ID   PABC_VIBHA              Reviewed;         271 AA.
AC   Q56693;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Aminodeoxychorismate lyase;
DE            EC=4.1.3.38;
DE   AltName: Full=4-amino-4-deoxychorismate lyase;
DE            Short=ADC lyase;
DE            Short=ADCL;
GN   Name=pabC;
OS   Vibrio harveyi (Beneckea harveyi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33843 / NCIMB 1871 / 392 / MAV;
RX   PubMed=8550484; DOI=10.1128/jb.178.2.571-573.1996;
RA   Shen Z., Byers D.M.;
RT   "Isolation of Vibrio harveyi acyl carrier protein and the fabG, acpP, and
RT   fabF genes involved in fatty acid biosynthesis.";
RL   J. Bacteriol. 178:571-573(1996).
CC   -!- FUNCTION: Involved in the biosynthesis of p-aminobenzoate (PABA), a
CC       precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into
CC       4-aminobenzoate (PABA) and pyruvate (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC       aminobenzoate from chorismate: step 2/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; U39441; AAC43592.1; -; Genomic_DNA.
DR   PIR; T12054; T12054.
DR   RefSeq; WP_069687377.1; NZ_CP009467.1.
DR   AlphaFoldDB; Q56693; -.
DR   SMR; Q56693; -.
DR   STRING; 669.AL538_03880; -.
DR   GeneID; 57821880; -.
DR   PATRIC; fig|669.65.peg.2401; -.
DR   UniPathway; UPA00077; UER00150.
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   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01559; ADCL_like; 1.
DR   Gene3D; 3.20.10.10; -; 1.
DR   Gene3D; 3.30.470.10; -; 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   Pfam; PF01063; Aminotran_4; 1.
DR   SUPFAM; SSF56752; SSF56752; 1.
DR   TIGRFAMs; TIGR03461; pabC_Proteo; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
KW   Folate biosynthesis; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..271
FT                   /note="Aminodeoxychorismate lyase"
FT                   /id="PRO_0000103307"
FT   MOD_RES         140
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   271 AA;  29958 MW;  3AE5BEB9F398D1CD CRC64;
     MFWVNGLPQT HVPLGDRSFQ YGDGCFSTIK TKKGQLEHWQ AHVERMEACL TTLQIPFPDW
     RTVLDWAMSA TLKDESAGIK IHISRGCGGR GYSPSGVEGP VVTISNFSFP AHYLAWQERG
     VQLGVCETRL GIQPLLAGHK HNNRIEQVLA KAEIDGTEFA DAVTLNVQNH VIETTMANLF
     WVKDEKVFTP GLCLSGVAGV MRRKVLEYLQ SEGYSVQVAD FTLTDLLDAD EVWMCNSLLG
     VAPVSGISAP ENKIDFPIGK LTRRLQGNLN T