PABC_YEAST
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 03-AUG-2022, entry version 141.
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}.
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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; Q03266; -.
DR PRIDE; Q03266; -.
DR EnsemblFungi; YMR289W_mRNA; YMR289W; YMR289W.
DR GeneID; 855333; -.
DR KEGG; sce:YMR289W; -.
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 BioCyc; YEAST:MON3O-131; -.
DR BRENDA; 4.1.3.38; 984.
DR UniPathway; UPA00077; UER00150.
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: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; -; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR043132; BCAT-like_C.
DR Pfam; PF01063; Aminotran_4; 1.
DR SUPFAM; SSF56752; SSF56752; 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
