ID A4XSS9_PSEMY Unreviewed; 271 AA.
AC A4XSS9;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=aminodeoxychorismate lyase {ECO:0000256|ARBA:ARBA00035676};
DE EC=4.1.3.38 {ECO:0000256|ARBA:ARBA00035676};
GN OrderedLocusNames=Pmen_1631 {ECO:0000313|EMBL:ABP84395.1};
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP84395.1};
RN [1] {ECO:0000313|EMBL:ABP84395.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ymp {ECO:0000313|EMBL:ABP84395.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) 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}.
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DR EMBL; CP000680; ABP84395.1; -; Genomic_DNA.
DR AlphaFoldDB; A4XSS9; -.
DR STRING; 399739.Pmen_1631; -.
DR KEGG; pmy:Pmen_1631; -.
DR PATRIC; fig|399739.8.peg.1653; -.
DR eggNOG; COG0115; Bacteria.
DR HOGENOM; CLU_020844_2_1_6; -.
DR OrthoDB; 9805628at2; -.
DR GO; GO:0008696; F:4-amino-4-deoxychorismate lyase activity; IEA:UniProtKB-EC.
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 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:ABP84395.1}.
SQ SEQUENCE 271 AA; 29443 MW; 89FB5B1E01D628B7 CRC64;
MLSWVNGAPG EQLSVRDRGL AYGDGLFETI AVRGGRIPLL ARHMARLTEG CRRLSIPLDL
VLMESELQAF AGQLGEGVAK LIVTRGAGQR GYAPPQPCQP QRILQAAALP QYPPAHAEQG
VRLFPCATRL AEQPLLAGLK HLNRLEQVLA RAEWQGAEYA EGLMLDASGR VIEGVYSNLF
LVRGGGLVTA DLSRCGVAGV MRAEILQQAQ LLGLSIELRD VSHDELLSAD EVFLCNSLYG
IWPVTALQER HWPVGPLTRK LQAIVCDLLS K
//
