ID   PABC_BACSU              Reviewed;         293 AA.
AC   P28821;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 131.
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 {ECO:0000303|PubMed:2123867}; OrderedLocusNames=BSU00760;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=ASB342;
RX   PubMed=2123867; DOI=10.1128/jb.172.12.7211-7226.1990;
RA   Slock J., Stahly D.P., Han C.-Y., Six E.W., Crawford I.P.;
RT   "An apparent Bacillus subtilis folic acid biosynthetic operon containing
RT   pab, an amphibolic trpG gene, a third gene required for synthesis of para-
RT   aminobenzoic acid, and the dihydropteroate synthase gene.";
RL   J. Bacteriol. 172:7211-7226(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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   -!- DISRUPTION PHENOTYPE: Requires p-aminobenzoic acid for growth.
CC       {ECO:0000269|PubMed:2123867}.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; M34053; AAA22696.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05311.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11852.1; -; Genomic_DNA.
DR   PIR; C37854; C37854.
DR   RefSeq; NP_387957.1; NC_000964.3.
DR   RefSeq; WP_003244544.1; NZ_JNCM01000028.1.
DR   AlphaFoldDB; P28821; -.
DR   SMR; P28821; -.
DR   STRING; 224308.BSU00760; -.
DR   PaxDb; P28821; -.
DR   PRIDE; P28821; -.
DR   EnsemblBacteria; CAB11852; CAB11852; BSU_00760.
DR   GeneID; 936944; -.
DR   KEGG; bsu:BSU00760; -.
DR   PATRIC; fig|224308.179.peg.76; -.
DR   eggNOG; COG0115; Bacteria.
DR   InParanoid; P28821; -.
DR   OMA; GEVWTST; -.
DR   PhylomeDB; P28821; -.
DR   BioCyc; BSUB:BSU00760-MON; -.
DR   BioCyc; MetaCyc:BSU00760-MON; -.
DR   UniPathway; UPA00077; UER00150.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0019752; P:carboxylic acid metabolic process; IBA:GO_Central.
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   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   3: Inferred from homology;
KW   Folate biosynthesis; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..293
FT                   /note="Aminodeoxychorismate lyase"
FT                   /id="PRO_0000103304"
FT   MOD_RES         146
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   293 AA;  33515 MW;  59D3BF98E29A0E1F CRC64;
     MIYVNGRYME EKDAVLSPFD HGFLYGIGVF ETFRLYEGCP FLLDWHIERL ERALKDLQIE
     YTVSKHEILE MLDKLLKLND IKDGNARVRL NISAGISDKG FVAQTYDKPT VLCFVNQLKP
     ESLPLQKEGK VLSIRRNTPE GSFRLKSHHY LNNMYAKREI GNDPRVEGIF LTEDGAVAEG
     IISNVFWRKG RCIYTPSLDT GILDGVTRRF IIENAKDIGL ELKTGRYELE ALLTADEAWM
     TNSVLEIIPF TKIEEVNYGS QSGEATSALQ LLYKKEIKNM IHEKGGRAWR STQ