XYLA_ACTS3
ID XYLA_ACTS3 Reviewed; 394 AA.
AC P10654;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Xylose isomerase;
DE EC=5.3.1.5;
GN Name=xylA;
OS Actinoplanes sp. (strain ATCC 31351 / 3876) (Ampullariella sp.).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Actinoplanes; unclassified Actinoplanes.
OX NCBI_TaxID=1872;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3027039; DOI=10.1128/jb.169.2.612-618.1987;
RA Saari G.C., Kumar A.A., Kawasaki G.H., Insley M.Y., O'Hara P.J.;
RT "Sequence of the Ampullariella sp. strain 3876 gene coding for xylose
RT isomerase.";
RL J. Bacteriol. 169:612-618(1987).
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; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000305}.
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DR EMBL; M15050; AAA92578.1; -; Genomic_DNA.
DR PIR; A27756; ISMAXA.
DR AlphaFoldDB; P10654; -.
DR SMR; P10654; -.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium; Metal-binding;
KW Xylose metabolism.
FT CHAIN 1..394
FT /note="Xylose isomerase"
FT /id="PRO_0000195759"
FT ACT_SITE 54
FT /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 394 AA; 43396 MW; 22070462486F8567 CRC64;
MSLQATPDDK FSFGLWTVGW QARDAFGDAT RPVLDPIEAV HKLAEIGAYG VTFHDDDLVP
FGADAATRDG IVAGFSKALD ETGLIVPMVT TNLFTHPVFK DGGFTSNDRS VRRYAIRKVL
RQMDLGAELG AKTLVLWGGR EGAEYDSAKD VGAALDRYRE ALNLLAQYSE DQGYGLPFAI
EPKPNEPRGD ILLPTAGHAI AFVQELERPE LFGINRETGH EQMSNLNFTQ GIAQALWHKK
LFHIDLNGQH GPKFDQDLVF GHGDLLNAFS LVDLLENGPD GGPAYDGPRH FDYKPSRTED
FDGVWESAKD NIRMYLLLKE RAKAFRADPE VQAALAESKV DELRTPTLNP GETYADLLAD
RSAFEDYDAD AVGAKGYGFV KLNQLAIDHL LGAR
