ILVE1_BACSU
ID ILVE1_BACSU Reviewed; 356 AA.
AC O31461;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Branched-chain-amino-acid transaminase 1;
DE Short=BCAT 1;
DE EC=2.6.1.42;
GN Name=ilvE; Synonyms=ybgE; OrderedLocusNames=BSU02390;
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;
RA Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT Bacillus subtilis chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
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, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
CC -!- FUNCTION: Transaminates branched-chain amino acids and ketoglutarate.
CC Involved in the final step of the methionine regeneration pathway,
CC where ketomethiobutyrate (KMTB) is converted to methionine via a
CC transamination. The amino donor preference is isoleucine, leucine,
CC valine, phenylalanine, and tyrosine. {ECO:0000269|PubMed:12670965}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-
CC glutamate; Xref=Rhea:RHEA:18321, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17865, ChEBI:CHEBI:29985, ChEBI:CHEBI:57427; EC=2.6.1.42;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate +
CC L-glutamate; Xref=Rhea:RHEA:24801, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; EC=2.6.1.42;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-
CC glutamate; Xref=Rhea:RHEA:24813, ChEBI:CHEBI:11851,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57762; EC=2.6.1.42;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- ACTIVITY REGULATION: Inhibited by canaline.
CC {ECO:0000269|PubMed:12670965}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.36 mM for isoleucine (with 10 mM ketomethiobutyrate)
CC {ECO:0000269|PubMed:12670965};
CC KM=2.78 mM for leucine (with 10 mM ketomethiobutyrate)
CC {ECO:0000269|PubMed:12670965};
CC KM=2.82 mM for valine (with 10 mM alpha-ketoglutarate)
CC {ECO:0000269|PubMed:12670965};
CC KM=3.15 mM for isoleucine (with 10 mM alpha-ketoglutarate)
CC {ECO:0000269|PubMed:12670965};
CC KM=3.20 mM for valine (with 10 mM ketomethiobutyrate)
CC {ECO:0000269|PubMed:12670965};
CC KM=3.99 mM for leucine (with 10 mM alpha-ketoglutarate)
CC {ECO:0000269|PubMed:12670965};
CC Vmax=1.84 umol/min/mg enzyme toward isoleucine (with 10 mM
CC ketomethiobutyrate) {ECO:0000269|PubMed:12670965};
CC Vmax=1.87 umol/min/mg enzyme toward leucine (with 10 mM
CC ketomethiobutyrate) {ECO:0000269|PubMed:12670965};
CC Vmax=2.03 umol/min/mg enzyme toward valine (with 10 mM
CC ketomethiobutyrate) {ECO:0000269|PubMed:12670965};
CC Vmax=13.93 umol/min/mg enzyme toward valine (with 10 mM alpha-
CC ketoglutarate) {ECO:0000269|PubMed:12670965};
CC Vmax=14.58 umol/min/mg enzyme toward leucine (with 10 mM alpha-
CC ketoglutarate) {ECO:0000269|PubMed:12670965};
CC Vmax=16.61 umol/min/mg enzyme toward isoleucine (with 10 mM alpha-
CC ketoglutarate) {ECO:0000269|PubMed:12670965};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 4/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 4/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 4/4.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AB006424; BAA33137.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12033.1; -; Genomic_DNA.
DR PIR; H69750; H69750.
DR RefSeq; NP_388121.1; NC_000964.3.
DR RefSeq; WP_003246499.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; O31461; -.
DR SMR; O31461; -.
DR STRING; 224308.BSU02390; -.
DR PaxDb; O31461; -.
DR PRIDE; O31461; -.
DR EnsemblBacteria; CAB12033; CAB12033; BSU_02390.
DR GeneID; 938420; -.
DR KEGG; bsu:BSU02390; -.
DR PATRIC; fig|224308.179.peg.245; -.
DR eggNOG; COG0115; Bacteria.
DR InParanoid; O31461; -.
DR OMA; GTAWFIT; -.
DR PhylomeDB; O31461; -.
DR BioCyc; BSUB:BSU02390-MON; -.
DR BioCyc; MetaCyc:BSU02390-MON; -.
DR SABIO-RK; O31461; -.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0050048; F:L-leucine:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01557; BCAT_beta_family; 1.
DR Gene3D; 3.20.10.10; -; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR018300; Aminotrans_IV_CS.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR005786; B_amino_transII.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR033939; BCAT_family.
DR PANTHER; PTHR11825; PTHR11825; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR PIRSF; PIRSF006468; BCAT1; 1.
DR SUPFAM; SSF56752; SSF56752; 1.
DR TIGRFAMs; TIGR01123; ilvE_II; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aminotransferase;
KW Branched-chain amino acid biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..356
FT /note="Branched-chain-amino-acid transaminase 1"
FT /id="PRO_0000103288"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 356 AA; 39676 MW; 6591FC3168887DEE CRC64;
MNKLIEREKT VYYKEKPDPS SLGFGQYFTD YMFVMDYEEG IGWHHPRIAP YAPLTLDPSS
SVFHYGQAVF EGLKAYRTDD GRVLLFRPDQ NIKRLNRSCE RMSMPPLDEE LVLEALTQLV
ELEKDWVPKE KGTSLYIRPF VIATEPSLGV KASRSYTFMI VLSPVGSYYG DDQLKPVRIY
VEDEYVRAVN GGVGFAKTAG NYAASLQAQR KANELGYDQV LWLDAIEKKY VEEVGSMNIF
FVINGEAVTP ALSGSILSGV TRASAIELIR SWGIPVREER ISIDEVYAAS ARGELTEVFG
TGTAAVVTPV GELNIHGKTV IVGDGQIGDL SKKLYETITD IQLGKVKGPF NWTVEV
