XYLA_ACTM4
ID XYLA_ACTM4 Reviewed; 394 AA.
AC P12851; I0GZR8;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA; Synonyms=XI; OrderedLocusNames=AMIS_10350;
OS Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 /
OS JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Actinoplanes.
OX NCBI_TaxID=512565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 / NCIMB
RC 12654 / NRRL B-3342 / UNCC 431;
RX PubMed=2798103; DOI=10.1093/nar/17.18.7515;
RA Amore R., Hollenberg C.P.;
RT "Xylose isomerase from Actinoplanes missouriensis: primary structure of the
RT gene and the protein.";
RL Nucleic Acids Res. 17:7515-7515(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 / NCIMB
RC 12654 / NRRL B-3342 / UNCC 431;
RA Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT 102363).";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=3237716; DOI=10.1002/prot.340040303;
RA Rey F., Jenkins J., Janin J., Lasters I., Alard P., Claessens M.,
RA Matthyssens G., Wodak S.J.;
RT "Structural analysis of the 2.8 A model of Xylose isomerase from
RT Actinoplanes missouriensis.";
RL Proteins 4:165-172(1988).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=1610791; DOI=10.1021/bi00139a005;
RA Jenkins J., Janin J., Rey F., Chiadmi M., van Tilbeurgh H., Lasters I.,
RA de Maeyer M., van Belle D., Wodak S.J., Lauwereys M., Stanssens P.,
RA Mrabet N.T., Snauwaert J., Matthyssens G., Lambeir A.-M.;
RT "Protein engineering of xylose (glucose) isomerase from Actinoplanes
RT missouriensis. 1. Crystallography and site-directed mutagenesis of metal
RT binding sites.";
RL Biochemistry 31:5449-5458(1992).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS).
RX PubMed=10089406; DOI=10.1107/s090744499800626x;
RA Ramin M., Shepard W., Fourme R., Kahn R.;
RT "Multiwavelength anomalous solvent contrast (MASC): derivation of envelope
RT structure-factor amplitudes and comparison with model values.";
RL Acta Crystallogr. D 55:157-167(1999).
RN [6]
RP MUTAGENESIS.
RX PubMed=1610792; DOI=10.1021/bi00139a006;
RA Lambeir A.-M., Lauwereys M., Stanssens P., Mrabet N.T., Snauwaert J.,
RA van Tilbeurgh H., Matthyssens G., Lasters I., de Maeyer M., Wodak S.J.,
RA Jenkins J., Chiadmi M., Janin J.;
RT "Protein engineering of xylose (glucose) isomerase from Actinoplanes
RT missouriensis. 2. Site-directed mutagenesis of the xylose binding site.";
RL Biochemistry 31:5459-5466(1992).
RN [7]
RP MUTAGENESIS.
RX PubMed=1610793; DOI=10.1021/bi00139a007;
RA van Tilbeurgh H., Jenkins J., Chiadmi M., Janin J., Wodak S.J.,
RA Mrabet N.T., Lambeir A.-M.;
RT "Protein engineering of xylose (glucose) isomerase from Actinoplanes
RT missouriensis. 3. Changing metal specificity and the pH profile by site-
RT directed mutagenesis.";
RL Biochemistry 31:5467-5472(1992).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 2 magnesium ions per subunit.;
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
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DR EMBL; X16042; CAA34164.1; -; Genomic_DNA.
DR EMBL; AP012319; BAL86255.1; -; Genomic_DNA.
DR PIR; S05998; ISMAXM.
DR RefSeq; WP_014441152.1; NC_017093.1.
DR PDB; 1BHW; X-ray; 4.10 A; A/B/C/D=2-394.
DR PDB; 1XIM; X-ray; 2.20 A; A/B/C/D=2-394.
DR PDB; 1XIN; X-ray; 2.40 A; A/B/C/D=2-394.
DR PDB; 2XIM; X-ray; 2.30 A; A/B/C/D=2-394.
DR PDB; 2XIN; X-ray; 2.30 A; A/B/C/D=2-394.
DR PDB; 3XIM; X-ray; 2.30 A; A/B/C/D=2-394.
DR PDB; 3XIN; X-ray; 2.30 A; A/B/C/D=2-394.
