ID A0A0A1THL4_9HYPO Unreviewed; 862 AA.
AC A0A0A1THL4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=VHEMI05672 {ECO:0000313|EMBL:CEJ89848.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ89848.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ89848.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
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; CDHN01000003; CEJ89848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1THL4; -.
DR STRING; 1531966.A0A0A1THL4; -.
DR HOGENOM; CLU_006493_0_0_1; -.
DR OrthoDB; 201921at2759; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000039046; 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; PR00095; ANTSNTHASEI.
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:UP000039046};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 27..256
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 337..491
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 558..850
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT ACT_SITE 122
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 240
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 862 AA; 94504 MW; 2EF22EF93D6DB3D8 CRC64;
MPLLPAKLPL VHSFSDGALH QPQRRILLID AYDSFTNNIV SLLKDALGTA VHIHVLHMDL
KTLHADPTPD WTPAQFLQRL ASFDAVVCGP GPGSPLREED VGAFRLLWDL CGEKAVPVMG
VCLGFQSLVA HFGGGIRKLR RGLHGMVRLI DHKGRHNDTA DVFTGVVDFK ATLYHSLCAD
IGQDDVPDDD WDTKRWESPS CGPDLVPLAW VTEPEQGNER ILMAVRHATL PFWGVQYHPE
SVCTEEGAKD VLKNWFQQAV KWNETNREQI QPWLFPSAQS DSLDSPQIGN TPREAAREGV
PAVLYDKLKS GLAAKNATSK YVCQTIKLPA HVDTADVAEL LNHDAVETIM LDSSSAPNGD
PLARNSVIAV GIDNALRFEY HAGDNYAAFR QPATNSTEEE TQQVKLSETG ADPMAAWQLM
SAYWQKRKIF DEDGAEPSFK GGFMGFITYE MGLSTLSEGI LATERGHRRP DICMAWVTKS
VVLDHKAGVV YVQELAKPDG TSSWVQDTVA ILEQSTIWAG TFSGPPLTNV KAQFTHEELL
QDVEATKHAV LDFSIPNSEK YEADVKRCQD AIAEGESYEL CLTAQTLMSR PGAKAAHGKP
ALSKSYGTDA ALTPWDIYRT QRARQPAPFG SFIRLGGATI MSSSPERFLS NTPHGLCAMR
PMKGTVRKSA TVSTLEEAEK ILHIPKEEAE NLMIVDLVRH DLHGVCGPGR VTVPELLKVE
EYATVFQMVT AVNGQLPGGA DLRSRTQLSG LDVLAAALPP GSMTGAPKKR SCEILKVIEP
TERSIYSGVV GFFDVKGQGD WSVTIRTMFH WDDETEHDGQ TGREVWRIGA GGAVTILSTP
EGEREEMFTK LCGPLGVFRD VA
//
