P37254 (PABS_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aminodeoxychorismate synthase
Short name=ADC synthase
EC=2.6.1.85

Alternative name(s):
P-aminobenzoic acid synthase
Short name=PABA synthase
Para-aminobenzoate synthase

Gene names

Name:	ABZ1
Ordered Locus Names:	YNR033W
ORF Names:	N3286

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	787 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from chorismate and glutamine. Required for the synthesis of 4-aminobenzoate (PABA), an important component in tetrahydrofolate biosynthesis. Ref.1
Catalytic activity	Chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate.
Pathway	Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 1/2.
Subcellular location	Cytoplasm Ref.6.
Domain	The PABA component provides the glutamine amidotransferase activity. The PABB component catalyzes the formation of ADC by binding chorismate and ammonia.
Miscellaneous	Present with 1550 molecules/cell in log phase SD medium.
Sequence similarities	In the C-terminal section; belongs to the anthranilate synthase component I family. Contains 1 glutamine amidotransferase type-1 domain.
Sequence caution	The sequence AAA34840.1 differs from that shown. Reason: Frameshift at positions 581, 586, 591, 716, 729 and 734. The sequence AAB49319.1 differs from that shown. Reason: Frameshift at positions 581, 586 and 591.

Ontologies

Keywords
Biological process	Folate biosynthesis
Cellular component	Cytoplasm
Domain	Glutamine amidotransferase
Molecular function	Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	folic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW para-aminobenzoic acid biosynthetic process Inferred from mutant phenotype Ref.1. Source: SGD tetrahydrofolate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4-amino-4-deoxychorismate synthase activity Inferred from mutant phenotype Ref.1. Source: SGD oxo-acid-lyase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 787	787	Aminodeoxychorismate synthase		PRO_0000154142
Regions
	Domain	16 – 233	218	Glutamine amidotransferase type-1
	Region	304 – 787	484	PABB component
	Compositional bias	10 – 14	5	Poly-Gln
Sites
	Active site	112	1	By similarity
	Active site	207	1	By similarity
	Active site	209	1	By similarity
Experimental info
	Sequence conflict	85	1	G → D in AAT93048. Ref.5
	Sequence conflict	171	1	A → P in AAA34840. Ref.1
	Sequence conflict	171	1	A → P in AAB49319. Ref.2
	Sequence conflict	533	1	A → T in AAA34840. Ref.1
	Sequence conflict	586	1	D → Y in AAB49319. Ref.2
	Sequence conflict	590 – 591	2	CE → FV in AAA34840. Ref.1
	Sequence conflict	721	1	G → GL in AAB49319. Ref.2
	Sequence conflict	722	1	V → G in AAA34840. Ref.1
	Sequence conflict	735 – 737	3	NGD → FGF in AAA34840. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P37254 [UniParc]. Last modified February 21, 2006. Version 4. Checksum: 13117891486B5B0E	FASTA	787	88,544
