ID D9SR73_CLOC7 Unreviewed; 439 AA.
AC D9SR73;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
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 OrderedLocusNames=Clocel_0590 {ECO:0000313|EMBL:ADL50361.1};
OS Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL50361.1, ECO:0000313|Proteomes:UP000002730};
RN [1] {ECO:0000313|EMBL:ADL50361.1, ECO:0000313|Proteomes:UP000002730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B
RC {ECO:0000313|Proteomes:UP000002730};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Hemme C.L., Woyke T.;
RT "Complete sequence of Clostridium cellulovorans 743B.";
RL Submitted (AUG-2010) 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|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.
CC {ECO:0000256|ARBA:ARBA00005765, ECO:0000256|HAMAP-Rule:MF_00455,
CC ECO:0000256|RuleBase:RU000609}.
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DR EMBL; CP002160; ADL50361.1; -; Genomic_DNA.
DR RefSeq; WP_010074860.1; NC_014393.1.
DR AlphaFoldDB; D9SR73; -.
DR SMR; D9SR73; -.
DR STRING; 573061.Clocel_0590; -.
DR KEGG; ccb:Clocel_0590; -.
DR eggNOG; COG2115; Bacteria.
DR HOGENOM; CLU_037261_1_0_9; -.
DR OrthoDB; 9763981at2; -.
DR BRENDA; 5.3.1.5; 6835.
DR Proteomes; UP000002730; 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; IPR013452; Xylose_isom_bac.
DR InterPro; IPR001998; Xylose_isomerase.
DR NCBIfam; TIGR02630; xylose_isom_A; 1.
DR PANTHER; PTHR48320; -; 1.
DR PANTHER; PTHR48320:SF1; XYLOSE ISOMERASE; 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}; Cytoplasm {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:UP000002730};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW Rule:MF_00455}.
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 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00455"
SQ SEQUENCE 439 AA; 49667 MW; 12704D1F44F2FDE7 CRC64;
MREYFANVPK IKYEGKDSKN PLAFKYYNPD EVVGGKTMKE HLRFTLSYWH TLTGAGSDPF
GVGTMLRPWD CAEDEMELAK MRMEANFELM DKLGIEYFAF HDRDIAPEGK TLADTNEKLD
EIVAYCKELM QKHGKKLLWG TANMFGNPRF VHGAATTCNA DVFAYAAAQT KKAMDVTKEL
GGENYVFWGG REGYETLLNT DLGLEQDNLA RFFQMAVDYA KKIGFTGQFL IEPKPKEPTK
HQYDFDVATV LGFLRKYNLE KYFKMNIEAN HATLAQHTFQ HEVAVARVNG VLGSLDVNQG
DPNLGWDTDQ FPTNIYDATM VMYEVLKNGG IAPGGLNFDA KTRRASFEPE DLFLSYIAGM
DTMAKGLRVA YSLLDDAVLE NNTSERYKTF SEGIGKDIVE GKVDFESLEK YALENSVISN
KSGRQEYLES VVNQYIFND
//
