DLYKI_BACSU
ID DLYKI_BACSU Reviewed; 167 AA.
AC P96578;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Probable D-lyxose ketol-isomerase {ECO:0000250|UniProtKB:A3E7Z6};
DE EC=5.3.1.15 {ECO:0000250|UniProtKB:A3E7Z6};
DE AltName: Full=D-lyxose isomerase {ECO:0000250|UniProtKB:A3E7Z6};
GN Name=ydaE; OrderedLocusNames=BSU04200;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT subtilis genome.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3] {ECO:0007744|PDB:2Y0O}
RP X-RAY CRYSTALLOGRAPHY (1.23 ANGSTROMS) IN COMPLEX WITH ZINC, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=21520290; DOI=10.1002/prot.23028;
RA Marles-Wright J., Lewis R.J.;
RT "The structure of a D-lyxose isomerase from the sigmaB regulon of Bacillus
RT subtilis.";
RL Proteins 79:2015-2019(2011).
CC -!- FUNCTION: Sugar isomerase that catalyzes the reversible isomerization
CC of D-lyxose to D-xylulose. {ECO:0000250|UniProtKB:A3E7Z6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-lyxose = D-xylulose; Xref=Rhea:RHEA:14201,
CC ChEBI:CHEBI:16789, ChEBI:CHEBI:17140; EC=5.3.1.15;
CC Evidence={ECO:0000250|UniProtKB:A3E7Z6};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A3E7Z6};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21520290}.
CC -!- SIMILARITY: Belongs to the D-lyxose ketol-isomerase family.
CC {ECO:0000305}.
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DR EMBL; AB001488; BAA19258.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12227.1; -; Genomic_DNA.
DR PIR; E69768; E69768.
DR RefSeq; NP_388301.1; NC_000964.3.
DR RefSeq; WP_003234400.1; NZ_JNCM01000031.1.
DR PDB; 2Y0O; X-ray; 1.23 A; A=1-167.
DR PDBsum; 2Y0O; -.
DR AlphaFoldDB; P96578; -.
DR SMR; P96578; -.
DR STRING; 224308.BSU04200; -.
DR PaxDb; P96578; -.
DR PRIDE; P96578; -.
DR EnsemblBacteria; CAB12227; CAB12227; BSU_04200.
DR GeneID; 938182; -.
DR KEGG; bsu:BSU04200; -.
DR PATRIC; fig|224308.179.peg.446; -.
DR eggNOG; COG1917; Bacteria.
DR InParanoid; P96578; -.
DR OMA; TFRCRWG; -.
DR BioCyc; BSUB:BSU04200-MON; -.
DR BRENDA; 5.3.1.15; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0047828; F:D-lyxose ketol-isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Isomerase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..167
FT /note="Probable D-lyxose ketol-isomerase"
FT /id="PRO_0000049486"
FT BINDING 69
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000305|PubMed:21520290,
FT ECO:0007744|PDB:2Y0O"
FT BINDING 71
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000305|PubMed:21520290,
FT ECO:0007744|PDB:2Y0O"
FT BINDING 82
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000305|PubMed:21520290,
FT ECO:0007744|PDB:2Y0O"
FT BINDING 137
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000305|PubMed:21520290,
FT ECO:0007744|PDB:2Y0O"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:2Y0O"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:2Y0O"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2Y0O"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:2Y0O"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:2Y0O"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:2Y0O"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2Y0O"
FT STRAND 82..98
FT /evidence="ECO:0007829|PDB:2Y0O"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:2Y0O"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:2Y0O"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:2Y0O"
FT STRAND 137..153
FT /evidence="ECO:0007829|PDB:2Y0O"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2Y0O"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:2Y0O"
SQ SEQUENCE 167 AA; 19252 MW; 16154473125D5CBD CRC64;
MGITKEEVNS YYQKAGIVLT DEEVDQIQLM DYGLGKERKV GLQLFVYVNT DRYCSKELVL
FPGQTCPEHR HPPVDGQEGK QETFRCRYGK VYLYVEGEKT PLPKVLPPQE DREHYTVWHE
IELEPGGQYT IPPNTKHWFQ AGEEGAVVTE MSSTSTDKHD IFTDPRI
