ULAF_MYCPN
ID ULAF_MYCPN Reviewed; 242 AA.
AC P75289;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable L-ribulose-5-phosphate 4-epimerase UlaF {ECO:0000250|UniProtKB:P39306};
DE EC=5.1.3.4 {ECO:0000250|UniProtKB:P39306};
DE AltName: Full=L-ascorbate utilization protein F {ECO:0000250|UniProtKB:P39306};
DE AltName: Full=Phosphoribulose isomerase {ECO:0000250|UniProtKB:P39306};
GN Name=ulaF {ECO:0000250|UniProtKB:P39306}; Synonyms=sgaE;
GN OrderedLocusNames=MPN_498; ORFNames=MP345;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
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-ribulose 5-phosphate to D-
CC xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate
CC utilization. {ECO:0000250|UniProtKB:P39306}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ribulose 5-phosphate = D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:22368, ChEBI:CHEBI:57737, ChEBI:CHEBI:58226;
CC EC=5.1.3.4; Evidence={ECO:0000250|UniProtKB:P39306};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P08203};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08203};
CC -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose 5-
CC phosphate from L-ascorbate: step 4/4. {ECO:0000250|UniProtKB:P39306}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC subfamily. {ECO:0000250|UniProtKB:P39306}.
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DR EMBL; U00089; AAB95992.1; -; Genomic_DNA.
DR PIR; S73671; S73671.
DR RefSeq; NP_110186.1; NC_000912.1.
DR RefSeq; WP_010874854.1; NC_000912.1.
DR AlphaFoldDB; P75289; -.
DR SMR; P75289; -.
DR STRING; 272634.MPN_498; -.
DR EnsemblBacteria; AAB95992; AAB95992; MPN_498.
DR KEGG; mpn:MPN_498; -.
DR PATRIC; fig|272634.6.peg.541; -.
DR HOGENOM; CLU_006033_5_0_14; -.
DR OMA; PIFGTTH; -.
DR BioCyc; MPNE272634:G1GJ3-815-MON; -.
DR UniPathway; UPA00263; UER00380.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Isomerase; Metal-binding; Reference proteome;
KW Zinc.
FT CHAIN 1..242
FT /note="Probable L-ribulose-5-phosphate 4-epimerase UlaF"
FT /id="PRO_0000162922"
FT ACT_SITE 124
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P08203"
FT ACT_SITE 234
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P08203"
FT BINDING 31..32
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 48..49
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 78..79
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB87"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P08203"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P08203"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P08203"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P08203"
SQ SEQUENCE 242 AA; 27092 MW; 3F326B0F364CBB8B CRC64;
MDQKMINDLK EQVFQTNLLL PKYGLVIHTW GNVSMIAPNR QFFVIKPSGV SYDKMRAQDM
VVVDLDNNVL DTNGLKPSSD TPTHALMYKH CPDIKAIVHT HSTFATSFAQ ADKPIPCLGT
THADNFFGPI PCTRALSDSE INGAYEHNTG LVILEHLKNN QVDVNACAAI LVKEHGSFVW
SNKNGKDAVD RALTLEQVAQ MALYTQMINP HMKEANPALQ QKHYNRKHGK DAYYGQDTKQ
ED
