GLF_MYCTU
ID GLF_MYCTU Reviewed; 399 AA.
AC P9WIQ1; 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 42.
DE RecName: Full=UDP-galactopyranose mutase {ECO:0000303|PubMed:9692181};
DE Short=UGM;
DE EC=5.4.99.9 {ECO:0000269|PubMed:9692181};
DE AltName: Full=UDP-GALP mutase;
DE AltName: Full=Uridine 5-diphosphate galactopyranose mutase;
GN Name=glf {ECO:0000303|PubMed:9692181}; OrderedLocusNames=Rv3809c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9692181; DOI=10.1016/s0962-8479(98)80005-1;
RA Weston A., Stern R.J., Lee R.E., Nassau P.M., Monsey D., Martin S.L.,
RA Scherman M.S., Besra G.S., Duncan K., McNeil M.R.;
RT "Biosynthetic origin of mycobacterial cell wall galactofuranosyl
RT residues.";
RL Tuber. Lung Dis. 78:123-131(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9784509; DOI=10.1128/iai.66.11.5099-5106.1998;
RA Chen P., Bishai W.R.;
RT "Novel selection for isoniazid (INH) resistance genes supports a role for
RT NAD+-binding proteins in mycobacterial INH resistance.";
RL Infect. Immun. 66:5099-5106(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH FAD, COFACTOR, AND
RP SUBUNIT.
RX PubMed=15843027; DOI=10.1016/j.jmb.2005.02.057;
RA Beis K., Srikannathasan V., Liu H., Fullerton S.W., Bamford V.A.,
RA Sanders D.A., Whitfield C., McNeil M.R., Naismith J.H.;
RT "Crystal structures of Mycobacteria tuberculosis and Klebsiella pneumoniae
RT UDP-galactopyranose mutase in the oxidised state and Klebsiella pneumoniae
RT UDP-galactopyranose mutase in the (active) reduced state.";
RL J. Mol. Biol. 348:971-982(2005).
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.
CC {ECO:0000269|PubMed:9692181}.
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; Evidence={ECO:0000269|PubMed:9692181};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:15843027};
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC {ECO:0000305|PubMed:9692181}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15843027}.
CC -!- SIMILARITY: Belongs to the UDP-galactopyranose/dTDP-fucopyranose mutase
CC family. {ECO:0000305}.
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DR EMBL; U96128; AAC46190.1; -; Genomic_DNA.
DR EMBL; AF026540; AAC69358.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46638.1; -; Genomic_DNA.
DR PIR; E70888; E70888.
DR RefSeq; NP_218326.1; NC_000962.3.
DR RefSeq; WP_003420798.1; NZ_NVQJ01000022.1.
DR PDB; 1V0J; X-ray; 2.25 A; A/B/C/D=1-399.
DR PDB; 4RPG; X-ray; 2.40 A; A/B/C=1-399.
DR PDB; 4RPH; X-ray; 2.60 A; A/B/C=1-399.
DR PDB; 4RPJ; X-ray; 2.50 A; A/B/C=1-399.
DR PDB; 4RPK; X-ray; 2.55 A; A/B/C=1-399.
DR PDB; 4RPL; X-ray; 2.25 A; A/B/C=1-399.
DR PDBsum; 1V0J; -.
DR PDBsum; 4RPG; -.
DR PDBsum; 4RPH; -.
DR PDBsum; 4RPJ; -.
DR PDBsum; 4RPK; -.
DR PDBsum; 4RPL; -.
DR AlphaFoldDB; P9WIQ1; -.
DR SMR; P9WIQ1; -.
DR STRING; 83332.Rv3809c; -.
DR BindingDB; P9WIQ1; -.
DR ChEMBL; CHEMBL4450; -.
DR DrugBank; DB03709; Bicine.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugCentral; P9WIQ1; -.
DR PaxDb; P9WIQ1; -.
DR DNASU; 886142; -.
DR GeneID; 886142; -.
DR KEGG; mtu:Rv3809c; -.
DR PATRIC; fig|83332.111.peg.4234; -.
DR TubercuList; Rv3809c; -.
DR eggNOG; COG0562; Bacteria.
DR OMA; INVHKYG; -.
DR PhylomeDB; P9WIQ1; -.
DR BioCyc; MetaCyc:G185E-8105-MON; -.
DR BRENDA; 5.4.99.9; 3445.
DR UniPathway; UPA00963; -.
DR PRO; PR:P9WIQ1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0008767; F:UDP-galactopyranose mutase activity; IDA:MTBBASE.
DR GO; GO:0071766; P:Actinobacterium-type cell wall biogenesis; IDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; FAD; Flavoprotein;
KW Isomerase; Reference proteome.
FT CHAIN 1..399
FT /note="UDP-galactopyranose mutase"
FT /id="PRO_0000420735"
FT BINDING 18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15843027"
FT BINDING 38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15843027"
FT BINDING 46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15843027"
FT BINDING 66
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15843027"
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:0000269|PubMed:15843027"
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:0000269|PubMed:15843027"
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:0000269|PubMed:15843027"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4RPL"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:4RPL"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:4RPL"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 141..149
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1V0J"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4RPL"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 204..211
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:4RPL"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 260..273
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 310..319
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:4RPG"
FT HELIX 333..353
FT /evidence="ECO:0007829|PDB:4RPL"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 359..363
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 369..382
FT /evidence="ECO:0007829|PDB:4RPL"
FT HELIX 384..390
FT /evidence="ECO:0007829|PDB:4RPL"
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
