ID A0A1Z9YZR7_9GAMM Unreviewed; 279 AA.
AC A0A1Z9YZR7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=aminodeoxychorismate lyase {ECO:0000256|ARBA:ARBA00035676};
DE EC=4.1.3.38 {ECO:0000256|ARBA:ARBA00035676};
GN ORFNames=CAP51_08150 {ECO:0000313|EMBL:OUY07698.1};
OS Acinetobacter populi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1582270 {ECO:0000313|EMBL:OUY07698.1, ECO:0000313|Proteomes:UP000196536};
RN [1] {ECO:0000313|EMBL:OUY07698.1, ECO:0000313|Proteomes:UP000196536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBJ7 {ECO:0000313|EMBL:OUY07698.1,
RC ECO:0000313|Proteomes:UP000196536};
RA Nemec A., Radolfova-Krizova L.;
RT "Acinetobacter populi ANC 5415 (= PBJ7), whole genome shotgun sequencing
RT project.";
RL Submitted (MAY-2017) 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 -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009320}.
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:OUY07698.1}.
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DR EMBL; NEXX01000002; OUY07698.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z9YZR7; -.
DR OrthoDB; 9805628at2; -.
DR Proteomes; UP000196536; Unassembled WGS sequence.
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 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 NCBIfam; TIGR03461; pabC_Proteo; 1.
DR PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42743:SF2; AMINODEOXYCHORISMATE LYASE; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:OUY07698.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000196536}.
SQ SEQUENCE 279 AA; 31943 MW; E32E2BCE14A92289 CRC64;
MLYLKNGDFV DQHIVSIEDR AFLYGDGCFT TARLKAGEIM LWKRHLQRLQ QAITALRINC
DIDFIKNDKE KFLQHLPDGA TGTIKILISR GTSARGYAIP NQSADIYFYY YPDAHCLTQP
VILERVGLIA ETLASSFRPL KGIKTLNRLE QIMLKSMAIQ QQWDEALCFD VEQNLVEGIS
SNCFVFIDGI WHTPDLQCTG INGIMRQEIL ARMQHYQIPH QVRIISKAEI SQIEAGFLCN
ALHPMQIMGQ LVRDQDIVQS LDRQKCLQLF ESLQLKELV
//
