ID C6WCX6_ACTMD Unreviewed; 379 AA. AC C6WCX6; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 92. 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=Amir_1795 {ECO:0000313|EMBL:ACU35743.1}; OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 OS / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101). OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales; OC Pseudonocardiaceae; Actinosynnema. OX NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU35743.1, ECO:0000313|Proteomes:UP000002213}; RN [1] {ECO:0000313|EMBL:ACU35743.1, ECO:0000313|Proteomes:UP000002213} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 / RC NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213}; RX PubMed=21304636; DOI=10.4056/sigs.21137; RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G., RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L., RA Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K., RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T., RA Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Actinosynnema mirum type strain (101)."; RL Stand. Genomic Sci. 1:46-53(2009). 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; CP001630; ACU35743.1; -; Genomic_DNA. DR RefSeq; WP_015800632.1; NC_013093.1. DR AlphaFoldDB; C6WCX6; -. DR STRING; 446462.Amir_1795; -. DR KEGG; ami:Amir_1795; -. DR eggNOG; COG2115; Bacteria. DR HOGENOM; CLU_060750_0_0_11; -. DR OrthoDB; 9763981at2; -. DR Proteomes; UP000002213; 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; PTHR30268; L-RHAMNOSE ISOMERASE; 1. DR PANTHER; PTHR30268:SF0; L-RHAMNOSE 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:UP000002213}; KW Xylose metabolism {ECO:0000256|HAMAP-Rule:MF_00455, KW ECO:0000256|RuleBase:RU000609}. FT DOMAIN 33..284 FT /note="Xylose isomerase-like TIM barrel" FT /evidence="ECO:0000259|Pfam:PF01261" FT ACT_SITE 47 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT ACT_SITE 50 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 174 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 210 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 210 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 213 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 238 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" FT BINDING 280 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455" SQ SEQUENCE 379 AA; 41711 MW; FDF9C447C8617C62 CRC64; MTDFSFGLWT VGWQGRDPFG DATRPVLDAP TAVRKLAELG AWGVTFHDDD LIPFGAGAAE RDRRVSAFRG ALDETGLVVP MVTTNLFTHP VFKDGGFTSN DRSVRRFALR KVLRNLELAA ELGAKTIVLW GGREGSETDA GKDVQAALER YREALDTVAQ HSVDQGYGFR FALEPKPNEP RGDILLPTVG HALAFISTLQ HHELVGVNPE VGHEQMANLN FVHGIAQALW QKKLFHIDLN GQKGPRFDQD LVFGHGDLLS AFFLVDLLEN GGYDGPRHFD YKPLRTEDVD GVWDSAAANM RTYTLLKERA QAYRADPEVQ EALRVSGVTE QAVPTLGEGE SIADFLAADE SFDPDKAAER GYGFVKLSQL ALEHLLGAR //