ID A0A1B1BFN6_9MICO Unreviewed; 396 AA.
AC A0A1B1BFN6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Xylose isomerase {ECO:0000256|ARBA:ARBA00018232, 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=PA27867_0395 {ECO:0000313|EMBL:ANP71368.1};
OS Cryobacterium arcticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=670052 {ECO:0000313|EMBL:ANP71368.1, ECO:0000313|Proteomes:UP000092582};
RN [1] {ECO:0000313|EMBL:ANP71368.1, ECO:0000313|Proteomes:UP000092582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27867 {ECO:0000313|EMBL:ANP71368.1,
RC ECO:0000313|Proteomes:UP000092582};
RA Lee J., Kim O.-S.;
RT "Genome sequencing of Cryobacterium arcticum PAMC 27867.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00011881,
CC ECO:0000256|HAMAP-Rule:MF_00455, 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00455}.
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DR EMBL; CP016282; ANP71368.1; -; Genomic_DNA.
DR RefSeq; WP_066592498.1; NZ_CP016282.1.
DR AlphaFoldDB; A0A1B1BFN6; -.
DR STRING; 670052.PA27867_0395; -.
DR KEGG; cart:PA27867_0395; -.
DR PATRIC; fig|670052.7.peg.416; -.
DR OrthoDB; 9763981at2; -.
DR Proteomes; UP000092582; 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 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; 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, 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|HAMAP-Rule:MF_00455,
KW ECO:0000256|RuleBase:RU000609}.
FT DOMAIN 42..279
FT /note="Xylose isomerase-like TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01261"
FT ACT_SITE 54
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT ACT_SITE 57
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
SQ SEQUENCE 396 AA; 43487 MW; 4F96928D4581C2DD CRC64;
MSLTPTPADK FSFGLWTIGY NGADPFGGPT RPQLDTVEAV TRLAELGAYG LTFHDDDLFA
FGSTDAARQK EIDRLKQVLA DTGVIVPMIT TNLFSAPVFK DGGFTSNDRS VRRFALRKVL
RNLDLAAELG AKTFVMWGGR EGAEYDAAKD IRSALDRYRE AVNLLGDYVT DKGYDIRFAI
EPKPNEPRGD ILLPTVGHAM AFITTLERPE LVGVNPEVGH EQMAGLNFTA GIAQALYQGK
LFHIDLNGQR GIKYDQDLVF GHGDLQNAFS LVDLLENGGP NGGPSYDGPR HFDYKPSRTE
DITGVWDSAA ANMRTYLLLK ERAAAFRADP EVQEQLAASR VPELSVPTLS EGESYDDFLA
DTSAYEDFAP EEYFGGKGFG FVRLQQLALE HLLGAR
//
