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Database: UniProt
Entry: A0A1P8NH78_9MICO
LinkDB: A0A1P8NH78_9MICO
Original site: A0A1P8NH78_9MICO 
ID   A0A1P8NH78_9MICO        Unreviewed;       397 AA.
AC   A0A1P8NH78;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   17-JUN-2020, entry version 19.
DE   RecName: Full=Xylose isomerase {ECO:0000256|HAMAP-Rule:MF_00455, ECO:0000256|RuleBase:RU000609};
DE            EC=5.3.1.5 {ECO:0000256|HAMAP-Rule:MF_00455, ECO:0000256|RuleBase:RU000609};
GN   Name=xylA {ECO:0000256|HAMAP-Rule:MF_00455};
GN   ORFNames=BH708_14195 {ECO:0000313|EMBL:APX33674.1};
OS   Brachybacterium sp. P6-10-X1.
OC   Bacteria; Actinobacteria; Micrococcales; Dermabacteraceae; Brachybacterium;
OC   unclassified Brachybacterium.
OX   NCBI_TaxID=1903186 {ECO:0000313|EMBL:APX33674.1, ECO:0000313|Proteomes:UP000185991};
RN   [1] {ECO:0000313|EMBL:APX33674.1, ECO:0000313|Proteomes:UP000185991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6-10-X1 {ECO:0000313|EMBL:APX33674.1,
RC   ECO:0000313|Proteomes:UP000185991};
RA   Zhao B., Liao L., Chen B.;
RT   "Complete genome of Brachybacterium sp. P6-10-X1.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-xylose = D-xylulose; Xref=Rhea:RHEA:22816,
CC         ChEBI:CHEBI:17140, ChEBI:CHEBI:53455; EC=5.3.1.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00455,
CC         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|HAMAP-Rule:MF_00455,
CC       ECO:0000256|RuleBase:RU000610}.
CC   -!- SIMILARITY: Belongs to the xylose isomerase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00455, ECO:0000256|RuleBase:RU000609,
CC       ECO:0000256|SAAS:SAAS00580662}.
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; CP017297; APX33674.1; -; Genomic_DNA.
DR   RefSeq; WP_076809699.1; NZ_CP017297.1.
DR   KEGG; brx:BH708_14195; -.
DR   OrthoDB; 481478at2; -.
DR   Proteomes; UP000185991; 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   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 {ECO:0000256|HAMAP-Rule:MF_00455,
KW   ECO:0000256|RuleBase:RU000609, ECO:0000256|SAAS:SAAS00472203};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00455};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_00455, ECO:0000256|RuleBase:RU000609,
KW   ECO:0000256|SAAS:SAAS00108565, ECO:0000313|EMBL:APX33674.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00455};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00455,
KW   ECO:0000256|RuleBase:RU000609, ECO:0000256|SAAS:SAAS00472349};
KW   Xylose metabolism {ECO:0000256|HAMAP-Rule:MF_00455,
KW   ECO:0000256|RuleBase:RU000609}.
FT   DOMAIN          42..266
FT                   /note="AP_endonuc_2"
FT                   /evidence="ECO:0000259|Pfam:PF01261"
FT   ACT_SITE        55
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   ACT_SITE        58
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   METAL           182
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   METAL           218
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   METAL           218
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   METAL           221
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   METAL           246
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT   METAL           294
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
SQ   SEQUENCE   397 AA;  44273 MW;  314EEA36FA8B7620 CRC64;
     MTAPTPTRED KFSFGLWTTG WEAQDQFGSA SRPPLELSAH IRRLSELGAW GFTFHDNDVV
     PFDATAAERS RIIDQLKKVT EETGLVIEMV TTDTFAHPVF KDGAFTSNDR DVRRFGLRKV
     LANVDLAAEL GASTFVMWGG REGAEYDGSK DLFAALERYR EGIDTVAGYI KDKGYDLRIG
     LEPKPNEPRG NIFLPTVGHA LAFIEQLEHG DIVGINPETG HEQMATLNYT HGLAQALWSE
     KLFHIDLNGQ HGPMYDQDLV FGHGDLISAF FTVDLLENGF PSKPGAYEGA RHFDFKPSRT
     EHEKGQYDAA AANMEMYLML KERAIAFRQD AEVQEALSYS GVDELAQPTI AEGESLADLL
     ADRSTYEEFD PDKAGERNYG FVRLQQLALQ HLLGFRA
//
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