ID A0A1M6H641_9CLOT Unreviewed; 456 AA.
AC A0A1M6H641;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=aminodeoxychorismate synthase {ECO:0000256|ARBA:ARBA00013139};
DE EC=2.6.1.85 {ECO:0000256|ARBA:ARBA00013139};
GN ORFNames=SAMN02745975_01454 {ECO:0000313|EMBL:SHJ17654.1};
OS Geosporobacter subterraneus DSM 17957.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Geosporobacter.
OX NCBI_TaxID=1121919 {ECO:0000313|EMBL:SHJ17654.1, ECO:0000313|Proteomes:UP000184536};
RN [1] {ECO:0000313|EMBL:SHJ17654.1, ECO:0000313|Proteomes:UP000184536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17957 {ECO:0000313|EMBL:SHJ17654.1,
RC ECO:0000313|Proteomes:UP000184536};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FQZV01000016; SHJ17654.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6H641; -.
DR STRING; 1121919.SAMN02745975_01454; -.
DR OrthoDB; 9803598at2; -.
DR Proteomes; UP000184536; Unassembled WGS sequence.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro.
DR Gene3D; 3.60.120.10; Anthranilate synthase; 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 NCBIfam; TIGR00553; pabB; 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 PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; ADC synthase; 1.
PE 4: Predicted;
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..146
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 193..446
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
SQ SEQUENCE 456 AA; 52032 MW; 1C338D5008870810 CRC64;
MIIQKIDTSL NSFQLYTIFK DRSYSFFLDS GMDHEKLGKY SFIGFDPLLV FKSKNEQIEI
IEESQTSIYY GNPLNKLKEI IDRYKMDYKS EMPFVGGLVG YLSYDLCHHI ERLPRRAIDD
IDIPDCYFGV YDGIIIIDHR QNTVYIAALG IKTPADQRVQ TIEDEIAKAE QRGVSIEVKM
NPREVDFKAN MTKEVYLEAI EKVRKYIRAG DIYQANFTQR FECNLEDSPY ELYGKLRTIN
PAPFASLLDF GDVAIVSSSP ERFIQIKNRI METRPIKGTR PRGKTPEEDM QNRQDLLTSE
KDQAELLMIV DLERNDLGRV SKTGTVKVTE LFHLEEYATV YHLVSTIVGE MKEECDVVDC
ISATFPGGSI TGAPKIRAME IIDELEPTQR NIYTGSIGYI GFNGDTDLNI VIRTIVCKNG
KAYFQVGGGI VWDSDAEMEY EETLHKGRAL FKALSS
//