ID A0A444Y468_ARAHY Unreviewed; 349 AA.
AC A0A444Y468;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=aminodeoxychorismate lyase {ECO:0000256|ARBA:ARBA00035676};
DE EC=4.1.3.38 {ECO:0000256|ARBA:ARBA00035676};
GN ORFNames=Ahy_B08g092532 {ECO:0000313|EMBL:RYQ96689.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYQ96689.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYQ96689.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYQ96689.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RYQ96689.1}.
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DR EMBL; SDMP01000018; RYQ96689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444Y468; -.
DR STRING; 3818.A0A444Y468; -.
DR OrthoDB; 1050601at2759; -.
DR Proteomes; UP000289738; Chromosome b08.
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; 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:SF8; OS01G0238500 PROTEIN; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
PE 4: Predicted;
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738}.
SQ SEQUENCE 349 AA; 38378 MW; 64A5DF3B8E1FCD30 CRC64;
MENHTESTTV SHSSSELGNH SDLTVHVFNS SSELLEKLHQ RWSTVEKKPY PAMYSSIYGG
IILDPAMMVI PIDDHMVHRG HGVFDTAIIL DGYLYELDVH LDRILRSAAK AKISLPFPQS
TLRSILIQLT AVSKCKKGTL RYWLSAGPGN FLLSSSGCPT PAFYAVVIDD DFSQCKEGVK
VITSTVAMKP PLFATMKNVN YLPNVLSVME AEEKGAFASI WVDEAGYIAE GPNVNVAFIT
KEKELLMPLF DSILHGCTAK RLLELAPRLV EQGILKGVTI KNVTVEEAKG AAEMMYVGST
LPLLPIIMWD DQPIGKGQVG ELTMALSDLL WNDMVAGPDT KRIPVPYIE
//
