XYLA_BACTN
ID XYLA_BACTN Reviewed; 438 AA.
AC Q8A9M2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Xylose isomerase {ECO:0000255|HAMAP-Rule:MF_00455};
DE EC=5.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00455};
GN Name=xylA {ECO:0000255|HAMAP-Rule:MF_00455}; OrderedLocusNames=BT_0793;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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:0000255|HAMAP-Rule:MF_00455};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00455};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00455};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00455}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00455}.
CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000255|HAMAP-
CC Rule:MF_00455}.
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DR EMBL; AE015928; AAO75900.1; -; Genomic_DNA.
DR RefSeq; NP_809706.1; NC_004663.1.
DR RefSeq; WP_011107447.1; NC_004663.1.
DR PDB; 4XKM; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-438.
DR PDBsum; 4XKM; -.
DR AlphaFoldDB; Q8A9M2; -.
DR SMR; Q8A9M2; -.
DR STRING; 226186.BT_0793; -.
DR PaxDb; Q8A9M2; -.
DR PRIDE; Q8A9M2; -.
DR EnsemblBacteria; AAO75900; AAO75900; BT_0793.
DR GeneID; 60926762; -.
DR KEGG; bth:BT_0793; -.
DR PATRIC; fig|226186.12.peg.811; -.
DR eggNOG; COG2115; Bacteria.
DR HOGENOM; CLU_037261_1_0_10; -.
DR InParanoid; Q8A9M2; -.
DR OMA; TLAMYEI; -.
DR BRENDA; 5.3.1.5; 709.
DR Proteomes; UP000001414; 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; IBA:GO_Central.
DR GO; GO:0042843; P:D-xylose catabolic process; IBA:GO_Central.
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; IPR013452; Xylose_isom_bac.
DR InterPro; IPR001998; Xylose_isomerase.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR PRINTS; PR00688; XYLOSISMRASE.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR02630; xylose_isom_A; 1.
DR PROSITE; PS51415; XYLOSE_ISOMERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium;
KW Metal-binding; Reference proteome; Xylose metabolism.
FT CHAIN 1..438
FT /note="Xylose isomerase"
FT /id="PRO_0000195768"
FT ACT_SITE 103
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT ACT_SITE 106
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT BINDING 341
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:4XKM"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 77..95
FT /evidence="ECO:0007829|PDB:4XKM"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 114..135
FT /evidence="ECO:0007829|PDB:4XKM"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:4XKM"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 162..181
FT /evidence="ECO:0007829|PDB:4XKM"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:4XKM"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 204..224
FT /evidence="ECO:0007829|PDB:4XKM"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:4XKM"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:4XKM"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:4XKM"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 281..290
FT /evidence="ECO:0007829|PDB:4XKM"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 317..329
FT /evidence="ECO:0007829|PDB:4XKM"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 352..378
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 381..388
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 395..401
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:4XKM"
FT HELIX 427..435
FT /evidence="ECO:0007829|PDB:4XKM"
SQ SEQUENCE 438 AA; 48938 MW; DDF724888AE5EF71 CRC64;
MATKEFFPGI EKIKFEGKDS KNPMAFRYYD AEKVINGKKM KDWLRFAMAW WHTLCAEGGD
QFGGGTKQFP WNGNADAIQA AKDKMDAGFE FMQKMGIEYY CFHDVDLVSE GASVEEYEAN
LKEIVAYAKQ KQAETGIKLL WGTANVFGHA RYMNGAATNP DFDVVARAAV QIKNAIDATI
ELGGENYVFW GGREGYMSLL NTDQKREKEH LAQMLTIARD YARARGFKGT FLIEPKPMEP
TKHQYDVDTE TVIGFLKAHG LDKDFKVNIE VNHATLAGHT FEHELAVAVD NGMLGSIDAN
RGDYQNGWDT DQFPIDNYEL TQAMMQIIRN GGLGTGGTNF DAKTRRNSTD LEDIFIAHIA
GMDAMARALE SAAALLDESP YKKMLADRYA SFDGGKGKEF EDGKLTLEDV VAYAKTKGEP
KQTSGKQELY EAILNMYC
