ID A0A0H3DC15_AMYMU Unreviewed; 382 AA.
AC A0A0H3DC15;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ECO:0000313|EMBL:ADJ48500.1};
GN OrderedLocusNames=AMED_6776 {ECO:0000313|EMBL:ADJ48500.1};
OS Amycolatopsis mediterranei (strain U-32).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=749927 {ECO:0000313|EMBL:ADJ48500.1, ECO:0000313|Proteomes:UP000000328};
RN [1] {ECO:0000313|EMBL:ADJ48500.1, ECO:0000313|Proteomes:UP000000328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U-32 {ECO:0000313|Proteomes:UP000000328};
RX PubMed=20567260; DOI=10.1038/cr.2010.87;
RA Zhao W., Zhong Y., Yuan H., Wang J., Zheng H., Wang Y., Cen X., Xu F.,
RA Bai J., Han X., Lu G., Zhu Y., Shao Z., Yan H., Li C., Peng N., Zhang Z.,
RA Zhang Y., Lin W., Fan Y., Qin Z., Hu Y., Zhu B., Wang S., Ding X.,
RA Zhao G.P.;
RT "Complete genome sequence of the rifamycin SV-producing Amycolatopsis
RT mediterranei U32 revealed its genetic characteristics in phylogeny and
RT metabolism.";
RL Cell Res. 20:1096-1108(2010).
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; CP002000; ADJ48500.1; -; Genomic_DNA.
DR RefSeq; WP_013228546.1; NC_014318.1.
DR RefSeq; YP_003768902.1; NC_014318.1.
DR AlphaFoldDB; A0A0H3DC15; -.
DR KEGG; amd:AMED_6776; -.
DR PATRIC; fig|749927.5.peg.7048; -.
DR eggNOG; COG2115; Bacteria.
DR HOGENOM; CLU_060750_0_0_11; -.
DR OrthoDB; 9763981at2; -.
DR Proteomes; UP000000328; 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; IPR013453; XylA_actinobac.
DR InterPro; IPR001998; Xylose_isomerase.
DR NCBIfam; TIGR02631; xylA_Arthro; 1.
DR PANTHER; PTHR12110; HYDROXYPYRUVATE ISOMERASE; 1.
DR PANTHER; PTHR12110:SF59; 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}; Reference proteome {ECO:0000313|Proteomes:UP000000328};
KW Xylose metabolism {ECO:0000256|HAMAP-Rule:MF_00455,
KW ECO:0000256|RuleBase:RU000609}.
FT DOMAIN 42..306
FT /note="Xylose isomerase-like TIM barrel"
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 BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 218
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
SQ SEQUENCE 382 AA; 42369 MW; 51F4D6A0D0023310 CRC64;
MSDFAPQPAD KFTFGLWTVG WPANDPFGVA TRPPLDPVES VHRLAELGAY GVTFHDDDLL
ATEPDRDKAI ERFRKALAET GLKVPMATTN LFTHPVFKDG GLTSNDRDIR RYALRKVRRN
LDLAAELGAQ TYVVWGGREG AESDAAKDVR AALDRYKEGL DLLADYVVEK GYSLRFALEP
KPNEPRGDIL LPTIGHALGF ISQLARPEMF GLNPEVGHEQ MAGLNFVHGI SQALWQGKLF
HIDLNGQHGP KFDQDLIFGH GDLKSAFFLV DLLENAGYDG PRHFDYKPMR TEDAEDVWVS
AAANMRTYLI LKEKSAAFRA DPEVVEALAA SRVPDLSTPT LAPGETFDDV LNDEFDLEAA
AARGYHFTRL NQLALEHLLG VR
//
