ID   ULAD_MYCPN              Reviewed;         218 AA.
AC   P75293;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Probable 3-keto-L-gulonate-6-phosphate decarboxylase;
DE            Short=KGPDC;
DE            EC=4.1.1.85;
DE   AltName: Full=3-dehydro-L-gulonate-6-phosphate decarboxylase;
DE   AltName: Full=L-ascorbate utilization protein D;
GN   Name=ulaD; Synonyms=sgaH; OrderedLocusNames=MPN_493; ORFNames=MP349;
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).
RN   [2]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=9274005; DOI=10.1099/00221287-143-8-2519;
RA   Reizer J., Reizer A., Saier M.H. Jr.;
RT   "Is the ribulose monophosphate pathway widely distributed in bacteria?";
RL   Microbiology 143:2519-2520(1997).
CC   -!- FUNCTION: Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into
CC       L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-dehydro-L-gulonate 6-phosphate + H(+) = CO2 + L-xylulose 5-
CC         phosphate; Xref=Rhea:RHEA:14353, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57829, ChEBI:CHEBI:58774; EC=4.1.1.85;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Cofactor degradation; L-ascorbate degradation; D-xylulose 5-
CC       phosphate from L-ascorbate: step 2/4.
CC   -!- SIMILARITY: Belongs to the HPS/KGPDC family. KGPDC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U00089; AAB95997.1; -; Genomic_DNA.
DR   PIR; S73675; S73675.
DR   RefSeq; NP_110181.1; NC_000912.1.
DR   RefSeq; WP_010874849.1; NC_000912.1.
DR   AlphaFoldDB; P75293; -.
DR   SMR; P75293; -.
DR   IntAct; P75293; 1.
DR   STRING; 272634.MPN_493; -.
DR   PRIDE; P75293; -.
DR   EnsemblBacteria; AAB95997; AAB95997; MPN_493.
DR   KEGG; mpn:MPN_493; -.
DR   PATRIC; fig|272634.6.peg.533; -.
DR   HOGENOM; CLU_081825_0_0_14; -.
DR   OMA; WEQAQEW; -.
DR   BioCyc; MPNE272634:G1GJ3-810-MON; -.
DR   UniPathway; UPA00263; UER00378.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0033982; F:3-dehydro-L-gulonate-6-phosphate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0019854; P:L-ascorbic acid catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04726; KGPDC_HPS; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR041710; HPS/KGPDC.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..218
FT                   /note="Probable 3-keto-L-gulonate-6-phosphate
FT                   decarboxylase"
FT                   /id="PRO_0000212104"
FT   BINDING         11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         33
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            64
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   SITE            67
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   218 AA;  24133 MW;  5285E03888F1CBA4 CRC64;
     MALPLIQIAL DNLSLASALN DLAKVGDAVD VIEVGTILLT AEGVNAVKEI AKRYPHKLIV
     ADGKIADTGK VFNQMFFDAG AHFTTVICAA ELPTVKDVVT VGNSYTPIKE TQVEMTSNFT
     WEQVTQWKQV GVQQVVWHRS RDAQAAGVNW SDKDLQAVKR LADLGFKVTV TGGITLNDIQ
     LFKDIPIYIF IAGRTIRDAS DPLQTVQQFK DEFHKYWK