ID K0JQV9_SACES Unreviewed; 318 AA.
AC K0JQV9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Xylose isomerase {ECO:0000256|ARBA:ARBA00018232, ECO:0000256|RuleBase:RU000609};
DE EC=5.3.1.5 {ECO:0000256|ARBA:ARBA00011958, ECO:0000256|RuleBase:RU000609};
GN Name=xylA {ECO:0000313|EMBL:CCH29915.1};
GN OrderedLocusNames=BN6_26020 {ECO:0000313|EMBL:CCH29915.1};
OS Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC
OS 15066 / NRRL 15764).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1179773 {ECO:0000313|EMBL:CCH29915.1, ECO:0000313|Proteomes:UP000006281};
RN [1] {ECO:0000313|EMBL:CCH29915.1, ECO:0000313|Proteomes:UP000006281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764
RC {ECO:0000313|Proteomes:UP000006281};
RX PubMed=22958348; DOI=10.1186/1471-2164-13-465;
RA Strobel T., Al-Dilaimi A., Blom J., Gessner A., Kalinowski J.,
RA Luzhetska M., Puhler A., Szczepanowski R., Bechthold A., Ruckert C.;
RT "Complete genome sequence of Saccharothrix espanaensis DSM 44229T and
RT comparison to the other completely sequenced Pseudonocardiaceae.";
RL BMC Genomics 13:465-465(2012).
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,
CC ECO:0000256|RuleBase:RU000609};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|RuleBase:RU000610}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU000610}.
CC -!- SIMILARITY: Belongs to the xylose isomerase family.
CC {ECO:0000256|ARBA:ARBA00005765, ECO:0000256|RuleBase:RU000609}.
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DR EMBL; HE804045; CCH29915.1; -; Genomic_DNA.
DR AlphaFoldDB; K0JQV9; -.
DR STRING; 1179773.BN6_26020; -.
DR KEGG; sesp:BN6_26020; -.
DR PATRIC; fig|1179773.3.peg.2601; -.
DR eggNOG; COG2115; Bacteria.
DR HOGENOM; CLU_060750_0_0_11; -.
DR Proteomes; UP000006281; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009045; F:xylose isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 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 NCBIfam; TIGR02631; xylA_Arthro; 1.
DR PANTHER; PTHR30268; L-RHAMNOSE ISOMERASE; 1.
DR PANTHER; PTHR30268:SF0; L-RHAMNOSE 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,
KW ECO:0000256|RuleBase:RU000609}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000609};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000609};
KW Reference proteome {ECO:0000313|Proteomes:UP000006281};
KW Xylose metabolism {ECO:0000256|RuleBase:RU000609}.
FT DOMAIN 16..223
FT /note="Xylose isomerase-like TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01261"
SQ SEQUENCE 318 AA; 35021 MW; C4583C06E56B6F82 CRC64;
MDRSSFGLWT VGRHTGLVVP MVTTNLFTHP VFKDGGFTSN DRSVRRFALR KVLRNLELAA
ELGASTVVLW GGREGSEVDA GKDVRAALDR YREALDIVVR YSEDQGCGLR FAVEPKPNEP
RGDILLPTIG HALAFISTLE HHELVGVNPE VGHEQMAGLN VVHGVAQALW QGKLFHLDLN
GQKGPRYDQD LVFGHGDLLS AFFLVDLVEH GGYDGPRHFD YKPLRTEDLD GVWVSAAANM
RTYRLLRERA VVFRADPEVQ EALRHSGVYE LGESTLAPGE SVAEFVVQDE DASGAAERGY
GFVRLSQLAL EHLVGARG
//
