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Database: UniProt/TrEMBL
Entry: F8AT19_BIFLN
LinkDB: F8AT19_BIFLN
Original site: F8AT19_BIFLN 
ID   F8AT19_BIFLN            Unreviewed;       449 AA.
AC   F8AT19;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Xylose isomerase {ECO:0000256|ARBA:ARBA00011958, 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=BLNIAS_00502 {ECO:0000313|EMBL:AEI96909.1};
OS   Bifidobacterium longum subsp. longum KACC 91563.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1035817 {ECO:0000313|EMBL:AEI96909.1, ECO:0000313|Proteomes:UP000008938};
RN   [1] {ECO:0000313|EMBL:AEI96909.1, ECO:0000313|Proteomes:UP000008938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC 91563 {ECO:0000313|EMBL:AEI96909.1,
RC   ECO:0000313|Proteomes:UP000008938};
RX   PubMed=21742881; DOI=10.1128/JB.05620-11;
RA   Ham J.S., Lee T., Byun M.J., Lee K.T., Kim M.K., Han G.S., Jeong S.G.,
RA   Oh M.H., Kim D.H., Kim H.;
RT   "Complete Genome Sequence of Bifidobacterium longum subsp. longum KACC
RT   91563.";
RL   J. Bacteriol. 193:5044-5044(2011).
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|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00455, 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; CP002794; AEI96909.1; -; Genomic_DNA.
DR   RefSeq; WP_014485384.1; NC_017221.1.
DR   AlphaFoldDB; F8AT19; -.
DR   KEGG; blk:BLNIAS_00502; -.
DR   PATRIC; fig|1035817.4.peg.332; -.
DR   HOGENOM; CLU_037261_1_0_11; -.
DR   Proteomes; UP000008938; 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; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   InterPro; IPR013452; Xylose_isom_bac.
DR   InterPro; IPR001998; Xylose_isomerase.
DR   NCBIfam; TIGR02630; xylose_isom_A; 1.
DR   PANTHER; PTHR48306; XYLOSE ISOMERASE; 1.
DR   PANTHER; PTHR48306:SF1; XYLOSE ISOMERASE; 1.
DR   Pfam; PF01261; AP_endonuc_2; 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};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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};
KW   Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW   Rule:MF_00455}.
FT   DOMAIN          90..286
FT                   /note="Xylose isomerase-like TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01261"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   ACT_SITE        104
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         271
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
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         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   BINDING         340
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
SQ   SEQUENCE   449 AA;  50853 MW;  37EF0010D407452C CRC64;
     MGLWDVDKIE YVGRAKGPKE DFAFHYYDAD KVVAGKKMKD WLRFGVAWWH TFNQELVDPF
     GTGTAHRPYY KYTNPMDQAL AKVDYAFELF QKLGVEYFCF HDRDIAPEGD TLRETNANLD
     KVVDKIDENM KSTGVKLLWN TSSLFTNPRF VSGAATSPFA DIYAYAGGQL KKSLEIGKRL
     GAENYVFWGG REGYENLWNT EMKRETDHIA KFFHMCADYA KEIGFEAQFL IEPKPKEPTL
     HQYDFDAATA IEFLRNHDLT DVFKLNLEGN HANLAGHTYQ HEIRVARESG FLGSLDANQG
     DKLIGWDMDE FPTDLYETVA VMWEVLQAGS IGPHGGLNFD AKPRRTSFYE EDLFRSHIAG
     MDAYAAGLLV ADKMNQDGFI QNLQAERYSS YDSGIGKDID EGNVTLADLE AYSLDKPQSE
     LIAATKSDHL ESVKATINNY IIDALAEVE
//
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