ADCS_YEAST
ID ADCS_YEAST Reviewed; 787 AA.
AC P37254; D6W1K8; Q02982; Q6B1Q1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 4.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Aminodeoxychorismate synthase {ECO:0000305};
DE Short=ADC synthase {ECO:0000305};
DE EC=2.6.1.85 {ECO:0000269|PubMed:8346682};
DE AltName: Full=P-aminobenzoic acid synthase {ECO:0000303|PubMed:8346682};
DE Short=PABA synthase {ECO:0000303|PubMed:8346682};
DE AltName: Full=Para-aminobenzoate synthase;
GN Name=ABZ1; OrderedLocusNames=YNR033W; ORFNames=N3286;
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 [GENOMIC DNA], FUNCTION, AND DOMAIN.
RX PubMed=8346682; DOI=10.1002/yea.320090613;
RA Edman J.C., Goldstein A.L., Erbe J.G.;
RT "Para-aminobenzoate synthase gene of Saccharomyces cerevisiae encodes a
RT bifunctional enzyme.";
RL Yeast 9:669-675(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8725220; DOI=10.1093/genetics/143.2.699;
RA Shen W.-C., Stanford D.R., Hopper A.K.;
RT "Los1p, involved in yeast pre-tRNA splicing, positively regulates members
RT of the SOL gene family.";
RL Genetics 143:699-712(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
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 [7]
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: Catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC)
CC from chorismate and glutamine. Required for the synthesis of 4-
CC aminobenzoate (PABA), an important component in tetrahydrofolate
CC biosynthesis. {ECO:0000269|PubMed:8346682}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-
CC glutamate; Xref=Rhea:RHEA:11672, ChEBI:CHEBI:29748,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58406; EC=2.6.1.85;
CC Evidence={ECO:0000305|PubMed:8346682};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC aminobenzoate from chorismate: step 1/2. {ECO:0000269|PubMed:8346682}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The PABA component provides the glutamine amidotransferase
CC activity. {ECO:0000305|PubMed:8346682}.
CC -!- DOMAIN: The PABB component catalyzes the formation of ADC by binding
CC chorismate and ammonia. {ECO:0000305|PubMed:8346682}.
CC -!- MISCELLANEOUS: Present with 1550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC synthase component I family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34840.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB49319.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L15299; AAA34840.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U43608; AAB49319.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z71648; CAA96313.1; -; Genomic_DNA.
DR EMBL; AY693029; AAT93048.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10574.1; -; Genomic_DNA.
DR PIR; S63364; S63364.
DR RefSeq; NP_014431.1; NM_001183210.1.
DR AlphaFoldDB; P37254; -.
DR SMR; P37254; -.
DR BioGRID; 35858; 77.
DR DIP; DIP-6278N; -.
DR IntAct; P37254; 9.
DR MINT; P37254; -.
DR STRING; 4932.YNR033W; -.
DR MEROPS; C26.958; -.
DR iPTMnet; P37254; -.
DR MaxQB; P37254; -.
DR PaxDb; P37254; -.
DR PRIDE; P37254; -.
DR EnsemblFungi; YNR033W_mRNA; YNR033W; YNR033W.
DR GeneID; 855768; -.
DR KEGG; sce:YNR033W; -.
DR SGD; S000005316; ABZ1.
DR VEuPathDB; FungiDB:YNR033W; -.
DR eggNOG; KOG1224; Eukaryota.
DR HOGENOM; CLU_006493_0_0_1; -.
DR InParanoid; P37254; -.
DR OMA; DWSVNIR; -.
DR BioCyc; YEAST:YNR033W-MON; -.
DR UniPathway; UPA00077; UER00149.
DR PRO; PR:P37254; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P37254; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IMP:SGD.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008153; P:para-aminobenzoic acid biosynthetic process; IMP:SGD.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.60.120.10; -; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR006805; Anth_synth_I_N.
DR InterPro; IPR015890; Chorismate_C.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR010117; PabB_fungal.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR01823; PabB-fungal; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Folate biosynthesis; Glutamine amidotransferase;
KW Multifunctional enzyme; Reference proteome; Transferase.
FT CHAIN 1..787
FT /note="Aminodeoxychorismate synthase"
FT /id="PRO_0000154142"
FT DOMAIN 16..233
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT REGION 304..787
FT /note="PABB component"
FT ACT_SITE 112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT CONFLICT 85
FT /note="G -> D (in Ref. 5; AAT93048)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="A -> P (in Ref. 1; AAA34840 and 2; AAB49319)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="A -> T (in Ref. 1; AAA34840)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="D -> Y (in Ref. 2; AAB49319)"
FT /evidence="ECO:0000305"
FT CONFLICT 590..591
FT /note="CE -> FV (in Ref. 1; AAA34840)"
FT /evidence="ECO:0000305"
FT CONFLICT 721
FT /note="G -> GL (in Ref. 2; AAB49319)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="V -> G (in Ref. 1; AAA34840)"
FT /evidence="ECO:0000305"
FT CONFLICT 735..737
FT /note="NGD -> FGF (in Ref. 1; AAA34840)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 787 AA; 88544 MW; 13117891486B5B0E CRC64;
MLSDTIDTKQ QQQQLHVLFI DSYDSFTYNV VRLIEQQTDI SPGVNAVHVT TVHSDTFQSM
DQLLPLLPLF DAIVVGPGPG NPNNGAQDMG IISELFENAN GKLDEVPILG ICLGFQAMCL
AQGADVSELN TIKHGQVYEM HLNDAARACG LFSGYPDTFK STRYHSLHVN AEGIDTLLPL
CTTEDENGIL LMSAQTKNKP WFGVQYHPES CCSELGGLLV SNFLKLSFIN NVKTGRWEKK
KLNGEFSDIL SRLDRTIDRD PIYKVKEKYP KGEDTTYVKQ FEVSEDPKLT FEICNIIREE
KFVMSSSVIS ENTGEWSIIA LPNSASQVFT HYGAMKKTTV HYWQDSEISY TLLKKCLDGQ
DSDLPGSLEV IHEDKSQFWI TLGKFMENKI IDNHREIPFI GGLVGILGYE IGQYIACGRC
NDDENSLVPD AKLVFINNSI VINHKQGKLY CISLDNTFPV ALEQSLRDSF VRKKNIKQSL
SWPKYLPEEI DFIITMPDKL DYAKAFKKCQ DYMHKGDSYE MCLTTQTKVV PSAVIEPWRI
FQTLVQRNPA PFSSFFEFKD IIPRQDETPP VLCFLSTSPE RFLKWDADTC ELRPIKGTVK
KGPQMNLAKA TRILKTPKEF GENLMILDLI RNDLYELVPD VRVEEFMSVQ EYATVYQLVS
VVKAHGLTSA SKKTRYSGID VLKHSLPPGS MTGAPKKITV QLLQDKIESK LNKHVNGGAR
GVYSGVTGYW SVNSNGDWSV NIRCMYSYNG GTSWQLGAGG AITVLSTLDG ELEEMYNKLE
SNLQIFM