	10 20 30 40 50 60 MLSDTIDTKQ QQQQLHVLFI DSYDSFTYNV VRLIEQQTDI SPGVNAVHVT TVHSDTFQSM 70 80 90 100 110 120 DQLLPLLPLF DAIVVGPGPG NPNNGAQDMG IISELFENAN GKLDEVPILG ICLGFQAMCL 130 140 150 160 170 180 AQGADVSELN TIKHGQVYEM HLNDAARACG LFSGYPDTFK STRYHSLHVN AEGIDTLLPL 190 200 210 220 230 240 CTTEDENGIL LMSAQTKNKP WFGVQYHPES CCSELGGLLV SNFLKLSFIN NVKTGRWEKK 250 260 270 280 290 300 KLNGEFSDIL SRLDRTIDRD PIYKVKEKYP KGEDTTYVKQ FEVSEDPKLT FEICNIIREE 310 320 330 340 350 360 KFVMSSSVIS ENTGEWSIIA LPNSASQVFT HYGAMKKTTV HYWQDSEISY TLLKKCLDGQ 370 380 390 400 410 420 DSDLPGSLEV IHEDKSQFWI TLGKFMENKI IDNHREIPFI GGLVGILGYE IGQYIACGRC 430 440 450 460 470 480 NDDENSLVPD AKLVFINNSI VINHKQGKLY CISLDNTFPV ALEQSLRDSF VRKKNIKQSL 490 500 510 520 530 540 SWPKYLPEEI DFIITMPDKL DYAKAFKKCQ DYMHKGDSYE MCLTTQTKVV PSAVIEPWRI 550 560 570 580 590 600 FQTLVQRNPA PFSSFFEFKD IIPRQDETPP VLCFLSTSPE RFLKWDADTC ELRPIKGTVK 610 620 630 640 650 660 KGPQMNLAKA TRILKTPKEF GENLMILDLI RNDLYELVPD VRVEEFMSVQ EYATVYQLVS 670 680 690 700 710 720 VVKAHGLTSA SKKTRYSGID VLKHSLPPGS MTGAPKKITV QLLQDKIESK LNKHVNGGAR 730 740 750 760 770 780 GVYSGVTGYW SVNSNGDWSV NIRCMYSYNG GTSWQLGAGG AITVLSTLDG ELEEMYNKLE SNLQIFM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Para-aminobenzoate synthase gene of Saccharomyces cerevisiae encodes a bifunctional enzyme." Edman J.C., Goldstein A.L., Erbe J.G. Yeast 9:669-675(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"Los1p, involved in yeast pre-tRNA splicing, positively regulates members of the SOL gene family." Shen W.-C., Stanford D.R., Hopper A.K. Genetics 143:699-712(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L15299 Genomic DNA. Translation: AAA34840.1. Frameshift. U43608 Genomic DNA. Translation: AAB49319.1. Frameshift. Z71648 Genomic DNA. Translation: CAA96313.1. AY693029 Genomic DNA. Translation: AAT93048.1. BK006947 Genomic DNA. Translation: DAA10574.1.
PIR	S63364.
RefSeq	NP_014431.1. NM_001183210.1.
3D structure databases
ProteinModelPortal	P37254.
SMR	P37254. Positions 17-224, 492-786.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6278N.
IntAct	P37254. 9 interactions.
MINT	MINT-604611.
Chemistry
DrugBank	DB00259. Sulfanilamide.
Protein family/group databases
MEROPS	C26.958.
Proteomic databases
PaxDb	P37254.
PeptideAtlas	P37254.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNR033W; YNR033W; YNR033W.
GeneID	855768.
KEGG	sce:YNR033W.
Organism-specific databases
CYGD	YNR033w.
SGD	S000005316. ABZ1.
Phylogenomic databases
eggNOG	COG0147.
GeneTree	ENSGT00620000088738.
HOGENOM	HOG000025143.
KO	K13950.
OMA	SPERFIT.
OrthoDB	EOG7PZS5V.
Enzyme and pathway databases
BioCyc	YEAST:YNR033W-MONOMER.
UniPathway	UPA00077; UER00149.
Gene expression databases
Genevestigator	P37254.
Family and domain databases
Gene3D	3.60.120.10. 1 hit.
InterPro	IPR005801. ADC_synthase. IPR006805. Anth_synth_I_N. IPR015890. Chorismate-bd_C. IPR017926. GATASE. IPR010117. PabB_fungal. IPR006221. TrpG/PapA_dom. [Graphical view]
PANTHER	PTHR11236:SF6. PTHR11236:SF6. 1 hit.
Pfam	PF04715. Anth_synt_I_N. 1 hit. PF00425. Chorismate_bind. 1 hit. PF00117. GATase. 1 hit. [Graphical view]
SUPFAM	SSF56322. SSF56322. 1 hit.
TIGRFAMs	TIGR01823. PabB-fungal. 1 hit. TIGR00566. trpG_papA. 1 hit.
PROSITE	PS51273. GATASE_TYPE_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	980214.

Entry information

Entry name

PABS_YEAST

Accession

Primary (citable) accession number: P37254
Secondary accession number(s): D6W1K8, Q02982, Q6B1Q1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	February 21, 2006
Last modified:	December 11, 2013
This is version 141 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program