ID   PABC_VIBCH              Reviewed;         267 AA.
AC   Q9KQI0;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   25-MAY-2022, entry version 118.
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; OrderedLocusNames=VC_2018;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF95166.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE003852; AAF95166.1; ALT_INIT; Genomic_DNA.
DR   PIR; C82128; C82128.
DR   RefSeq; NP_231652.2; NC_002505.1.
DR   RefSeq; WP_000289970.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KQI0; -.
DR   SMR; Q9KQI0; -.
DR   STRING; 243277.VC_2018; -.
DR   PRIDE; Q9KQI0; -.
DR   DNASU; 2613397; -.
DR   EnsemblBacteria; AAF95166; AAF95166; VC_2018.
DR   GeneID; 57740639; -.
DR   KEGG; vch:VC_2018; -.
DR   PATRIC; fig|243277.26.peg.1928; -.
DR   eggNOG; COG0115; Bacteria.
DR   HOGENOM; CLU_020844_2_1_6; -.
DR   OMA; VPWTRNE; -.
DR   UniPathway; UPA00077; UER00150.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008696; F:4-amino-4-deoxychorismate lyase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IBA:GO_Central.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008153; P:para-aminobenzoic acid biosynthetic process; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..267
FT                   /note="Aminodeoxychorismate lyase"
FT                   /id="PRO_0000103306"
FT   MOD_RES         140
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   267 AA;  30063 MW;  0945BE846795B1E3 CRC64;
     MYWVNGQRRN EVPIHDRSFQ YGDGCFTTIL TKEGQVQQWS SHKARLQACL DILHIPEPNW
     DRVWQGLQSM ILPQEKAGLK IHISRGLGGR GYSPTQVSES IVTISAFAFP AHYQAWRDKG
     LAVGICQQRM GLNPLLAGHK HNNRLEQILL KREMDNAGWD DGVCLDINGK VIETTAANIF
     WCRDGTMFTP CLRHAGVAGV ARRQILELAQ QQEIPIVIDE FTLEDLLSAE EVFITNALLE
     VAPVTQIGQQ RLTIGSMTRR FQESSNS