ILVE2_BACSU
ID ILVE2_BACSU Reviewed; 363 AA.
AC P39576;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 5.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Branched-chain-amino-acid aminotransferase 2;
DE Short=BCAT 2;
DE EC=2.6.1.42;
DE AltName: Full=Vegetative protein 85;
DE Short=VEG85;
GN Name=ilvK; Synonyms=ywaA; OrderedLocusNames=BSU38550; ORFNames=ipa-0r;
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 Glaser P., Lubochinsky B., Danchin A.;
RL Submitted (JUL-1995) 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 SEQUENCE REVISION TO 60.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [5]
RP PROTEIN SEQUENCE OF 2-10.
RC STRAIN=168 / IS58;
RX PubMed=9298659; DOI=10.1002/elps.1150180820;
RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT "First steps from a two-dimensional protein index towards a response-
RT regulation map for Bacillus subtilis.";
RL Electrophoresis 18:1451-1463(1997).
RN [6]
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 {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=2.11 mM for isoleucine (with 10 mM ketomethiobutyrate)
CC {ECO:0000269|PubMed:12670965};
CC KM=3.04 mM for leucine (with 10 mM alpha-ketoglutarate)
CC {ECO:0000269|PubMed:12670965};
CC KM=3.34 mM for valine (with 10 mM alpha-ketoglutarate)
CC {ECO:0000269|PubMed:12670965};
CC KM=4.83 mM for isoleucine (with 10 mM alpha-ketoglutarate)
CC {ECO:0000269|PubMed:12670965};
CC KM=5.68 mM for leucine (with 10 mM ketomethiobutyrate)
CC {ECO:0000269|PubMed:12670965};
CC Vmax=0.02 umol/min/mg enzyme toward isoleucine (with 10 mM
CC ketomethiobutyrate) {ECO:0000269|PubMed:12670965};
CC Vmax=0.02 umol/min/mg enzyme toward leucine (with 10 mM
CC ketomethiobutyrate) {ECO:0000269|PubMed:12670965};
CC Vmax=0.05 umol/min/mg enzyme toward valine (with 10 mM alpha-
CC ketoglutarate) {ECO:0000269|PubMed:12670965};
CC Vmax=0.1 umol/min/mg enzyme toward leucine (with 10 mM alpha-
CC ketoglutarate) {ECO:0000269|PubMed:12670965};
CC Vmax=0.23 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; Z49992; CAA90289.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15881.2; -; Genomic_DNA.
DR EMBL; X73124; CAA51556.1; -; Genomic_DNA.
DR PIR; S57763; S57763.
DR RefSeq; NP_391734.2; NC_000964.3.
DR RefSeq; WP_003244231.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P39576; -.
DR SMR; P39576; -.
DR STRING; 224308.BSU38550; -.
DR jPOST; P39576; -.
DR PaxDb; P39576; -.
DR PRIDE; P39576; -.
DR EnsemblBacteria; CAB15881; CAB15881; BSU_38550.
DR GeneID; 937372; -.
DR KEGG; bsu:BSU38550; -.
DR PATRIC; fig|224308.179.peg.4174; -.
DR eggNOG; COG0115; Bacteria.
DR InParanoid; P39576; -.
DR OMA; PVGSYYK; -.
DR PhylomeDB; P39576; -.
DR BioCyc; BSUB:BSU38550-MON; -.
DR BioCyc; MetaCyc:BSU38550-MON; -.
DR SABIO-RK; P39576; -.
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; Direct protein sequencing;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298659"
FT CHAIN 2..363
FT /note="Branched-chain-amino-acid aminotransferase 2"
FT /id="PRO_0000103272"
FT MOD_RES 197
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 60
FT /note="A -> T (in Ref. 1; CAA90289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 40292 MW; 57C599776D811DB4 CRC64;
MTKQTIRVEL TSTKKPKPDP NQLSFGRVFT DHMFVMDYAA DKGWYDPRII PYQPLSMDPA
AMVYHYGQTV FEGLKAYVSE DDHVLLFRPE KNMERLNQSN DRLCIPQIDE EQVLEGLKQL
VAIDKDWIPN AEGTSLYIRP FIIATEPFLG VAASHTYKLL IILSPVGSYY KEGIKPVKIA
VESEFVRAVK GGTGNAKTAG NYASSLKAQQ VAEEKGFSQV LWLDGIEKKY IEEVGSMNIF
FKINGEIVTP MLNGSILEGI TRNSVIALLK HWGLQVSERK IAIDEVIQAH KDGILEEAFG
TGTAAVISPV GELIWQDETL SINNGETGEI AKKLYDTITG IQKGAVADEF GWTTEVAALT
ESK
