ID N4TXY4_FUSC1 Unreviewed; 830 AA.
AC N4TXY4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=FOC1_g10014253 {ECO:0000313|EMBL:ENH68468.1};
OS Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH68468.1, ECO:0000313|Proteomes:UP000016928};
RN [1] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
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}.
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DR EMBL; KB730248; ENH68468.1; -; Genomic_DNA.
DR AlphaFoldDB; N4TXY4; -.
DR STRING; 1229664.N4TXY4; -.
DR VEuPathDB; FungiDB:FOC1_g10014253; -.
DR HOGENOM; CLU_006493_0_0_1; -.
DR OMA; DWSVNIR; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000016928; 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 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000016928};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..231
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 327..467
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 527..818
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT ACT_SITE 113
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 830 AA; 92448 MW; 41AA79E9712DC9CF CRC64;
MTTGSEPSVG APKRILFIDA YDSFTNNIVS LLRTILGADI FVIRIDLSVV DRASDDDAPT
KWTEQEFIDN LAQFDAVVCG PGPGSPLNIE DVGAFNLLWD LPEHLQLPVL GICLGFQSLL
AAHGGSVRRL KRGLHGMVRE IEHRGEDIFC GVPPFKATLY HSLCVDIGQY SDDWAEENRW
RSTSEFSPLA WATEFREDGR REQILQGVRH NKKPFWGLQY HPESVCTEKN AQGVLINWFQ
AALQWNKYRG RRVQGPLLEI QTLSPPNHLE SAAAHKVHLG NWWSTSNSSE ISLRDFARGS
EYTYRTITLP QGAGVPELVE MMGLEKGEAV ILDSSSSKNG DALALNSIVA LEVDDALRFE
YNVCDDYVTV RHPSTDGKDK TEMISLENGT INVWEVISDF WETRSHPPGS DCSNSAFKGG
FMGFITYEMG LHGLEKKMVP EDRGHKRPDI CLAWVTKSIV LDHRAGVAYV QNLKARGSND
SWLDRMTERI QQSDCWNAIK MSNGVNGHVI ENRAQNKEIN ITTPQPDRYE EQVRVCQDFI
AAGESYELCL TSQTTMARPR SRNNERSPWT IYQTLRKRQP APFGSFIRLC GATMLSCSPE
RFLRYDTNGL CSMRPMKGTV RKSEAVSTLA QAEKILHVPK EVAENLMIVD LVRHDLHGVC
GVGHVTVPDL MKVEEYATVF QMITVVNGQL PGRNGNKPHG ARRSSFDSHC PYTGLDALAA
ALPPGSMTGA PKKRSCELLQ IIEGQHERSL YSGVVGYMDV AGAGDWSVTI RTMFRWDDEV
APAEEGETEP REVWRIGAGG AVTILSTPEG ERDEMFTKLA GPMGVFRDAA
//
