SCMK_BACSU
ID SCMK_BACSU Reviewed; 441 AA.
AC P54950;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=N-acetyl-S-(2-succino)cysteine monooxygenase {ECO:0000305|PubMed:29626092};
DE EC=1.14.-.- {ECO:0000305|PubMed:29626092};
DE AltName: Full=S-(2-succino)cysteine metabolism operon protein K {ECO:0000303|PubMed:29626092};
GN Name=scmK {ECO:0000303|PubMed:29626092}; Synonyms=yxeK;
GN OrderedLocusNames=BSU39520; ORFNames=LP9C;
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 / BGSC1A1;
RX PubMed=8867804; DOI=10.1093/dnares/2.6.295;
RA Yoshida K., Fujimyra M., Yanai N., Fujita Y.;
RT "Cloning and sequencing of a 23-kb region of the Bacillus subtilis genome
RT between the iol and hut operons.";
RL DNA Res. 2:295-301(1995).
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 FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=168;
RX PubMed=29626092; DOI=10.1074/jbc.ra118.002925;
RA Niehaus T.D., Folz J., McCarty D.R., Cooper A.J.L., Moraga Amador D.,
RA Fiehn O., Hanson A.D.;
RT "Identification of a metabolic disposal route for the oncometabolite S-(2-
RT succino)cysteine in Bacillus subtilis.";
RL J. Biol. Chem. 293:8255-8263(2018).
CC -!- FUNCTION: Probably catalyzes the oxygenation of the 2-position of the
CC succinyl moiety of N-acetyl-S-(2-succino)cysteine, causing a
CC spontaneous elimination reaction of the resulting hemithioketal that
CC generates oxaloacetate and N-acetylcysteine (NAC). Is involved in a S-
CC (2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to
CC grow on 2SC as a sole sulfur source, via its metabolization to
CC cysteine. {ECO:0000269|PubMed:29626092}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis.
CC {ECO:0000305|PubMed:29626092}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene almost lose the ability
CC to grow on 2SC as the sulfur source but are still able to grow on
CC sulfate. Moreover, they show a massive accumulation of N-acetyl-S-(2-
CC succino)cysteine when S2C is added to the medium.
CC {ECO:0000269|PubMed:29626092}.
CC -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; D45912; BAA08327.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15988.1; -; Genomic_DNA.
DR PIR; E70075; E70075.
DR RefSeq; NP_391831.1; NC_000964.3.
DR RefSeq; WP_003242500.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P54950; -.
DR SMR; P54950; -.
DR STRING; 224308.BSU39520; -.
DR PaxDb; P54950; -.
DR PRIDE; P54950; -.
DR EnsemblBacteria; CAB15988; CAB15988; BSU_39520.
DR GeneID; 937570; -.
DR KEGG; bsu:BSU39520; -.
DR PATRIC; fig|224308.179.peg.4277; -.
DR eggNOG; COG2141; Bacteria.
DR InParanoid; P54950; -.
DR OMA; DRDKLHT; -.
DR PhylomeDB; P54950; -.
DR BioCyc; BSUB:BSU39520-MON; -.
DR BioCyc; MetaCyc:BSU39520-MON; -.
DR UniPathway; UPA00136; -.
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 GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Flavoprotein; FMN;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..441
FT /note="N-acetyl-S-(2-succino)cysteine monooxygenase"
FT /id="PRO_0000050017"
FT BINDING 59
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:O34974"
FT BINDING 96
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:O34974"
FT BINDING 146..150
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:O34974"
FT BINDING 218..221
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:O34974"
SQ SEQUENCE 441 AA; 49339 MW; 4C7FAF8FDF34C906 CRC64;
MTSKKKQIKL GVFLAGTGHH VASWRHPDAP SDASMNLDYF KELAKTAERG KLDMLFLADS
LSIDSKSHPN VLTRFEPFTL LSALAQVTSK IGLTATASTT YSEPFHIARQ FASLDHLSNG
RAGWNVVTSS IESTALNFSG EKHLEHHLRY QRAEEFVEIV KGLWDSWEED AFIRNKETGE
FFDKEKMHEL NHKGEYFSVR GPLNVSRTPQ GQPVIIQAGS SGDGKALAAK TAEVIFTAQN
HLESAQEFYQ SIKEQAAEFG RDPEKIAIMP GIFPIIADTE EAAQAKYKEL QDLIIPSVGL
QILQNYLGGI DLSAYPLDGP LPKLDAEASN AVKSRFKLVQ EMAERDNMTI RELYKYVAGS
RGHHIFVGTP EQLADKMQEW VDTKACDGFN IMPPLLPEGI EVFVDQVVPI LQERGVFRKE
YEGTTLREHF GLEKPVNRYA K
