GLF_MYCTO
ID GLF_MYCTO Reviewed; 399 AA.
AC P9WIQ0; F2GDG8; L0TDM1; O06934; Q7ARQ0; Q7D4U3;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
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=MT3916;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the interconversion through a 2-keto intermediate
CC of uridine diphosphogalactopyranose (UDP-GalP) into uridine
CC diphosphogalactofuranose (UDP-GalF) which is a key building block for
CC cell wall construction in Mycobacterium tuberculosis. {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 -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UDP-galactopyranose/dTDP-fucopyranose mutase
CC family. {ECO:0000305}.
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DR EMBL; AE000516; AAK48282.1; -; Genomic_DNA.
DR PIR; E70888; E70888.
DR RefSeq; WP_003420798.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WIQ0; -.
DR SMR; P9WIQ0; -.
DR PRIDE; P9WIQ0; -.
DR EnsemblBacteria; AAK48282; AAK48282; MT3916.
DR KEGG; mtc:MT3916; -.
DR PATRIC; fig|83331.31.peg.4213; -.
DR HOGENOM; CLU_042118_0_0_11; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0008767; F:UDP-galactopyranose mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR004379; UDP-GALP_mutase.
DR InterPro; IPR015899; UDP-GalPyranose_mutase_C.
DR Pfam; PF03275; GLF; 1.
DR TIGRFAMs; TIGR00031; UDP-GALP_mutase; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; FAD; Flavoprotein; Isomerase.
FT CHAIN 1..399
FT /note="UDP-galactopyranose mutase"
FT /id="PRO_0000427966"
FT BINDING 18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 224..225
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 367..369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 399 AA; 45814 MW; 3D475965C213C18E CRC64;
MQPMTARFDL FVVGSGFFGL TIAERVATQL DKRVLVLERR PHIGGNAYSE AEPQTGIEVH
KYGAHLFHTS NKRVWDYVRQ FTDFTDYRHR VFAMHNGQAY QFPMGLGLVS QFFGKYFTPE
QARQLIAEQA AEIDTADAQN LEEKAISLIG RPLYEAFVKG YTAKQWQTDP KELPAANITR
LPVRYTFDNR YFSDTYEGLP TDGYTAWLQN MAADHRIEVR LNTDWFDVRG QLRPGSPAAP
VVYTGPLDRY FDYAEGRLGW RTLDFEVEVL PIGDFQGTAV MNYNDLDVPY TRIHEFRHFH
PERDYPTDKT VIMREYSRFA EDDDEPYYPI NTEADRALLA TYRARAKSET ASSKVLFGGR
LGTYQYLDMH MAIASALNMY DNVLAPHLRD GVPLLQDGA
