ID   YIIM_ECOLI              Reviewed;         224 AA.
AC   P32157; Q2M8K7;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   04-NOV-2026, entry version 168.
DE   RecName: Full=6-hydroxylaminopurine reductase YiiM {ECO:0000305};
DE            EC=1.-.-.- {ECO:0000269|PubMed:34921810};
DE   AltName: Full=Hydroxylaminopurine resistance protein YiiM {ECO:0000303|PubMed:29459651};
GN   Name=yiiM; OrderedLocusNames=b3910, JW5559;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA   Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT   from 87.2 to 89.2 minutes.";
RL   Nucleic Acids Res. 21:3391-3398(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   DOMAIN.
RX   PubMed=11886751; DOI=10.1111/j.1574-6968.2002.tb11028.x;
RA   Anantharaman V., Aravind L.;
RT   "MOSC domains: ancient, predicted sulfur-carrier domains, present in
RT   diverse metal-sulfur cluster biosynthesis proteins including Molybdenum
RT   cofactor sulfurases.";
RL   FEMS Microbiol. Lett. 207:55-61(2002).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / BW25113;
RX   PubMed=18312271; DOI=10.1111/j.1365-2958.2008.06128.x;
RA   Kozmin S.G., Leroy P., Pavlov Y.I., Schaaper R.M.;
RT   "YcbX and yiiM, two novel determinants for resistance of Escherichia coli
RT   to N-hydroxylated base analogues.";
RL   Mol. Microbiol. 68:51-65(2008).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC   STRAIN=K12;
RX   PubMed=34921810; DOI=10.1016/j.bbabio.2021.148523;
RA   Kalimuthu P., Harmer J.R., Baldauf M., Hassan A.H., Kruse T.,
RA   Bernhardt P.V.;
RT   "Electrochemically driven catalysis of the bacterial molybdenum enzyme
RT   YiiM.";
RL   Biochim. Biophys. Acta 1863:148523-148523(2022).
RN   [7] {ECO:0007744|PDB:1O65, ECO:0007744|PDB:1O67}
RP   X-RAY CRYSTALLOGRAPHY, AND SUBUNIT.
RX   PubMed=16021622; DOI=10.1002/prot.20541;
RA   Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA   Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA   Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA   Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA   Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA   Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA   Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA   Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA   Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT   "Structural analysis of a set of proteins resulting from a bacterial
RT   genomics project.";
RL   Proteins 60:787-796(2005).
RN   [8] {ECO:0007744|PDB:5YHI}
RP   X-RAY CRYSTALLOGRAPHY, COFACTOR, SUBUNIT, AND DOMAIN.
RX   PubMed=29459651; DOI=10.1038/s41598-018-21660-y;
RA   Namgung B., Kim J.H., Song W.S., Yoon S.I.;
RT   "Crystal structure of the hydroxylaminopurine resistance protein, YiiM, and
RT   its putative molybdenum cofactor-binding catalytic site.";
RL   Sci. Rep. 8:3304-3304(2018).
CC   -!- FUNCTION: Reductase involved in the detoxification of N-hydroxylated
CC       base analogs (PubMed:18312271). Contributes to the detoxification of 6-
CC       N-hydroxylaminopurine (HAP) by catalyzing the reduction of HAP to
CC       adenine (PubMed:18312271, PubMed:34921810). Is specific for N-
CC       hydroxylated substrates over N-oxides or sulfoxides (PubMed:34921810).
CC       In the presence of methyl viologen as reduced electron donor, it
CC       preferentially reduces N-hydroxylated compounds such as hydroxylamines,
CC       amidoximes, N-hydroxypurines and N-hydroxyureas but shows little or no
CC       activity against amine-oxides or sulfoxides (PubMed:34921810). YiiM is
CC       not involved in molybdenum cofactor (MoCo) biosynthesis or in MoCo
CC       sulfuration (PubMed:18312271). {ECO:0000269|PubMed:18312271,
CC       ECO:0000269|PubMed:34921810}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-hydroxyadenine + AH2 = adenine + A + H2O;
CC         Xref=Rhea:RHEA:84551, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16708, ChEBI:CHEBI:17499, ChEBI:CHEBI:78235;
CC         Evidence={ECO:0000269|PubMed:34921810};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84552;
CC         Evidence={ECO:0000269|PubMed:34921810};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-amino-N(6)-hydroxyadenine + AH2 = 2,6-diaminopurine + A +
CC         H2O; Xref=Rhea:RHEA:84591, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:40235, ChEBI:CHEBI:78685;
CC         Evidence={ECO:0000269|PubMed:34921810};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84592;
CC         Evidence={ECO:0000269|PubMed:34921810};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000269|PubMed:29459651, ECO:0000269|PubMed:34921810,
CC         ECO:0000305|PubMed:18312271};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=640 uM for 6-hydroxyaminopurine {ECO:0000269|PubMed:34921810};
CC         KM=460 uM for benzamidoxime {ECO:0000269|PubMed:34921810};
CC         KM=222 uM for hydroxylamine {ECO:0000269|PubMed:34921810};
CC         KM=337 uM for N-hydroxyurea {ECO:0000269|PubMed:34921810};
CC         KM=317 uM for N-hydroxyacetamidine {ECO:0000269|PubMed:34921810};
CC         KM=668 uM for 2-amino-6-hydroxyaminopurine
CC         {ECO:0000269|PubMed:34921810};
CC         KM=245 uM for nicotinamide N-oxide {ECO:0000269|PubMed:34921810};
CC       pH dependence:
CC         Optimum pH is 7.1. {ECO:0000269|PubMed:34921810};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16021622,
CC       ECO:0000269|PubMed:29459651}.
