GenomeNet

Database: UniProt
Entry: Q47PB8_THEFY
LinkDB: Q47PB8_THEFY
Original site: Q47PB8_THEFY 
ID   Q47PB8_THEFY            Unreviewed;       700 AA.
AC   Q47PB8;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=aminodeoxychorismate synthase {ECO:0000256|ARBA:ARBA00013139};
DE            EC=2.6.1.85 {ECO:0000256|ARBA:ARBA00013139};
GN   OrderedLocusNames=Tfu_1666 {ECO:0000313|EMBL:AAZ55701.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ55701.1};
RN   [1] {ECO:0000313|EMBL:AAZ55701.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YX {ECO:0000313|EMBL:AAZ55701.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of Thermobifida fusca YX.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC       synthase component I family. {ECO:0000256|ARBA:ARBA00005970}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000088; AAZ55701.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47PB8; -.
DR   STRING; 269800.Tfu_1666; -.
DR   MEROPS; C26.955; -.
DR   KEGG; tfu:Tfu_1666; -.
DR   eggNOG; COG0147; Bacteria.
DR   eggNOG; COG0512; Bacteria.
DR   HOGENOM; CLU_006493_0_1_11; -.
DR   OrthoDB; 3518032at2; -.
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   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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; 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   NCBIfam; TIGR00553; pabB; 1.
DR   NCBIfam; TIGR00566; trpG_papA; 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; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
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   Aminotransferase {ECO:0000313|EMBL:AAZ55701.1};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605,
KW   ECO:0000313|EMBL:AAZ55701.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAZ55701.1}.
FT   DOMAIN          4..187
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   DOMAIN          256..393
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          437..690
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   REGION          198..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   700 AA;  75582 MW;  056F756D4C2C1B83 CRC64;
     MRVLLVDNHD SYTYNLVHLL ARTLGEEPLV VTNDDPRWKC LDPADFDAAV ISPGPGRPQR
     ASDVGHTRRV LDEPHLPILG VCLGHQAIAH HAGAAVVSAP RPRHGHLSRV RHDNSALFAG
     IPQDFTAVRY HSLCVASPLP EDVEATAWAE DGVVMALRHR VLPRWGVQFH PESVASDHGP
     TLVANFVRLA RAHRRVVAGR PGATAQQSGS PRPALHTTPV RPGQQGVPPT GAAPRALHEV
     RKTLRFRVMP RAVDTEAAFL TCYAGRDYAF WLDSSLTGGT ARFSFLGGLD SPQSEVLTYR
     VGDGTVAVRS ADGTTHTEPG TIFDALATRT ASAPYGRPDL PFDFLGGYVG YFGYELKADC
     GGTAVHRAAT PDAVWLRCDR FIAVDHAADR TYLVAVDGDE AWLDAMARSL SGLRSPSALQ
     QTGRGVDPTP FLERSPDDYV ADVKRCLEEL AAGESYEICL TTRARLPAPG DGTAFYLRLR
     RANPAPYAAL LHAGETAVYS ASPERFLRVT PDGWVESRPI KGTAPRHDDP VRDARARDAL
     RGDPKTRAEN LMIVDLLRND LGRVCEIGSV EVPAFLYTES YATVHQLIST IRGRLRADRS
     AVDAVAACFP PGSMTGAPKK RTMEIVDRLE TSARGVYSGA LGYLSFSGTA DLSVVIRTAV
     CHDGQVTVGA GGAVVLESVP EREYAEMLLK AAVPLRALEA
//
DBGET integrated database retrieval system