:0000313|Proteomes:UP000002029}; RX PubMed=21304675; DOI=10.4056/sigs.631049; RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T., RA Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L., RA Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N., RA Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Streptosporangium roseum type strain (NI RT 9100)."; RL Stand. Genomic Sci. 2:29-37(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: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|ARBA:ARBA00011881, CC ECO:0000256|HAMAP-Rule:MF_00455, ECO:0000256|RuleBase:RU000610}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00455, 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-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; CP001814; ACZ83385.1; -; Genomic_DNA. DR RefSeq; WP_012887131.1; NC_013595.1. DR AlphaFoldDB; D2B0X8; -. DR STRING; 479432.Sros_0353; -. DR KEGG; sro:Sros_0353; -. DR eggNOG; COG2115; Bacteria. DR HOGENOM; CLU_060750_0_0_11; -. DR OrthoDB; 9763981at2; -. DR Proteomes; UP000002029; 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; IPR013022; Xyl_isomerase-like_TIM-brl. DR InterPro; IPR013453; XylA_actinobac. DR InterPro; IPR001998; Xylose_isomerase. DR NCBIfam; TIGR02631; xylA_Arthro; 1. DR PANTHER; PTHR48320; -; 1. DR PANTHER; PTHR48320:SF1; XYLOSE ISOMERASE; 1. DR Pfam; PF01261; AP_endonuc_2; 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}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:UP000002029}; KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP- KW Rule:MF_00455}. FT DOMAIN 42..306 FT /note="Xylose isomerase-like TIM barrel" FT /evidence="ECO:0000259|Pfam:PF01261" FT ACT_SITE 55 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT ACT_SITE 58 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 179 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 215 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 215 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 218 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 243 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 285 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" SQ SEQUENCE 383 AA; 42749 MW; DDF6DA2E5CEAD8E6 CRC64; MSDYTPKPED RFTFGLWTVG WQARDQFGDA SRAPLDPVES VHRLAELGAY GVTFHDDDLL AVEPDRDKAV ERFKKALAET GLKVPMATTN LFTHPVFKDG GFTSNDRDVR RYALRKVMRN VDLAAELGAT TYVCWGGREG AESGAAKDIR AALSRYKEGM DLLTSYVIDR GYDIRFAIEP KPNEPRGDIL LPTVGHALAF INELEHSERV GLNPEVGHEE MAGLNFAHGI AQALWHGKLF HIDLNGQHGP RFDQDLVFGH GDVKNSFFLV DLLENGGYDG PRHFDYKPLR TEDAEDVWVS AAANMRTYLI LKEKVKAFHA DPEVVEARAA SRVAELSEPT LAPGETLEDL HRDDFDVDRA AARGFHFSRL NQLALEHLLG VRG //