ADCS_ARATH
ID ADCS_ARATH Reviewed; 919 AA.
AC Q8LPN3; Q9ZV26;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Aminodeoxychorismate synthase, chloroplastic;
DE Short=ADC synthase;
DE EC=2.6.1.85;
DE AltName: Full=P-aminobenzoic acid synthase;
DE Short=PABA synthase;
DE AltName: Full=Para-aminobenzoate synthase;
DE AltName: Full=Protein EMBRYO DEFFECTIVE 1997;
DE Flags: Precursor;
GN Name=ADCS; Synonyms=EMB1997; OrderedLocusNames=At2g28880;
GN ORFNames=F8N16.17;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
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. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=16466344; DOI=10.1042/bj20051851;
RA Sahr T., Ravanel S., Basset G., Nichols B.P., Hanson A.D., Rebeille F.;
RT "Folate synthesis in plants: purification, kinetic properties, and
RT inhibition of aminodeoxychorismate synthase.";
RL Biochem. J. 396:157-162(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=20851095; DOI=10.1016/j.abb.2010.09.010;
RA Camara D., Richefeu-Contesto C., Gambonnet B., Dumas R., Rebeille F.;
RT "The synthesis of pABA: Coupling between the glutamine amidotransferase and
RT aminodeoxychorismate synthase domains of the bifunctional
RT aminodeoxychorismate synthase from Arabidopsis thaliana.";
RL Arch. Biochem. Biophys. 505:83-90(2011).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the biosynthesis of 4-
CC amino-4-deoxychorismate (ADC) from chorismate and glutamine. In the
CC first step, a glutamine amidotransferase generates ammonia that is
CC channelled between the binding sites of glutamine and chorismate and
CC used along with chorismate in the second step, catalyzed by
CC aminodeoxychorismate synthase, to produce ADC. Required for the
CC synthesis of 4-aminobenzoate (PABA), an important component in
CC tetrahydrofolate biosynthesis. Does not possess ADC lyase activity.
CC {ECO:0000269|PubMed:14745019, ECO:0000269|PubMed:16466344,
CC ECO:0000269|PubMed:20851095}.
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, ECO:0000269|PubMed:16466344,
CC ECO:0000269|PubMed:20851095};
CC -!- ACTIVITY REGULATION: Activated by chorismate and inhibited by
CC dihydrofolate and methotrexate. {ECO:0000269|PubMed:16466344,
CC ECO:0000269|PubMed:20851095}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=600 uM for L-glutamine {ECO:0000269|PubMed:16466344};
CC KM=1.5 uM for chorismate {ECO:0000269|PubMed:16466344};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC aminobenzoate from chorismate: step 1/2.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:14745019}.
CC -!- DOMAIN: The PABA component provides the glutamine amidotransferase
CC activity. {ECO:0000269|PubMed:20851095}.
CC -!- DOMAIN: The PABB component catalyzes the formation of ADC by binding
CC chorismate and ammonia. {ECO:0000269|PubMed:20851095}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC synthase component I family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79592.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BK001419; DAA01457.1; -; mRNA.
DR EMBL; AC005727; AAC79592.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC08184.1; -; Genomic_DNA.
DR EMBL; AY096797; AAM19955.1; -; mRNA.
DR EMBL; BT002702; AAO11618.1; -; mRNA.
DR PIR; A84690; A84690.
DR RefSeq; NP_850127.1; NM_179796.2.
DR AlphaFoldDB; Q8LPN3; -.
DR SMR; Q8LPN3; -.
DR BioGRID; 2787; 1.
DR IntAct; Q8LPN3; 1.
DR STRING; 3702.AT2G28880.1; -.
DR PaxDb; Q8LPN3; -.
DR PRIDE; Q8LPN3; -.
DR ProteomicsDB; 244714; -.
DR EnsemblPlants; AT2G28880.1; AT2G28880.1; AT2G28880.
DR GeneID; 817437; -.
DR Gramene; AT2G28880.1; AT2G28880.1; AT2G28880.
DR KEGG; ath:AT2G28880; -.
DR Araport; AT2G28880; -.
DR TAIR; locus:2053255; AT2G28880.
DR eggNOG; KOG1224; Eukaryota.
DR HOGENOM; CLU_006493_0_2_1; -.
DR InParanoid; Q8LPN3; -.
DR OMA; DWSVNIR; -.
DR OrthoDB; 665558at2759; -.
DR PhylomeDB; Q8LPN3; -.
DR BioCyc; ARA:AT2G28880-MON; -.
DR BioCyc; MetaCyc:AT2G28880-MON; -.
DR SABIO-RK; Q8LPN3; -.
DR UniPathway; UPA00077; UER00149.
DR PRO; PR:Q8LPN3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8LPN3; baseline and differential.
DR Genevisible; Q8LPN3; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IDA:TAIR.
DR GO; GO:0046417; P:chorismate metabolic process; IDA:TAIR.
DR GO; GO:0046656; P:folic acid biosynthetic process; NAS:TAIR.
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; 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; 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..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..919
FT /note="Aminodeoxychorismate synthase, chloroplastic"
FT /id="PRO_0000430154"
FT DOMAIN 86..342
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT REGION 436..910
FT /note="PABB component"
FT ACT_SITE 172
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 919 AA; 102920 MW; 4DC9792D1C3D111D CRC64;
MNMNFSFCST SSELSYPSEN VLRFSVASRL FSPKWKKSFI SLPCRSKTTR KVLASSRYVP
GKLEDLSVVK KSLPRREPVE KLGFVRTLLI DNYDSYTFNI YQALSTINGV PPVVIRNDEW
TWEEAYHYLY EDVAFDNIVI SPGPGSPMCP ADIGICLRLL LECRDIPILG VCLGHQALGY
VHGAHVVHAP EPVHGRLSGI EHDGNILFSD IPSGRNSDFK VVRYHSLIID KESLPKELVP
IAWTIYDDTG SFSEKNSCVP VNNTGSPLGN GSVIPVSEKL ENRSHWPSSH VNGKQDRHIL
MGIMHSSFPH YGLQFHPESI ATTYGSQLFK NFKDITVNYW SRCKSTSLRR RNINDTANMQ
VPDATQLLKE LSRTRCTGNG SSYFGNPKSL FSAKTNGVDV FDMVDSSYPK PHTKLLRLKW
KKHERLAHKV GGVRNIFMEL FGKNRGNDTF WLDTSSSDKA RGRFSFMGGK GGSLWKQLTF
SLSDQSEVTS KHAGHLLIED SQSSTEKQFL EEGFLDFLRK ELSSISYDEK DFEELPFDFC
GGYVGCIGYD IKVECGMPIN RHKSNAPDAC FFFADNVVAI DHQLDDVYIL SLYEEGTAET
SFLNDTEEKL ISLMGLSTRK LEDQTLPVID SSQSKTSFVP DKSREQYIND VQSCMKYIKD
GESYELCLTT QNRRKIGNAD PLGLYLHLRE RNPAPYAAFL NFSNANLSLC SSSPERFLKL
DRNGMLEAKP IKGTIARGST PEEDEFLKLQ LKLSEKNQAE NLMIVDLLRN DLGRVCEPGS
VHVPNLMDVE SYTTVHTMVS TIRGLKKTDI SPVECVRAAF PGGSMTGAPK LRSVEILDSL
ENCSRGLYSG SIGYFSYNGT FDLNIVIRTV IIHEDEASIG AGGAIVALSS PEDEFEEMIL
KTRAPANAVM EFCSDQRRQ
