SCML_BACSU
ID SCML_BACSU Reviewed; 165 AA.
AC P54951;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=S-(2-succino)cysteine N-acetyltransferase {ECO:0000303|PubMed:29626092};
DE Short=2SC N-acetyltransferase {ECO:0000303|PubMed:29626092};
DE EC=2.3.1.- {ECO:0000269|PubMed:29626092};
DE AltName: Full=S-(2-succino)cysteine metabolism operon protein L {ECO:0000303|PubMed:29626092};
GN Name=scmL {ECO:0000303|PubMed:29626092};
GN Synonyms=snaB {ECO:0000303|PubMed:29626092}, yxeL;
GN OrderedLocusNames=BSU39510; ORFNames=LP9D;
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 SEQUENCE REVISION TO 162.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP DISRUPTION PHENOTYPE.
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: Catalyzes the N-acetylation of S-(2-succino)cysteine. Is
CC involved in a S-(2-succino)cysteine (2SC) degradation pathway that
CC allows B.subtilis to grow on 2SC as a sole sulfur source, via its
CC metabolization to cysteine. Moreover, 2SC is a toxic compound in
CC B.subtilis at high exogenous concentrations, and this enzyme relieves
CC 2SC toxicity via N-acetylation. {ECO:0000269|PubMed:29626092}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + S-(2-succino)-L-cysteine = CoA + H(+) + N-acetyl-
CC S-(2-succino)-L-cysteine; Xref=Rhea:RHEA:61440, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:143133,
CC ChEBI:CHEBI:144658; Evidence={ECO:0000269|PubMed:29626092};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=86.4 uM for S-(2-succino)-L-cysteine
CC {ECO:0000269|PubMed:29626092};
CC Note=kcat is 9.5 sec(-1). {ECO:0000269|PubMed:29626092};
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, in contrast to wild type, they highly accumulate 2SC
CC when grown on fumarate as the sulfur source. Addition of 2SC causes
CC growth inhibition of the deletion mutant but not the wild type grown on
CC sulfate as the sulfur source. {ECO:0000269|PubMed:29626092}.
CC -!- MISCELLANEOUS: Fumarate mediated succination of thiols increases in
CC certain tumors and in response to glucotoxicity associated with
CC diabetes. Therefore, S-(2-succino)-adducts such as S-(2-
CC succino)cysteine (2SC) are considered oncometabolites and biomarkers
CC for human disease. The demonstration of a metabolic disposal route for
CC a S-(2-succino)-compound paves the way toward the identification of
CC corresponding pathways in other species. {ECO:0000305|PubMed:29626092}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; D45912; BAA08328.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15987.2; -; Genomic_DNA.
DR PIR; F70075; F70075.
DR RefSeq; NP_391830.2; NC_000964.3.
DR RefSeq; WP_003242734.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P54951; -.
DR SMR; P54951; -.
DR STRING; 224308.BSU39510; -.
DR PaxDb; P54951; -.
DR PRIDE; P54951; -.
DR EnsemblBacteria; CAB15987; CAB15987; BSU_39510.
DR GeneID; 937563; -.
DR KEGG; bsu:BSU39510; -.
DR PATRIC; fig|224308.179.peg.4276; -.
DR eggNOG; COG0456; Bacteria.
DR InParanoid; P54951; -.
DR OMA; NIRKNAC; -.
DR PhylomeDB; P54951; -.
DR BioCyc; BSUB:BSU39510-MON; -.
DR BioCyc; MetaCyc:BSU39510-MON; -.
DR UniPathway; UPA00136; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Cysteine biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..165
FT /note="S-(2-succino)cysteine N-acetyltransferase"
FT /id="PRO_0000050018"
FT DOMAIN 3..162
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT CONFLICT 162
FT /note="R -> G (in Ref. 1; BAA08328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 165 AA; 19125 MW; B5594F5D7D143476 CRC64;
MKPRYRLAVE RDAEQLLELT LRAYEPIRKL GIRFAAAHAD LDLVLKNIRE NACYVMEEDG
RIIATITLRM PWGKQPGPYG VPHIWWFAVD PDTGKKGIGT KLLQWLEETI LRDTLKVPFV
SLGTADKHPW LIEMYERKGY VRSGEQDLGK GHITVYMKKQ LRHDL
