ADCS_ORYSJ
ID ADCS_ORYSJ Reviewed; 895 AA.
AC Q5Z856; Q0D9T5;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Probable 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 Flags: Precursor;
GN Name=ADCS; OrderedLocusNames=Os06g0699700, LOC_Os06g48620;
GN ORFNames=P0468G03.14;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 564-895.
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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 (By
CC similarity). {ECO:0000250}.
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 -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC aminobenzoate from chorismate: step 1/2.
CC -!- PATHWAY: Antibiotic biosynthesis; candicidin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- DOMAIN: The PABA component provides the glutamine amidotransferase
CC activity. {ECO:0000250}.
CC -!- DOMAIN: The PABB component catalyzes the formation of ADC by binding
CC chorismate and ammonia. {ECO:0000250}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC synthase component I family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF20388.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP004278; BAD54000.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF20388.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK059492; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015643126.1; XM_015787640.1.
DR AlphaFoldDB; Q5Z856; -.
DR SMR; Q5Z856; -.
DR STRING; 4530.OS06T0699700-01; -.
DR PaxDb; Q5Z856; -.
DR PRIDE; Q5Z856; -.
DR GeneID; 4341959; -.
DR KEGG; osa:4341959; -.
DR eggNOG; KOG1224; Eukaryota.
DR HOGENOM; CLU_006493_1_0_1; -.
DR InParanoid; Q5Z856; -.
DR OrthoDB; 665558at2759; -.
DR PlantReactome; R-OSA-1119494; Tryptophan biosynthesis.
DR UniPathway; UPA00077; UER00149.
DR UniPathway; UPA00101; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q5Z856; OS.
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; IBA:GO_Central.
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; 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 2: Evidence at transcript level;
KW Chloroplast; Folate biosynthesis; Glutamine amidotransferase;
KW Multifunctional enzyme; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..895
FT /note="Probable aminodeoxychorismate synthase,
FT chloroplastic"
FT /id="PRO_0000430155"
FT DOMAIN 49..307
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..875
FT /note="PABB component"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 895 AA; 99227 MW; 81F2E03ADA520040 CRC64;
MAALRLPTPP PPRAPAPWLH SSHRRRVAAP RGAGGGGGGG GAVPPPPVRT LLIDNYDSYT
YNIFQELSVV NGVPPVVVRN DEWTWRDVYR WVYKERAFDN IVISPGPGSP ACPSDIGIGL
RILCECGDIP ILGVCLGHQA LGFVHGAKIV HAPEAIHGRL SELEHNGCYL FNHIPSGINS
GFKVVRYHSL VIEPDSLSED LISIAWTASP KMLSFLESDK PDITSSTLWG SLDNLFVTNQ
SECSTTDGKM PSINDASELD GYRVLMGVRH STRPHYGVQF HPESVATHYG RQIFQNFKKI
TTDFGLQTPL LQERKVHSIG KLERSQISSP DLKNFVANDL LHSARLKLWD SVGPCALPKR
SSGDKCLRLQ WKKIDNFLNR IGGSENIFSV LFGHHSAEDT FWLDSSSVDQ NRARFSFMGG
KGGPLWKQMT FHLASQRANC GGNLTIRDAY GCTVRNFLKD GFLDFLDKEM QSIQYIEKDY
EGLPFDFHGG FVGYIGYGLK VECDASSNSA KSSTPDACFF FADNLVVVDH NNGDVYILSL
HDEYSSGNGD GDYQNSIHSL WLANTEKKLL RMDAMAPRLS INGNSSINGN SFTISSSVNK
QRFVIEKSKD EYIRDVQSCL DYIRDGESYE LCLTTQMKRR TDYMDALKLY LKLRKQNPAP
YAAWLNFSSE NLSICCSSPE RFLRLDRNAI LEAKPIKGTI ARGRTPEEDE CLRLQLKYSE
KDQAENLMIV DLLRNDLGKV CEPGSVHVPR LMDVESYKTV HTMVSTIRGT KMSDLSPVDC
VKAAFPGGSM TGAPKVRSME ILDSLETSPR GIYSGSVGFF SYNKTFDLNI VIRTVVLHNG
EASIGAGGAI VALSDPEAEY NEMLLKAKAP TKVVEECSQQ IYNPDRSDSM QTTVS
