ID   GLF_MYCPN               Reviewed;         399 AA.
AC   P75499;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=UDP-galactopyranose mutase;
DE            Short=UGM;
DE            EC=5.4.99.9;
DE   AltName: Full=UDP-GALP mutase;
DE   AltName: Full=Uridine 5-diphosphate galactopyranose mutase;
GN   Name=glf; OrderedLocusNames=MPN_278; ORFNames=MP557;
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: Involved in the conversion of UDP-GalP into UDP-GalF through
CC       a 2-keto intermediate. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-alpha-D-galactose = UDP-alpha-D-galactofuranose;
CC         Xref=Rhea:RHEA:24132, ChEBI:CHEBI:66914, ChEBI:CHEBI:66915;
CC         EC=5.4.99.9;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the UDP-galactopyranose/dTDP-fucopyranose mutase
CC       family. {ECO:0000305}.
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DR   EMBL; U00089; AAB96205.1; -; Genomic_DNA.
DR   PIR; S73883; S73883.
DR   RefSeq; NP_109966.1; NC_000912.1.
DR   RefSeq; WP_010874635.1; NZ_OU342337.1.
DR   AlphaFoldDB; P75499; -.
DR   SMR; P75499; -.
DR   IntAct; P75499; 2.
DR   STRING; 272634.MPN_278; -.
DR   EnsemblBacteria; AAB96205; AAB96205; MPN_278.
DR   KEGG; mpn:MPN_278; -.
DR   PATRIC; fig|272634.6.peg.298; -.
DR   HOGENOM; CLU_042118_0_0_14; -.
DR   OrthoDB; 9769600at2; -.
DR   BioCyc; MPNE272634:G1GJ3-437-MONOMER; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0008767; F:UDP-galactopyranose mutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR   InterPro; IPR004379; UDP-GALP_mutase.
DR   InterPro; IPR015899; UDP-GalPyranose_mutase_C.
DR   NCBIfam; TIGR00031; UDP-GALP_mutase; 1.
DR   PANTHER; PTHR21197; UDP-GALACTOPYRANOSE MUTASE; 1.
DR   PANTHER; PTHR21197:SF0; UDP-GALACTOPYRANOSE MUTASE; 1.
DR   Pfam; PF03275; GLF; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Isomerase; Reference proteome.
FT   CHAIN           1..399
FT                   /note="UDP-galactopyranose mutase"
FT                   /id="PRO_0000087510"
FT   BINDING         25
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         44..45
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         71..72
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         374
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         380
FT                   /ligand="UDP-alpha-D-galactose"
FT                   /ligand_id="ChEBI:CHEBI:66914"
FT                   /evidence="ECO:0000250"
FT   BINDING         381..386
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   399 AA;  45910 MW;  53ED30655351639A CRC64;
     MTLFSFPNYV NWNKFDFIVL GAGISGIVLS HVLAQHGKSV LLLEKRNQLG GNCYDKLDET
     TGLLFHQYGP HIFHTDNQKV MDFIQPFFEL NNYQHRVGLQ LDNNLDLTLP FDFSQMRKLL
     DTKTASSLIN FFQQHFPAEK HLTLMQLQTI NFAPVQQLYQ FLKIKVYGPY SVKMWGMPLE
     QIDPSVLGRV KISLSENSSY FPTATIQGLP KGGYTKAFTK MVDHPLIDLR LNCPANLISV
     NNNQLLFANQ PITKPVVYCG LIDQLFGYCF GRLQYRSLHF EWKRYAVKQH QAYPVMNWPL
     HPTITRQVEY KQLTQEGLES NQTIVSCETP GAFREGDPRF MEPYYPLNDV SNNALFARYL
     KLANAIPNIH LLGRLALYQY IDMDRAIAQS LAKAEQLLQ
//