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Database: UniProt
Entry: B8FVP6_DESHD
LinkDB: B8FVP6_DESHD
Original site: B8FVP6_DESHD 
ID   B8FVP6_DESHD            Unreviewed;       721 AA.
AC   B8FVP6;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   RecName: Full=aminodeoxychorismate synthase {ECO:0000256|ARBA:ARBA00013139};
DE            EC=2.6.1.85 {ECO:0000256|ARBA:ARBA00013139};
GN   OrderedLocusNames=Dhaf_4443 {ECO:0000313|EMBL:ACL22448.1};
OS   Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564 {ECO:0000313|EMBL:ACL22448.1, ECO:0000313|Proteomes:UP000007726};
RN   [1] {ECO:0000313|EMBL:ACL22448.1, ECO:0000313|Proteomes:UP000007726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10664 / DCB-2 {ECO:0000313|Proteomes:UP000007726};
RX   PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA   Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA   Tiedje J.M.;
RT   "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT   anaerobe capable of dehalogenation and metal reduction.";
RL   BMC Microbiol. 12:21-21(2012).
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DR   EMBL; CP001336; ACL22448.1; -; Genomic_DNA.
DR   RefSeq; WP_015945221.1; NC_011830.1.
DR   AlphaFoldDB; B8FVP6; -.
DR   MEROPS; C26.955; -.
DR   KEGG; dhd:Dhaf_4443; -.
DR   HOGENOM; CLU_006493_0_2_9; -.
DR   OMA; FPVAYWY; -.
DR   Proteomes; UP000007726; Chromosome.
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:SF50; AMINODEOXYCHORISMATE SYNTHASE COMPONENT 1; 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; 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   4: Predicted;
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..186
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   DOMAIN          212..366
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          453..707
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   REGION          424..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        79
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   721 AA;  81150 MW;  79FC370C06B15E6A CRC64;
     MIFILDNFDS FTFNLYQYFG ELGEEVVALR RDQCTIDAIE ELKPELIVIS PGPCAPRDTQ
     FTLTVIDYFK GKVPILGVCL GHQAIGEILG GEVIRAKAPV HGKVSEIHHD GQGVFFQLPN
     PLTVTRYHSL ALRRESLPEE LLITAETADG EIMGIRHREL PLEGVQFHPE AILTEKGHDL
     LGNAVKNART WWQAQGQSGH NSPWVIQELA IDLQPIELLE AFKESEYPFF LDSGRNYGGL
     GRYSFMGAFP FLQASACRDG VEVKRFAGEE EGSKEDLSSL IGQEWLAYPE GESLKILDDL
     VERYRVPNPT EFPFVGGAVG FWTYDLKDEL EKMPQSGIND LDLPLWRFSW YDGIVVYDHE
     NRRYTLLACG MTESGECRRA LAQARVERLV GVLEGFLEGR GGKGDHPGTA AAYQRQIGAR
     IGTQQERSGT YQGHDESQDM EQPQERVHYT VSKEQYLLDL QRVIDYIYAG DIYQANLTQR
     FQFPYTKEPM ALYKALHAHN PAPFAAFLPY EDFQILSSSP ERFVQISAQG EIETRPIKGT
     RPRGKTPEED EAYARELTES TKDRAELTMI IDLQRNDLGR ICRYGSVRVT DLIRLEQYPT
     VWHLVSTIVG KLKPELKTSE ILKAIFPGGS ITGAPKIRAM EIIEELEPYK RGLYTGSIGY
     MGFDGAWDTN IVIRTILLKD GQAYFNGGGG IVADSVPEEE YQEALQKVKA LLRVLSYPSI
     G
//
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