MOXC_BACSU
ID MOXC_BACSU Reviewed; 442 AA.
AC O34974; Q795U8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Putative monooxygenase MoxC;
DE EC=1.14.-.-;
GN Name=moxC; Synonyms=ytnJ; OrderedLocusNames=BSU29310;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RC STRAIN=168;
RX PubMed=11423008; DOI=10.1186/gb-2001-2-6-research0019;
RA Sekowska A., Robin S., Daudin J.-J., Henaut A., Danchin A.;
RT "Extracting biological information from DNA arrays: an unexpected link
RT between arginine and methionine metabolism in Bacillus subtilis.";
RL Genome Biol. 2:RESEARCH0019.1-RESEARCH0019.12(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH FMN, AND SUBUNIT.
RG New York structural genomix research consortium (NYSGXRC);
RT "Structure of ytnj from bacillus subtilis.";
RL Submitted (MAR-2005) to the PDB data bank.
RN [5]
RP INDUCTION BY METHIONINE.
RX PubMed=16109943; DOI=10.1128/jb.187.17.6019-6030.2005;
RA Burguiere P., Fert J., Guillouard I., Auger S., Danchin A.,
RA Martin-Verstraete I.;
RT "Regulation of the Bacillus subtilis ytmI operon, involved in sulfur
RT metabolism.";
RL J. Bacteriol. 187:6019-6030(2005).
CC -!- FUNCTION: May play a role in methionine degradation. May play a role in
CC a sulfur salvage pathway. {ECO:0000269|PubMed:11423008}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.4}.
CC -!- INDUCTION: Induced when methionine is the sulfur source, but not by
CC sulfate. {ECO:0000269|PubMed:16109943}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth with methionine or methionine
CC sulfoxide as unique source of sulfur. {ECO:0000269|PubMed:11423008}.
CC -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AF008220; AAC00332.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14891.1; -; Genomic_DNA.
DR PIR; E69997; E69997.
DR RefSeq; NP_390809.1; NC_000964.3.
DR RefSeq; WP_004398733.1; NZ_JNCM01000036.1.
DR PDB; 1TVL; X-ray; 2.10 A; A=2-442.
DR PDB; 1YW1; X-ray; 2.81 A; A=1-442.
DR PDB; 6ASK; X-ray; 1.69 A; A=1-442.
DR PDB; 6ASL; X-ray; 1.90 A; A=1-442.
DR PDBsum; 1TVL; -.
DR PDBsum; 1YW1; -.
DR PDBsum; 6ASK; -.
DR PDBsum; 6ASL; -.
DR AlphaFoldDB; O34974; -.
DR SMR; O34974; -.
DR STRING; 224308.BSU29310; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB03247; Flavin mononucleotide.
DR PaxDb; O34974; -.
DR PRIDE; O34974; -.
DR EnsemblBacteria; CAB14891; CAB14891; BSU_29310.
DR GeneID; 937365; -.
DR KEGG; bsu:BSU29310; -.
DR PATRIC; fig|224308.179.peg.3185; -.
DR eggNOG; COG2141; Bacteria.
DR InParanoid; O34974; -.
DR OMA; QVEGYHL; -.
DR PhylomeDB; O34974; -.
DR BioCyc; BSUB:BSU29310-MON; -.
DR EvolutionaryTrace; O34974; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd01095; Nitrilotriacetate_monoxgenase; 1.
DR Gene3D; 3.20.20.30; -; 1.
DR InterPro; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR InterPro; IPR016215; NTA_MOA.
DR Pfam; PF00296; Bac_luciferase; 1.
DR PIRSF; PIRSF000337; NTA_MOA; 1.
DR SUPFAM; SSF51679; SSF51679; 1.
DR TIGRFAMs; TIGR03860; FMN_nitrolo; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Flavoprotein; FMN; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..442
FT /note="Putative monooxygenase MoxC"
FT /id="PRO_0000360622"
FT BINDING 58
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 95
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 145..149
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.4"
FT BINDING 217..220
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|Ref.4"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:6ASK"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:6ASK"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:6ASK"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:6ASK"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:6ASK"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 145..163
FT /evidence="ECO:0007829|PDB:6ASK"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:6ASK"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:6ASK"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 241..257
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:6ASK"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 333..344
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 349..357
FT /evidence="ECO:0007829|PDB:6ASK"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 367..379
FT /evidence="ECO:0007829|PDB:6ASK"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 395..409
FT /evidence="ECO:0007829|PDB:6ASK"
FT HELIX 422..426
FT /evidence="ECO:0007829|PDB:6ASK"
SQ SEQUENCE 442 AA; 49411 MW; 8C9D72FEB983FBF5 CRC64;
MTRADFIQFG AMIHGVGGTT DGWRHPDVDP SASTNIEFYM KKAQTAEKGL FSFIFIADGL
FISEKSIPHF LNRFEPITIL SALASVTKNI GLVGTFSTSF TEPFTISRQL MSLDHISGGR
AGWNLVTSPQ EGAARNHSKS NLPEHTERYE IAQEHLDVVR GLWNSWEHDA FIHNKKTGQF
FDQAKLHRLN HKGKYFQVEG PLNIGRSKQG EPVVFQAGSS ETGRQFAAKN ADAIFTHSNS
LEETKAFYAD VKSRAADEGR DPSSVRIFPG ISPIVADTEE EAEKKYREFA ELIPIENAVT
YLARFFDDYD LSVYPLDEPF PDIGDVGKNA FQSTTDRIKR EAKARNLTLR EVAQEMAFPR
TLFIGTPERV ASLIETWFNA EAADGFIVGS DIPGTLDAFV EKVIPILQER GLYRQDYRGG
TLRENLGLGI PQHQSVLHSS HH
