ID B8ILN4_METNO Unreviewed; 295 AA.
AC B8ILN4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000256|RuleBase:RU364094};
DE Short=BCAT {ECO:0000256|RuleBase:RU364094};
DE EC=2.6.1.42 {ECO:0000256|RuleBase:RU364094};
GN Name=ilvE {ECO:0000256|RuleBase:RU364094};
GN OrderedLocusNames=Mnod_7270 {ECO:0000313|EMBL:ACL62009.1};
OS Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL62009.1, ECO:0000313|Proteomes:UP000008207};
RN [1] {ECO:0000313|EMBL:ACL62009.1, ECO:0000313|Proteomes:UP000008207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC {ECO:0000313|Proteomes:UP000008207};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts on leucine, isoleucine and valine.
CC {ECO:0000256|ARBA:ARBA00003109, ECO:0000256|RuleBase:RU364094}.
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 Evidence={ECO:0000256|ARBA:ARBA00000627,
CC ECO:0000256|RuleBase:RU364094};
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 Evidence={ECO:0000256|ARBA:ARBA00000995,
CC ECO:0000256|RuleBase:RU364094};
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 Evidence={ECO:0000256|ARBA:ARBA00001745,
CC ECO:0000256|RuleBase:RU364094};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU004516};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 4/4.
CC {ECO:0000256|ARBA:ARBA00004824, ECO:0000256|RuleBase:RU364094}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 4/4. {ECO:0000256|ARBA:ARBA00005072,
CC ECO:0000256|RuleBase:RU364094}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 4/4. {ECO:0000256|ARBA:ARBA00004931,
CC ECO:0000256|RuleBase:RU364094}.
CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009320,
CC ECO:0000256|RuleBase:RU004106}.
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DR EMBL; CP001349; ACL62009.1; -; Genomic_DNA.
DR RefSeq; WP_015933570.1; NC_011894.1.
DR AlphaFoldDB; B8ILN4; -.
DR STRING; 460265.Mnod_7270; -.
DR KEGG; mno:Mnod_7270; -.
DR eggNOG; COG0115; Bacteria.
DR HOGENOM; CLU_020844_3_1_5; -.
DR OrthoDB; 21319at2; -.
DR UniPathway; UPA00047; UER00058.
DR UniPathway; UPA00048; UER00073.
DR UniPathway; UPA00049; UER00062.
DR Proteomes; UP000008207; 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 Gene3D; 3.30.470.10; -; 1.
DR Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR018300; Aminotrans_IV_CS.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR005785; B_amino_transI.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR NCBIfam; TIGR01122; ilvE_I; 1.
DR PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42743:SF20; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE-LIKE PROTEIN 2; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU364094};
KW Aminotransferase {ECO:0000256|RuleBase:RU364094,
KW ECO:0000313|EMBL:ACL62009.1};
KW Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU364094};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004516};
KW Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW Transferase {ECO:0000256|RuleBase:RU364094, ECO:0000313|EMBL:ACL62009.1}.
SQ SEQUENCE 295 AA; 33090 MW; 447871A9D6E8B1BD CRC64;
MSVIPFDQRE GHIWFDGRMV PWADAKIHVL THGLHYGSCV FEGERAYGGQ IFKSTEHSAR
LRRSAELLDF EIPFSVAEID AAKALVLKES GLSDAYLRPV AWRGSEMMGV SAQHNTIHLA
IAAWEWPSYF DPATKMKGIR LDLADYRRPD PRTAPSASKA AGLYMICTIS KHRAERKGYA
DALMLDWEDN VAECTGANVF FIKDGVVHTP IADRFLDGIT RQTVIELARR RGYEVVERRI
RPEEMAGFTE CFITGSAAEV TPVSEIGPYR FQPATMTRTL MDDYSAEVQP RAKAA
//
