ID A0A1B1MXM5_9BACL Unreviewed; 438 AA.
AC A0A1B1MXM5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=AWM70_04535 {ECO:0000313|EMBL:ANS73924.1};
OS Paenibacillus yonginensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1462996 {ECO:0000313|EMBL:ANS73924.1, ECO:0000313|Proteomes:UP000092573};
RN [1] {ECO:0000313|EMBL:ANS73924.1, ECO:0000313|Proteomes:UP000092573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY84 {ECO:0000313|EMBL:ANS73924.1,
RC ECO:0000313|Proteomes:UP000092573};
RA Kim Y.J., Yang D.C., Sukweenadhi J.;
RT "Complete Genome Sequence of Paenibacillus yonginensis DCY84, a novel Plant
RT Growth-Promoting Bacteria with Elicitation of Induced Systemic
RT Resistance.";
RL Submitted (JAN-2016) 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|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}.
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DR EMBL; CP014167; ANS73924.1; -; Genomic_DNA.
DR RefSeq; WP_068694533.1; NZ_CP014167.1.
DR AlphaFoldDB; A0A1B1MXM5; -.
DR STRING; 1462996.AWM70_04535; -.
DR KEGG; pyg:AWM70_04535; -.
DR OrthoDB; 9763981at2; -.
DR Proteomes; UP000092573; 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:UP000092573};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW Rule:MF_00455}.
FT ACT_SITE 99
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT ACT_SITE 102
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
SQ SEQUENCE 438 AA; 49235 MW; A301B811A3E86F9F CRC64;
MSHFSDINVI AYEGPSSKNP LAFKHYNPKE VVAGKTMEEH LRFATAYWHT FVADGTDMFG
RGTALRPWDS YSGLDQAKFR VEASFEFYEK LGVPYFCFHD VDIAPEGDTL QETNKNLDVI
VAMMKDYMKT SKAKLLWNTA NMFTNPRYTH GAGTSSNAVV YARAAAQVKK GLEVGKELGA
QNYVFWGGRE GYETLLNTDM AFELDNLARL YRMAIDYAKE IGFDAQFLIE PKPKEPTKHQ
YDFDAATTIA FLYRYDLKDH FKLNLEANHA TLAGHTFEHE LRVARDNGVL GSLDANQGDV
LLGWDTDEFP YDLYTTTLTM HEVLKNGGLG KGGVNFDAKV RRGSFEPVDL FYAHIAGMDA
YAKGLKVAAK MIEDNYFENI VADRYSSFKS EVGESIVSGK ATLKSLEEFA LQNNPVNNKS
GRLELIRATL NQYILGDL
//
