ID   ULAE_MYCPN              Reviewed;         305 AA.
AC   P75294;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Probable L-ribulose-5-phosphate 3-epimerase UlaE;
DE            EC=5.1.3.22;
DE   AltName: Full=L-ascorbate utilization protein E;
DE   AltName: Full=L-xylulose-5-phosphate 3-epimerase;
GN   Name=ulaE; Synonyms=sgaU; OrderedLocusNames=MPN_492; ORFNames=MP350;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS   (Mycoplasmoides pneumoniae).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
CC   -!- FUNCTION: Catalyzes the isomerization of L-xylulose-5-phosphate to L-
CC       ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate
CC       utilization (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ribulose 5-phosphate = L-xylulose 5-phosphate;
CC         Xref=Rhea:RHEA:18497, ChEBI:CHEBI:57829, ChEBI:CHEBI:58226;
CC         EC=5.1.3.22;
CC   -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose 5-
CC       phosphate from L-ascorbate: step 3/4.
CC   -!- SIMILARITY: Belongs to the L-ribulose-5-phosphate 3-epimerase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U00089; AAB95998.1; -; Genomic_DNA.
DR   PIR; S73676; S73676.
DR   RefSeq; NP_110180.1; NC_000912.1.
DR   RefSeq; WP_010874848.1; NZ_OU342337.1.
DR   AlphaFoldDB; P75294; -.
DR   SMR; P75294; -.
DR   IntAct; P75294; 3.
DR   STRING; 272634.MPN_492; -.
DR   EnsemblBacteria; AAB95998; AAB95998; MPN_492.
DR   GeneID; 66608836; -.
DR   KEGG; mpn:MPN_492; -.
DR   PATRIC; fig|272634.6.peg.532; -.
DR   HOGENOM; CLU_082738_0_0_14; -.
DR   OrthoDB; 3185623at2; -.
DR   BioCyc; MPNE272634:G1GJ3-808-MONOMER; -.
DR   UniPathway; UPA00263; UER00379.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:InterPro.
DR   GO; GO:0034015; F:L-ribulose-5-phosphate 3-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1.
DR   InterPro; IPR004560; L-Ru-5P_3-Epase.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   NCBIfam; TIGR00542; hxl6Piso_put; 1.
DR   PANTHER; PTHR12110; HYDROXYPYRUVATE ISOMERASE; 1.
DR   PANTHER; PTHR12110:SF21; XYLOSE ISOMERASE-LIKE TIM BARREL DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   SUPFAM; SSF51658; Xylose isomerase-like; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome.
FT   CHAIN           1..305
FT                   /note="Probable L-ribulose-5-phosphate 3-epimerase UlaE"
FT                   /id="PRO_0000097717"
SQ   SEQUENCE   305 AA;  34888 MW;  DCDB9D0709CBA51B CRC64;
     MLVIHFKPYN NLKMSFTSTE NKHLLGVYEK AINNKFAWKD KIAIAKQASF DFIELSIDES
     DARLQRLDWS DTEINQLHNE LQAQTFCLNS MCLSAHRRFP LGSKNKTTVQ QGLTIFEKAC
     VLARKLGIRI IQLAAYDVYY EPHDTETERN FITNMRKVAE LAQKYAVTIA FEVMDTPFAG
     TIVRCLNLIK RIGKANILLY PDIGNLSQFS TAVFDEIALG QDKIVGFHFK DTLPKQFKEV
     PFGTGTAQFE AALKAIHQYV PTVPILIEMW SKNDPAESTV QNVAQLKQAK QFYEQQWDLA
     LKRVK
//