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P37254 (PABS_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length787 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 787787Aminodeoxychorismate synthase
PRO_0000154142

Regions

Domain16 – 233218Glutamine amidotransferase type-1
Region304 – 787484PABB component
Compositional bias10 – 145Poly-Gln

Sites

Active site1121 By similarity
Active site2071 By similarity
Active site2091 By similarity

Experimental info

Sequence conflict851G → D in AAT93048. Ref.5
Sequence conflict1711A → P in AAA34840. Ref.1
Sequence conflict1711A → P in AAB49319. Ref.2
Sequence conflict5331A → T in AAA34840. Ref.1
Sequence conflict5861D → Y in AAB49319. Ref.2
Sequence conflict590 – 5912CE → FV in AAA34840. Ref.1
Sequence conflict7211G → GL in AAB49319. Ref.2
Sequence conflict7221V → G in AAA34840. Ref.1
Sequence conflict735 – 7373NGD → FGF in AAA34840. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P37254 [UniParc].

Last modified February 21, 2006. Version 4.
Checksum: 13117891486B5B0E

FASTA78788,544
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
PIRS63364.
RefSeqNP_014431.1. NM_001183210.1.

3D structure databases

ProteinModelPortalP37254.
SMRP37254. Positions 17-224, 492-786.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35858. 46 interactions.
DIPDIP-6278N.
IntActP37254. 9 interactions.
MINTMINT-604611.

Chemistry

DrugBankDB00259. Sulfanilamide.

Protein family/group databases

MEROPSC26.958.

Proteomic databases

PaxDbP37254.
PeptideAtlasP37254.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNR033W; YNR033W; YNR033W.
GeneID855768.
KEGGsce:YNR033W.

Organism-specific databases

CYGDYNR033w.
SGDS000005316. ABZ1.

Phylogenomic databases

eggNOGCOG0147.
GeneTreeENSGT00620000088738.
HOGENOMHOG000025143.
KOK13950.
OMASPERFIT.
OrthoDBEOG7PZS5V.

Enzyme and pathway databases

BioCycYEAST:YNR033W-MONOMER.
UniPathwayUPA00077; UER00149.

Gene expression databases

GenevestigatorP37254.

Family and domain databases

Gene3D3.60.120.10. 1 hit.
InterProIPR005801. ADC_synthase.
IPR006805. Anth_synth_I_N.
IPR015890. Chorismate-bd_C.
IPR017926. GATASE.
IPR010117. PabB_fungal.
IPR006221. TrpG/PapA_dom.
[Graphical view]
PANTHERPTHR11236:SF6. PTHR11236:SF6. 1 hit.
PfamPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SUPFAMSSF56322. SSF56322. 1 hit.
TIGRFAMsTIGR01823. PabB-fungal. 1 hit.
TIGR00566. trpG_papA. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio980214.

Entry information

Entry namePABS_YEAST
AccessionPrimary (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: February 19, 2014
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways