MTNE_BACSU
ID MTNE_BACSU Reviewed; 398 AA.
AC O31665;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=L-glutamine--4-(methylsulfanyl)-2-oxobutanoate aminotransferase {ECO:0000305};
DE EC=2.6.1.117 {ECO:0000269|PubMed:12670965, ECO:0000269|PubMed:24837359};
DE AltName: Full=GTK {ECO:0000303|PubMed:24837359};
DE AltName: Full=Glutamine transaminase MtnE {ECO:0000305};
GN Name=mtnE {ECO:0000303|PubMed:15102328};
GN Synonyms=mtnV {ECO:0000303|PubMed:12022921}, ykrV;
GN OrderedLocusNames=BSU13580;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP FUNCTION, AND REVIEW.
RX PubMed=12022921; DOI=10.1186/1471-2180-2-8;
RA Sekowska A., Danchin A.;
RT "The methionine salvage pathway in Bacillus subtilis.";
RL BMC Microbiol. 2:8-8(2002).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12670965; DOI=10.1128/jb.185.8.2418-2431.2003;
RA Berger B.J., English S., Chan G., Knodel M.H.;
RT "Methionine regeneration and aminotransferases in Bacillus subtilis,
RT Bacillus cereus, and Bacillus anthracis.";
RL J. Bacteriol. 185:2418-2431(2003).
RN [4]
RP PATHWAY, AND NOMENCLATURE.
RX PubMed=15102328; DOI=10.1186/1471-2180-4-9;
RA Sekowska A., Denervaud V., Ashida H., Michoud K., Haas D., Yokota A.,
RA Danchin A.;
RT "Bacterial variations on the methionine salvage pathway.";
RL BMC Microbiol. 4:9-9(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=24837359; DOI=10.1016/j.phytochem.2014.04.012;
RA Ellens K.W., Richardson L.G., Frelin O., Collins J., Ribeiro C.L.,
RA Hsieh Y.F., Mullen R.T., Hanson A.D.;
RT "Evidence that glutamine transaminase and omega-amidase potentially act in
RT tandem to close the methionine salvage cycle in bacteria and plants.";
RL Phytochemistry 113:160-169(2015).
CC -!- FUNCTION: Involved in the methylthioribose (MTR) recycling pathway
CC (PubMed:12022921, PubMed:24837359). Catalyzes the formation of
CC methionine from 2-keto-4-methylthiobutyrate (KMTB) (PubMed:12670965,
CC PubMed:24837359). {ECO:0000269|PubMed:12022921,
CC ECO:0000269|PubMed:12670965, ECO:0000269|PubMed:24837359}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylsulfanyl-2-oxobutanoate + L-glutamine = 2-
CC oxoglutaramate + L-methionine; Xref=Rhea:RHEA:30391,
CC ChEBI:CHEBI:16723, ChEBI:CHEBI:16769, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58359; EC=2.6.1.117;
CC Evidence={ECO:0000269|PubMed:12670965, ECO:0000269|PubMed:24837359};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:O84395};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.91 mM for KMTB {ECO:0000269|PubMed:24837359};
CC Note=kcat is 2.32 sec(-1). {ECO:0000269|PubMed:24837359};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 6/6. {ECO:0000305|PubMed:15102328, ECO:0000305|PubMed:24837359}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant grows more slowly than the wild
CC type strain on methylthioribose (MTR) as the sulfur source.
CC {ECO:0000269|PubMed:24837359}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. MtnE subfamily. {ECO:0000305}.
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DR EMBL; AL009126; CAB13231.1; -; Genomic_DNA.
DR PIR; F69863; F69863.
DR RefSeq; NP_389241.1; NC_000964.3.
DR RefSeq; WP_003244774.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31665; -.
DR SMR; O31665; -.
DR STRING; 224308.BSU13580; -.
DR PaxDb; O31665; -.
DR PRIDE; O31665; -.
DR EnsemblBacteria; CAB13231; CAB13231; BSU_13580.
DR GeneID; 939330; -.
DR KEGG; bsu:BSU13580; -.
DR PATRIC; fig|224308.179.peg.1475; -.
DR eggNOG; COG0436; Bacteria.
DR InParanoid; O31665; -.
DR OMA; YPHMPTG; -.
DR PhylomeDB; O31665; -.
DR BioCyc; BSUB:BSU13580-MON; -.
DR BioCyc; MetaCyc:BSU13580-MON; -.
DR BRENDA; 2.6.1.117; 658.
DR UniPathway; UPA00904; UER00879.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase; Methionine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..398
FT /note="L-glutamine--4-(methylsulfanyl)-2-oxobutanoate
FT aminotransferase"
FT /id="PRO_0000123924"
FT MOD_RES 240
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:O84395"
SQ SEQUENCE 398 AA; 44043 MW; 6F36A87062F7DA8B CRC64;
MKFEQSHVLK ELPKQFFASL VQKVNRKLAE GHDVINLGQG NPDQPTPEHI VEEMKRAVAD
PENHKYSSFR GSYRLKSAAA AFYKREYGID LDPETEVAVL FGGKAGLVEL PQCLLNPGDT
ILVPDPGYPD YWSGVTLAKA KMEMMPLVKD RAFLPDYSSI TAEIREQAKL MYLNYPNNPT
GAVATSEFFE DTVRFAAENG ICVVHDFAYG AVGFDGCKPL SFLQTEGAKD IGIEIYTLSK
TYNMAGWRVG FAVGNASVIE AINLYQDHMF VSLFRATQEA AAEALLADQT CVAEQNARYE
SRRNAWITAC REIGWDVTAP AGSFFAWLPV PEGYTSEQFS DLLLEKANVA VAAGNGFGEY
GEGYVRVGLL TSEERLKEAA YRIGKLNLFT QKSIDKTL
