ID A0A1P8Y3R8_9ACTN Unreviewed; 275 AA.
AC A0A1P8Y3R8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=4-amino-4-deoxychorismate lyase {ECO:0000313|EMBL:AQA15052.1};
GN ORFNames=BV401_36280 {ECO:0000313|EMBL:AQA15052.1};
OS Streptomyces autolyticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=75293 {ECO:0000313|EMBL:AQA15052.1, ECO:0000313|Proteomes:UP000187851};
RN [1] {ECO:0000313|Proteomes:UP000187851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC0516 {ECO:0000313|Proteomes:UP000187851};
RA Yin M., Jiang M., Lu T.;
RT "Streptomyces autolyticus CGMCC0516 complete genome sequence.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts on leucine, isoleucine and valine.
CC {ECO:0000256|ARBA:ARBA00003109}.
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 -!- 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 -!- 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 -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate;
CC Xref=Rhea:RHEA:16201, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17836, ChEBI:CHEBI:58406; EC=4.1.3.38;
CC Evidence={ECO:0000256|ARBA:ARBA00035576};
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}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 4/4.
CC {ECO:0000256|ARBA:ARBA00005072}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 4/4. {ECO:0000256|ARBA:ARBA00004931}.
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC aminobenzoate from chorismate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00035633}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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; CP019458; AQA15052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8Y3R8; -.
DR STRING; 75293.BV401_36280; -.
DR KEGG; sauo:BV401_36280; -.
DR OrthoDB; 9805628at2; -.
DR Proteomes; UP000187851; Chromosome.
DR GO; GO:0008696; F:4-amino-4-deoxychorismate lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01559; ADCL_like; 1.
DR Gene3D; 3.30.470.10; -; 1.
DR Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR InterPro; IPR017824; Aminodeoxychorismate_lyase_IV.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR018300; Aminotrans_IV_CS.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
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 Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AQA15052.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004516}.
SQ SEQUENCE 275 AA; 29087 MW; B70EEB0498A1D86A CRC64;
MKPAIWLDGS LRDADSAMVS VFDHGLTVGD GVFETVKATE GQPFALTRHL RRLARSARGL
GLPEPDLDEV RRGCEEVLKA HPVPFGRLRI TYTGGISPLG SDRGTAGPTL VVALVEAARR
PDATAVITVP WARNERGALT GLKTTSYGEN VIALARAHEH GATEALFGNT VGALCEGTGT
NVFVVLDGQL HTPPLSSGCL AGITRALVLE WVGAKETDLP LEALRGAEEV FLTSTTRDVQ
AVHRVDDHTL PGAPGPVTAE ALRIFIERAA ADIDP
//
