ID PABC_YEAST Reviewed; 374 AA. AC Q03266; D6W0B6; Q03531; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 147. 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=ABZ2; OrderedLocusNames=YMR289W; ORFNames=YM8021.15; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [3] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [4] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Converts 4-amino-4-deoxychorismate into 4-aminobenzoate CC (PABA) and pyruvate. {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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 768 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z49704; CAA89787.1; -; Genomic_DNA. DR EMBL; X80836; CAA56798.1; -; Genomic_DNA. DR EMBL; BK006946; DAA10190.1; -; Genomic_DNA. DR PIR; S54596; S54596. DR RefSeq; NP_014016.1; NM_001182796.1. DR PDB; 4K6N; X-ray; 1.90 A; A=1-374. DR PDBsum; 4K6N; -. DR AlphaFoldDB; Q03266; -. DR SMR; Q03266; -. DR BioGRID; 35469; 137. DR DIP; DIP-7986N; -. DR IntAct; Q03266; 2. DR MINT; Q03266; -. DR STRING; 4932.YMR289W; -. DR MaxQB; Q03266; -. DR PaxDb; 4932-YMR289W; -. DR PeptideAtlas; Q03266; -. DR EnsemblFungi; YMR289W_mRNA; YMR289W; YMR289W. DR GeneID; 855333; -. DR KEGG; sce:YMR289W; -. DR AGR; SGD:S000004902; -. DR SGD; S000004902; ABZ2. DR VEuPathDB; FungiDB:YMR289W; -. DR eggNOG; ENOG502QQMK; Eukaryota. DR HOGENOM; CLU_020844_6_0_1; -. DR InParanoid; Q03266; -. DR OMA; CYKMRVL; -. DR OrthoDB; 1429615at2759; -. DR BioCyc; YEAST:MONOMER3O-131; -. DR BRENDA; 4.1.3.38; 984. DR UniPathway; UPA00077; UER00150. DR BioGRID-ORCS; 855333; 0 hits in 10 CRISPR screens. DR PRO; PR:Q03266; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; Q03266; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0008696; F:4-amino-4-deoxychorismate lyase activity; IDA:SGD. DR GO; GO:0019752; P:carboxylic acid metabolic process; IBA:GO_Central. DR GO; GO:0046656; P:folic acid biosynthetic process; IMP:SGD. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1. DR InterPro; IPR001544; Aminotrans_IV. DR InterPro; IPR036038; Aminotransferase-like. DR InterPro; IPR043132; BCAT-like_C. DR PANTHER; PTHR42743; AMINO-ACID AMINOTRANSFERASE; 1. DR PANTHER; PTHR42743:SF24; AMINODEOXYCHORISMATE LYASE; 1. DR Pfam; PF01063; Aminotran_4; 1. DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Folate biosynthesis; Lyase; Pyridoxal phosphate; KW Reference proteome. FT CHAIN 1..374 FT /note="Aminodeoxychorismate lyase" FT /id="PRO_0000203350" FT STRAND 27..33 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 35..37 FT /evidence="ECO:0007829|PDB:4K6N" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:4K6N" FT STRAND 47..50 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 60..67 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 72..75 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 86..90 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 93..95 FT /evidence="ECO:0007829|PDB:4K6N" FT STRAND 100..103 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 108..118 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 122..135 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 144..156 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 165..174 FT /evidence="ECO:0007829|PDB:4K6N" FT STRAND 178..185 FT /evidence="ECO:0007829|PDB:4K6N" FT STRAND 191..198 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 202..207 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 208..210 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 213..221 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 223..225 FT /evidence="ECO:0007829|PDB:4K6N" FT STRAND 232..237 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 246..249 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 256..273 FT /evidence="ECO:0007829|PDB:4K6N" FT STRAND 283..289 FT /evidence="ECO:0007829|PDB:4K6N" FT STRAND 293..309 FT /evidence="ECO:0007829|PDB:4K6N" FT TURN 310..312 FT /evidence="ECO:0007829|PDB:4K6N" FT STRAND 313..319 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 321..323 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 329..336 FT /evidence="ECO:0007829|PDB:4K6N" FT STRAND 339..343 FT /evidence="ECO:0007829|PDB:4K6N" FT HELIX 347..349 FT /evidence="ECO:0007829|PDB:4K6N" FT STRAND 355..360 FT /evidence="ECO:0007829|PDB:4K6N" FT TURN 361..363 FT /evidence="ECO:0007829|PDB:4K6N" FT STRAND 364..373 FT /evidence="ECO:0007829|PDB:4K6N" SQ SEQUENCE 374 AA; 42640 MW; 560B9757F6BBBB73 CRC64; MSLMDNWKTD MESYDEGGLV ANPNFEVLAT FRYDPGFARQ SASKKEIFET PDPRLGLRDE DIRQQIINED YSSYLRVREV NSGGDLLENI QHPDAWKHDC KTIVCQRVED MLQVIYERFF LLDEQYQRIR IALSYFKIDF STSLNDLLKL LVENLINCKE GNSEYHEKIQ KMINERQCYK MRVLVSKTGD IRIEAIPMPM EPILKLTTDY DSVSTYFIKT MLNGFLIDST INWDVVVSSE PLNASAFTSF KTTSRDHYAR ARVRMQTAIN NLRGSEPTSS VSQCEILFSN KSGLLMEGSI TNVAVIQKDP NGSKKYVTPR LATGCLCGTM RHYLLRLGLI EEGDIDIGSL TVGNEVLLFN GVMGCIKGTV KTKY //