ID A0A495X771_9PSEU Unreviewed; 378 AA.
AC A0A495X771;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 ORFNames=DFJ66_1997 {ECO:0000313|EMBL:RKT68804.1};
OS Saccharothrix variisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=543527 {ECO:0000313|EMBL:RKT68804.1, ECO:0000313|Proteomes:UP000272729};
RN [1] {ECO:0000313|EMBL:RKT68804.1, ECO:0000313|Proteomes:UP000272729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43911 {ECO:0000313|EMBL:RKT68804.1,
RC ECO:0000313|Proteomes:UP000272729};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000256|HAMAP-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKT68804.1}.
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DR EMBL; RBXR01000001; RKT68804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495X771; -.
DR Proteomes; UP000272729; Unassembled WGS sequence.
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; PTHR12110; HYDROXYPYRUVATE ISOMERASE; 1.
DR PANTHER; PTHR12110:SF59; 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:UP000272729};
KW Xylose metabolism {ECO:0000256|HAMAP-Rule:MF_00455,
KW ECO:0000256|RuleBase:RU000609}.
FT DOMAIN 33..283
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 378 AA; 41772 MW; 0ECA419CF9684B7A CRC64;
MDKFSFGLWT VGWQGRDPFG LASRPPLDPA VTVRKLAELG AWGVTFHDDD LVPFGADAAV
RDKRITDFRK ALDETGLVVP MVTTDLFTQP VFKDGGFTSN DRRVRRFALR KVLRNLELAA
ELGAQTIVLW GGREGSEVDA GKDVKAALDR YREALDTIAA YSESQGYGFR FALEPKPNEP
RGDILLPTIG HALAFISTLE HEPLFGVNPE VGHEQMAGLN FVHGIGQALW QGKLFHIDLN
GQKGPRYDQD FVFGHGDLLS AFFLVDLLEN GGYEGPRHFD YKPLRTEDFD GVWASAAANM
RTYKLLKERV AAFRADPEVQ EALQASGVFE QSESTLDAGE SIEDFIKADE DITAATERGY
GFVHLSQLAL EHVLGARG
//