DR PDB; 4XIM; X-ray; 2.30 A; A/B/C/D=2-394.
DR PDB; 5XIM; X-ray; 2.60 A; A/B/C/D=2-394.
DR PDB; 5XIN; X-ray; 2.30 A; A/B/C/D=2-394.
DR PDB; 6XIM; X-ray; 2.50 A; A/B/C/D=2-394.
DR PDB; 7XIM; X-ray; 2.40 A; A/B/C/D=2-394.
DR PDB; 8XIM; X-ray; 2.40 A; A/B/C/D=2-394.
DR PDB; 9XIM; X-ray; 2.40 A; A/B/C/D=2-394.
DR PDBsum; 1BHW; -.
DR PDBsum; 1XIM; -.
DR PDBsum; 1XIN; -.
DR PDBsum; 2XIM; -.
DR PDBsum; 2XIN; -.
DR PDBsum; 3XIM; -.
DR PDBsum; 3XIN; -.
DR PDBsum; 4XIM; -.
DR PDBsum; 5XIM; -.
DR PDBsum; 5XIN; -.
DR PDBsum; 6XIM; -.
DR PDBsum; 7XIM; -.
DR PDBsum; 8XIM; -.
DR PDBsum; 9XIM; -.
DR AlphaFoldDB; P12851; -.
DR SMR; P12851; -.
DR STRING; 512565.AMIS_10350; -.
DR DrugBank; DB11195; Xylitol.
DR EnsemblBacteria; BAL86255; BAL86255; AMIS_10350.
DR KEGG; ams:AMIS_10350; -.
DR PATRIC; fig|512565.3.peg.1041; -.
DR eggNOG; COG2115; Bacteria.
DR HOGENOM; CLU_060750_0_0_11; -.
DR OMA; HKFTFGL; -.
DR OrthoDB; 481478at2; -.
DR BRENDA; 5.3.1.5; 141.
DR SABIO-RK; P12851; -.
DR EvolutionaryTrace; P12851; -.
DR Proteomes; UP000007882; 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 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 Pfam; PF01261; AP_endonuc_2; 1.
DR PRINTS; PR00688; XYLOSISMRASE.
DR SUPFAM; SSF51658; SSF51658; 1.
DR TIGRFAMs; TIGR02631; xylA_Arthro; 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 INIT_MET 1
FT /note="Removed"
FT CHAIN 2..394
FT /note="Xylose isomerase"
FT /id="PRO_0000195757"
FT ACT_SITE 54
FT ACT_SITE 57
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:1XIM"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:1XIM"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:1XIM"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1XIM"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 109..129
FT /evidence="ECO:0007829|PDB:1XIM"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1XIM"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 151..172
FT /evidence="ECO:0007829|PDB:1XIM"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1XIM"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:1XIM"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1XIM"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:1XIM"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:1XIM"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:2XIN"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:1XIM"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 265..276
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1XIM"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 301..327
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 354..359
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:1XIM"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 369..373
FT /evidence="ECO:0007829|PDB:1XIM"
FT HELIX 379..390
FT /evidence="ECO:0007829|PDB:1XIM"
SQ SEQUENCE 394 AA; 43499 MW; 764B1FC35AE7A780 CRC64;
MSVQATREDK FSFGLWTVGW QARDAFGDAT RTALDPVEAV HKLAEIGAYG ITFHDDDLVP
FGSDAQTRDG IIAGFKKALD ETGLIVPMVT TNLFTHPVFK DGGFTSNDRS VRRYAIRKVL
RQMDLGAELG AKTLVLWGGR EGAEYDSAKD VSAALDRYRE ALNLLAQYSE DRGYGLRFAI
EPKPNEPRGD ILLPTAGHAI AFVQELERPE LFGINPETGH EQMSNLNFTQ GIAQALWHKK
LFHIDLNGQH GPKFDQDLVF GHGDLLNAFS LVDLLENGPD GAPAYDGPRH FDYKPSRTED
YDGVWESAKA NIRMYLLLKE RAKAFRADPE VQEALAASKV AELKTPTLNP GEGYAELLAD
RSAFEDYDAD AVGAKGFGFV KLNQLAIEHL LGAR
