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XYLA_PHOPR
ID   XYLA_PHOPR              Reviewed;         439 AA.
AC   Q6LUY7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   03-AUG-2022, entry version 96.
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=PBPRA0457;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG18888.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR378664; CAG18888.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011217244.1; NC_006370.1.
DR   AlphaFoldDB; Q6LUY7; -.
DR   SMR; Q6LUY7; -.
DR   STRING; 298386.PBPRA0457; -.
DR   EnsemblBacteria; CAG18888; CAG18888; PBPRA0457.
DR   KEGG; ppr:PBPRA0457; -.
DR   eggNOG; COG2115; Bacteria.
DR   HOGENOM; CLU_037261_1_0_6; -.
DR   OrthoDB; 481478at2; -.
DR   Proteomes; UP000000593; Chromosome 1.
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; IPR013452; Xylose_isom_bac.
DR   InterPro; IPR001998; Xylose_isomerase.
DR   PRINTS; PR00688; XYLOSISMRASE.
DR   SUPFAM; SSF51658; SSF51658; 1.
DR   TIGRFAMs; TIGR02630; xylose_isom_A; 1.
DR   PROSITE; PS51415; XYLOSE_ISOMERASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Isomerase; Magnesium; Metal-binding;
KW   Reference proteome; Xylose metabolism.
FT   CHAIN           1..439
FT                   /note="Xylose isomerase"
FT                   /id="PRO_0000195786"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   ACT_SITE        104
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         271
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
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         339
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00455"
SQ   SEQUENCE   439 AA;  49342 MW;  53C2264A1F2CAB97 CRC64;
     MTEFFKNINK IQFEGTDAIN PLAFRHYDAE RMILGKSMKE HLRFAACYWH NFCWPGSDVF
     GAATFDRPWL QSGNAMEMAH MKADAAFDFF SKLGVPYYCF HDTDIAPEGT SLKEYVNNFA
     QMVDVLEQKQ DETGLKLLWG TANAFSNPRY MSGAGTNPDP KVFAYAATQI FNAMGATQRL
     GGENYVLWGG REGYETLLNT DLRQEREQLG RLMQMVVEHK HKIGFKGTIL IEPKPQEPTK
     HQYDYDTATV YGFLKQFGLE NEIKVNIEAN HATLAGHSFQ HEIATATSLG LFGSIDANRG
     DPQLGWDTDQ FPNSVEENTL VMYEILKAGG FTTGGFNFDS HVRRPSIDAE DLFYGHIGGM
     DTMALALERA ANMIENDVLS KNIAQRYAGW NEDLGKKILS GDHSLETLAK FALDSNIAPV
     KESGRQEHLE NIVNGFIYK
 
 
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