CC   -!- DOMAIN: Contains an N-terminal MOSC (MoCo sulfurase C-terminal) domain,
CC       with a conserved cysteine, and a C-terminal compact tri-helical domain
CC       (PubMed:11886751). Folds into a triangular shape, with a cavity in the
CC       middle of this triangular architecture (PubMed:29459651). The cavity
CC       holds a conserved cysteine residue (Cys-120), which may function as a
CC       catalytic site (PubMed:29459651). The molybdenum cofactor binds in the
CC       cavity (PubMed:29459651). {ECO:0000269|PubMed:11886751,
CC       ECO:0000269|PubMed:29459651}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene leads to moderately
CC       increased sensitivity to 6-N-hydroxylaminopurine (HAP) as well as
CC       significantly enhanced 2-amino-HAP (AHAP) induced mutagenesis
CC       (PubMed:18312271). The mutant is also sensitized to hydroxylamine
CC       (PubMed:18312271). The mutant shows no significant defects in
CC       molybdenum cofactor biosynthesis (PubMed:18312271).
CC       {ECO:0000269|PubMed:18312271}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB03043.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L19201; AAB03043.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76892.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77399.1; -; Genomic_DNA.
DR   PIR; S40854; S40854.
DR   RefSeq; NP_418346.2; NC_000913.3.
DR   RefSeq; WP_001270260.1; NZ_CP009789.1.
DR   PDB; 1O65; X-ray; 2.33 A; A/B/C=1-224.
DR   PDB; 1O67; X-ray; 2.54 A; A/B/C=1-224.
DR   PDB; 5YHI; X-ray; 2.85 A; A/B=1-224.
DR   AlphaFoldDB; P32157; -.
DR   SMR; P32157; -.
DR   BioGRID; 4262643; 25.
DR   BioGRID; 852703; 4.
DR   DIP; DIP-12512N; -.
DR   FunCoup; P32157; 109.
DR   IntAct; P32157; 3.
DR   STRING; 511145.b3910; -.
DR   jPOST; P32157; -.
DR   PaxDb; 511145-b3910; -.
DR   EnsemblBacteria; AAC76892; AAC76892; b3910.
DR   GeneID; 75174151; -.
DR   GeneID; 948406; -.
DR   KEGG; ecj:JW5559; -.
DR   KEGG; eco:b3910; -.
DR   KEGG; ecoc:C3026_21145; -.
DR   PATRIC; fig|1411691.4.peg.2794; -.
DR   EchoBASE; EB1816; -.
DR   eggNOG; COG2258; Bacteria.
DR   HOGENOM; CLU_082566_1_1_6; -.
DR   InParanoid; P32157; -.
DR   OMA; AAEWPQC; -.
DR   OrthoDB; 9786134at2; -.
DR   PhylomeDB; P32157; -.
DR   BioCyc; EcoCyc:EG11870-MONOMER; -.
DR   BioCyc; MetaCyc:EG11870-MONOMER; -.
DR   EvolutionaryTrace; P32157; -.
DR   PRO; PR:P32157; -.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0030151; F:molybdenum ion binding; IDA:EcoCyc.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016661; F:oxidoreductase activity, acting on other nitrogenous compounds as donors; IDA:EcoCyc.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009636; P:response to toxic substance; IMP:EcoCyc.
DR   GO; GO:0009407; P:toxin catabolic process; IMP:EcoCyc.
DR   FunFam; 2.40.33.20:FF:000001; 6-N-hydroxylaminopurine resistance protein; 1.
DR   Gene3D; 2.40.33.20; PK beta-barrel domain-like; 1.
DR   InterPro; IPR005302; MoCF_Sase_C.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   InterPro; IPR005163; Tri_helical_YiiM-like.
DR   NCBIfam; NF008577; yiiM; 1.
DR   PANTHER; PTHR30212; PROTEIN YIIM; 1.
DR   PANTHER; PTHR30212:SF2; PROTEIN YIIM; 1.
DR   Pfam; PF03473; MOSC; 1.
DR   Pfam; PF03475; YiiM_3-alpha; 1.
DR   SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR   PROSITE; PS51340; MOSC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Molybdenum; Oxidoreductase; Reference proteome.
FT   CHAIN           1..224
FT                   /note="6-hydroxylaminopurine reductase YiiM"
FT                   /id="PRO_0000169688"
FT   DOMAIN          26..163
FT                   /note="MOSC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00670"
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   STRAND          30..35
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   HELIX           52..55
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   STRAND          56..61
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   HELIX           63..71
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   HELIX           73..78
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   TURN            81..84
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   STRAND          87..92
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   TURN            95..97
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   STRAND          103..106
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   STRAND          109..116
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   HELIX           122..126
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   HELIX           132..139
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   STRAND          144..150
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   STRAND          152..155
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   STRAND          160..164
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   HELIX           171..179
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   HELIX           185..192
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   HELIX           199..211
FT                   /evidence="ECO:0007829|PDB:1O65"
FT   HELIX           218..222
FT                   /evidence="ECO:0007829|PDB:1O65"
SQ   SEQUENCE   224 AA;  25343 MW;  D9691FB9357F0E38 CRC64;
     MRYPVDVYTG KIQAYPEGKP SAIAKIQVDG ELMLTELGLE GDEQAEKKVH GGPDRALCHY
     PREHYLYWAR EFPEQAELFV APAFGENLST DGLTESNVYM GDIFRWGEAL IQVSQPRSPC
     YKLNYHFDIS DIAQLMQNTG KVGWLYSVIA PGKVSADAPL ELVSRVSDVT VQEAAAIAWH
     MPFDDDQYHR LLSAAGLSKS WTRTMQKRRL SGKIEDFSRR LWGK
//