ID A0A1J5MNH5_9GAMM Unreviewed; 274 AA.
AC A0A1J5MNH5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=aminodeoxychorismate lyase {ECO:0000256|ARBA:ARBA00035676};
DE EC=4.1.3.38 {ECO:0000256|ARBA:ARBA00035676};
GN ORFNames=BM565_02890 {ECO:0000313|EMBL:OIQ48157.1};
OS Gammaproteobacteria bacterium MedPE.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1860093 {ECO:0000313|EMBL:OIQ48157.1, ECO:0000313|Proteomes:UP000182920};
RN [1] {ECO:0000313|EMBL:OIQ48157.1, ECO:0000313|Proteomes:UP000182920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MedPE {ECO:0000313|EMBL:OIQ48157.1};
RX PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT Associated Bacteria from the Mediterranean Sea.";
RL Front. Microbiol. 7:996-996(2016).
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: 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}.
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:OIQ48157.1}.
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DR EMBL; MPDF01000011; OIQ48157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5MNH5; -.
DR STRING; 1860093.BM565_02890; -.
DR Proteomes; UP000182920; 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 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 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.
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:OIQ48157.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU004516}.
SQ SEQUENCE 274 AA; 29922 MW; BC085796F8C717F0 CRC64;
MSNTWVNGVA TNQIAVTDRG FSYGDGIFTT IKVTNARCEL LSEHLVRLQQ GITALAITQI
DFKALLDEIS NVAKSLISGV IKVVVTRGEG QRGYSSVGCD SPTIVISTSA LPVMYQDWQQ
NGVGLGVSTI ALGLNPLTAG IKHLNRLEQV LVRQQIDENQ WTDAVVLDCQ ACVIETSMAN
IFWRSGEIVY TPNLDFSGVK GLMRQQVLSD LTASNIQLVE DRFKLSSIID ADEIFMTNCL
MGIVPVVAIE SKQYHIGELT QRLQSVLNSK DTNG
//
