ID H0GMV0_SACCK Unreviewed; 787 AA.
AC H0GMV0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=aminodeoxychorismate synthase {ECO:0000256|ARBA:ARBA00013139};
DE EC=2.6.1.85 {ECO:0000256|ARBA:ARBA00013139};
DE AltName: Full=Para-aminobenzoate synthase {ECO:0000256|ARBA:ARBA00031329};
DE AltName: Full=p-aminobenzoic acid synthase {ECO:0000256|ARBA:ARBA00031904};
GN ORFNames=VIN7_4266 {ECO:0000313|EMBL:EHN04946.1};
OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN04946.1, ECO:0000313|Proteomes:UP000009009};
RN [1] {ECO:0000313|EMBL:EHN04946.1, ECO:0000313|Proteomes:UP000009009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN04946.1,
RC ECO:0000313|Proteomes:UP000009009};
RX PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT origins.";
RL FEMS Yeast Res. 12:88-96(2012).
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:0000256|ARBA:ARBA00001000};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC aminobenzoate from chorismate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005009}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC synthase component I family. {ECO:0000256|ARBA:ARBA00005970}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHN04946.1}.
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DR EMBL; AGVY01000045; EHN04946.1; -; Genomic_DNA.
DR AlphaFoldDB; H0GMV0; -.
DR MEROPS; C26.958; -.
DR HOGENOM; CLU_006493_0_0_1; -.
DR PhylomeDB; H0GMV0; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000009009; Unassembled WGS sequence.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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; Anthranilate synthase; 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 NCBIfam; TIGR01823; PabB-fungal; 1.
DR NCBIfam; TIGR00566; trpG_papA; 1.
DR PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR PANTHER; PTHR11236:SF18; AMINODEOXYCHORISMATE SYNTHASE; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF56322; ADC synthase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 19..224
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 299..450
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 499..778
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT ACT_SITE 112
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 787 AA; 88588 MW; FBCBA43586898C86 CRC64;
MLSDTIDTKQ QQQQLHVLFI DSYDSFTYNV VRLIEQQTDI SPGVNAVHVT TVHSDTFQSM
DQLLPLLPLF DAIVVGPGPG NPNNGAQDMG IISELFENAN GKLDEVPILG ICLGFQAMCL
AQGADVSELN TIKHGQAYEM HLNDAARACG LFSGYPDTFK STRYHSLHVN AEGIDTLLPL
CTTEDENGIL LMSAQTKNKP WFGVQYHPES CCSELGGLLV SNFLKLSFIN NVKTGRWEKK
KLNGEFSDIL SRLDRTIDRD PIYKVKEKYP KGEDTTYVKQ FEVSEDPKLT FEICNIIREE
KFVMSSSVIS ENRGEWSIIA LPNSASQVFT HYGAMKKTTV HYWQDSEISY TLLKKCLDGQ
DSDLPGSLEV IHEDKSQFWI TLGKFMENKI IDNHREIPFI GGLVGILGYE IGQYIACGRC
NDDENSLVPD AKLVFINNSI VINHKQGKLY CISLDNTFPV ALEQSLRDSF VRKKDIKQSL
SWPKYLPEEI DFIITMPDKL DYAKAFKKCQ DYMHKGDSYE MCLTTQTKVV PSAVIEPWRI
FQTLVQRNPA PFSSFFEFRD IIPRQDETPP VLCFLSTSPE RFLKWDADTC ELRPIKGTVK
KGPQMNLAKA TRILKTPKEF GENLMILDLI RNDLYELVPD VRVEEFMSVE EYATVYQLVS
VVKAHGLTSA SKKTRYSGID VLKHSLPPGS MTGAPKKITV QLLQDKIESK LNKHVNGGAR
GVYSGVTGYW SVNSNGDWSV NIRCMYSYNG GTSWQLGAGG AITVLSTLDG ELEEMYTKLE
SNLQIFM
//
