ADCS_SOLLC
ID ADCS_SOLLC Reviewed; 902 AA.
AC Q6TAS3;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Aminodeoxychorismate synthase, chloroplastic {ECO:0000303|PubMed:14745019};
DE Short=ADC synthase {ECO:0000303|PubMed:14745019};
DE EC=2.6.1.85 {ECO:0000269|PubMed:14745019};
DE AltName: Full=P-aminobenzoic acid synthase {ECO:0000303|PubMed:14745019};
DE Short=PABA synthase {ECO:0000303|PubMed:14745019};
DE AltName: Full=Para-aminobenzoate synthase {ECO:0000303|PubMed:14745019};
DE Flags: Precursor;
GN Name=ADCS {ECO:0000303|PubMed:14745019}; OrderedLocusNames=Solyc04g049360;
GN ORFNames=LOC543912 {ECO:0000312|EMBL:CM001067};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. MicroTom;
RX PubMed=14745019; DOI=10.1073/pnas.0308331100;
RA Basset G.J.C., Quinlivan E.P., Ravanel S., Rebeille F., Nichols B.P.,
RA Shinozaki K., Seki M., Adams-Phillips L.C., Giovannoni J.J., Gregory J.F.,
RA Hanson A.D.;
RT "Folate synthesis in plants: the p-aminobenzoate branch is initiated by a
RT bifunctional PabA-PabB protein that is targeted to plastids.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1496-1501(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the biosynthesis of 4-
CC amino-4-deoxychorismate (ADC) from chorismate and glutamine
CC (PubMed:14745019). In the first step, a glutamine amidotransferase
CC generates ammonia that is channelled between the binding sites of
CC glutamine and chorismate and used along with chorismate in the second
CC step, catalyzed by aminodeoxychorismate synthase, to produce ADC
CC (PubMed:14745019). Required for the synthesis of 4-aminobenzoate
CC (PABA), an important component in tetrahydrofolate biosynthesis
CC (PubMed:14745019). Does not possess ADC lyase activity
CC (PubMed:14745019). {ECO:0000269|PubMed:14745019}.
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:0000269|PubMed:14745019};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC aminobenzoate from chorismate: step 1/2. {ECO:0000269|PubMed:14745019}.
CC -!- PATHWAY: Antibiotic biosynthesis; candicidin biosynthesis.
CC {ECO:0000269|PubMed:14745019}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:14745019}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:14745019}.
CC -!- DEVELOPMENTAL STAGE: During fruit development, expression is detected
CC at mature green and breaker stages, and then drop dramatically beneath
CC detection limit at ripe and red-ripe stages.
CC {ECO:0000269|PubMed:14745019}.
CC -!- DOMAIN: The PABA component provides the glutamine amidotransferase
CC activity. {ECO:0000250|UniProtKB:Q8LPN3}.
CC -!- DOMAIN: The PABB component catalyzes the formation of ADC by binding
CC chorismate and ammonia. {ECO:0000250|UniProtKB:Q8LPN3}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC synthase component I family. {ECO:0000305}.
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DR EMBL; AY425708; AAR83121.1; -; mRNA.
DR EMBL; CM001067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001234467.1; NM_001247538.1.
DR RefSeq; XP_010319690.1; XM_010321388.2.
DR RefSeq; XP_010319691.1; XM_010321389.2.
DR RefSeq; XP_010319692.1; XM_010321390.2.
DR AlphaFoldDB; Q6TAS3; -.
DR SMR; Q6TAS3; -.
DR STRING; 4081.Solyc04g049360.2.1; -.
DR PaxDb; Q6TAS3; -.
DR PRIDE; Q6TAS3; -.
DR EnsemblPlants; Solyc04g049360.3.1; Solyc04g049360.3.1; Solyc04g049360.3.
DR GeneID; 543912; -.
DR Gramene; Solyc04g049360.3.1; Solyc04g049360.3.1; Solyc04g049360.3.
DR KEGG; sly:543912; -.
DR eggNOG; KOG1224; Eukaryota.
DR HOGENOM; CLU_006493_0_2_1; -.
DR InParanoid; Q6TAS3; -.
DR OMA; DWSVNIR; -.
DR OrthoDB; 665558at2759; -.
DR PhylomeDB; Q6TAS3; -.
DR BioCyc; MetaCyc:MON-8741; -.
DR UniPathway; UPA00077; UER00149.
DR UniPathway; UPA00101; -.
DR Proteomes; UP000004994; Chromosome 4.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IDA:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; TAS:UniProtKB.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.60.120.10; -; 1.
DR InterPro; IPR005802; ADC_synth_comp_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; 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; 2.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00553; pabB; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Folate biosynthesis; Glutamine amidotransferase;
KW Multifunctional enzyme; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..902
FT /note="Aminodeoxychorismate synthase, chloroplastic"
FT /id="PRO_0000430156"
FT DOMAIN 85..332
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT REGION 415..889
FT /note="PABB component"
FT /evidence="ECO:0000250|UniProtKB:P32483"
FT ACT_SITE 171
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 902 AA; 101553 MW; 33B4788959C577B2 CRC64;
MNSAMSSSSS FMVASSCCQN LQTRKYFLLA PEPFEKIGMI DALQKYNRKE RKVFISSHLV
PGHLDASGTR KKFLHEPVPK LEFVRTLLID NYDSYTYNIF QELSIINGMP PVVIRNDEWT
WKEVYHYLYE ERTFDNIVIS PGPGSPTCPS DIGICLRLLL ECIDIPILGV CLGHQALGYV
HGAEVVHAPE PFHGRLSDIE HNGCQLFHEI PSGRSSGFKV VRYHSLVIDP KSLPKELIPI
AWTSTAETLP FQGVKRSNSF LNASKENKDI FNGMSELSDD SKDVKGGKVL MGIMHSSRPH
YGLQFHPESV ATCYGRQLFK NFRKITEDYW LLLMSTSFNE RRAHYAACMQ VPNLDPLSRS
VAKRGHLVNK LIERRTAEVD GTLNLSHPGH SVKFLKMTWK KLDCSASQVG GADNIFCELF
GDQEAKNSFW LDSSSIEKER ARFSFMGGKG GSLWKQLSFR LSNRSDRMCK GGGHLSVEDA
NGHVISKFLE DGFFDYLDKE LLSFCFDEKD YEGLPFDFYG GYIGYIGYDL KAECGVASNR
HRSKTPDACL FFTDNVIVID HQYDDIYTLS LHDGSTSTTS RLEDLEQRLL NLRAFTPRRL
QSQASRGFSV VELKSGFSAE KSREQYIKDV ENCQEFIKEG ESYELCLTTQ MRMKLGGIDS
LELYRNLRIR NPAPYAAWLN FSRENLSICC SSPERFLRLD RNAILEAKPI KGTIARGSTP
KEDEFLKLQL ECSEKDQAEN LMIVDLLRND LGRVCETGSV HVPHLMEIES YATVHTMVST
IRGKKRSDAS AIDCVRAAFP GGSMTGAPKL RSMELLDHLE NCSRGIYSGC IGFFSYNQAF
DLNIVIRTVV IHEGEASVGA GGAITALSDP NDEYEEMLLK TRAPIKAVLE HQSSIFSSDA
QK
