ID   FOSX_RHILO              Reviewed;         139 AA.
AC   Q98GG1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Fosfomycin resistance protein FosX;
GN   Name=fosX; OrderedLocusNames=mlr3345;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS), FUNCTION, COFACTOR, SUBUNIT, AND
RP   MUTAGENESIS OF GLU-44.
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=14677948; DOI=10.1021/ja039307z;
RA   Fillgrove K.L., Pakhomova S., Newcomer M.E., Armstrong R.N.;
RT   "Mechanistic diversity of fosfomycin resistance in pathogenic
RT   microorganisms.";
RL   J. Am. Chem. Soc. 125:15730-15731(2003).
CC   -!- FUNCTION: Catalyzes the hydration of fosfomycin.
CC       {ECO:0000269|PubMed:14677948}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:14677948};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14677948}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the fosfomycin resistance protein family.
CC       {ECO:0000305}.
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DR   EMBL; BA000012; BAB50255.1; -; Genomic_DNA.
DR   RefSeq; WP_010911601.1; NC_002678.2.
DR   PDB; 1R9C; X-ray; 1.83 A; A/B=1-139.
DR   PDBsum; 1R9C; -.
DR   AlphaFoldDB; Q98GG1; -.
DR   SMR; Q98GG1; -.
DR   KEGG; mlo:mlr3345; -.
DR   PATRIC; fig|266835.9.peg.2664; -.
DR   eggNOG; COG0346; Bacteria.
DR   HOGENOM; CLU_121356_1_0_5; -.
DR   EvolutionaryTrace; Q98GG1; -.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   CDD; cd08364; FosX; 1.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 1.
DR   InterPro; IPR037434; FosX.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR037523; VOC.
DR   PANTHER; PTHR36113:SF1; FOSFOMYCIN RESISTANCE PROTEIN FOSX; 1.
DR   PANTHER; PTHR36113; LYASE, PUTATIVE-RELATED-RELATED; 1.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 1.
DR   PROSITE; PS51819; VOC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic resistance; Cytoplasm; Manganese; Metal-binding.
FT   CHAIN           1..139
FT                   /note="Fosfomycin resistance protein FosX"
FT                   /id="PRO_0000164047"
FT   DOMAIN          4..122
FT                   /note="VOC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   ACT_SITE        44
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305"
FT   BINDING         7
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   BINDING         69
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   BINDING         118
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   MUTAGEN         44
FT                   /note="E->G: Decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:14677948"
FT   STRAND          2..13
FT                   /evidence="ECO:0007829|PDB:1R9C"
FT   HELIX           15..26
FT                   /evidence="ECO:0007829|PDB:1R9C"
FT   STRAND          29..33
FT                   /evidence="ECO:0007829|PDB:1R9C"
FT   HELIX           34..36
FT                   /evidence="ECO:0007829|PDB:1R9C"
FT   STRAND          44..49
FT                   /evidence="ECO:0007829|PDB:1R9C"
FT   STRAND          52..58
FT                   /evidence="ECO:0007829|PDB:1R9C"
FT   STRAND          69..73
FT                   /evidence="ECO:0007829|PDB:1R9C"
FT   HELIX           76..78
FT                   /evidence="ECO:0007829|PDB:1R9C"
FT   HELIX           79..89
FT                   /evidence="ECO:0007829|PDB:1R9C"
FT   STRAND          106..110
FT                   /evidence="ECO:0007829|PDB:1R9C"
FT   STRAND          116..120
FT                   /evidence="ECO:0007829|PDB:1R9C"
FT   HELIX           124..129
FT                   /evidence="ECO:0007829|PDB:1R9C"
SQ   SEQUENCE   139 AA;  16181 MW;  8F9138A570B900F2 CRC64;
     MIEGLSHMTF IVRDLERMTR ILEGVFDARE VYASDTEQFS LSREKFFLIG DIWVAIMQGE
     KLAERSYNHI AFKIDDADFD RYAERVGKLG LDMRPPRPRV EGEGRSIYFY DDDNHMFELH
     TGTLTERLAR KAKGLEAAQ
//