GenomeNet

Database: UniProt
Entry: A0A1D2I8T9_9ACTN
LinkDB: A0A1D2I8T9_9ACTN
Original site: A0A1D2I8T9_9ACTN 
ID   A0A1D2I8T9_9ACTN        Unreviewed;       727 AA.
AC   A0A1D2I8T9;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=aminodeoxychorismate synthase {ECO:0000256|ARBA:ARBA00013139};
DE            EC=2.6.1.85 {ECO:0000256|ARBA:ARBA00013139};
GN   Name=pabB_2 {ECO:0000313|EMBL:ODA70884.1};
GN   ORFNames=APS67_004888 {ECO:0000313|EMBL:ODA70884.1};
OS   Streptomyces sp. AVP053U2.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1737066 {ECO:0000313|EMBL:ODA70884.1, ECO:0000313|Proteomes:UP000054731};
RN   [1] {ECO:0000313|EMBL:ODA70884.1, ECO:0000313|Proteomes:UP000054731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AVP053U2 {ECO:0000313|EMBL:ODA70884.1,
RC   ECO:0000313|Proteomes:UP000054731};
RA   Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL   Submitted (JUN-2016) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ODA70884.1}.
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; LMTQ02000032; ODA70884.1; -; Genomic_DNA.
DR   RefSeq; WP_062190517.1; NZ_LMTQ02000032.1.
DR   AlphaFoldDB; A0A1D2I8T9; -.
DR   OrthoDB; 3518032at2; -.
DR   Proteomes; UP000054731; 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   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:ODA70884.1};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054731};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ODA70884.1}.
FT   DOMAIN          4..185
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   DOMAIN          257..391
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          442..696
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   REGION          192..236
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        169
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   727 AA;  78014 MW;  11ABA97CF46F1BFF CRC64;
     MRTLLVDNYD SFTYNLFHYL SRVNGREPEV IRNDDPAWRP GLLGSFDNVV LSPGPGTPHR
     PADFGLCAGI AEEGRLPVLG VCLGHQGMAL AHGASVGRAP EPHHGRVCAV RHDGTGLFEG
     LPQPLEVVRY HSLAVTDLPP ELEATAWSAD GVLMGLRHRT LPLWGVQFHP ESIGTREGHR
     LLENFRRLTE EHDRAGGHRP VVTTGVPAQR RPPEADTATA VAPAPATAGG AAGGGSPRRL
     RVVAERLRTR WDAEVAFDRL FRTGDHPFWL DSSRPGGRLG QLSVMGDASG PLARVASADV
     ETGTVTVTEG GTTRVEQSPF LAWLERDLAG LSTEVPDLPF DFALGWVGCL GYELKAECDG
     DAAHRSPDPD AVLVFADRAL VLDHRTDTTY LLALAEDGDE EPARSWLASA AGTLETLAGR
     EPGPCEAPAS GGTGPVVLRH DRDAYLKLID VCQQEIAAGE TYEVCLTNMA ETDTDLDPWQ
     AYRCLRRVSR APFAAFLHFG PMAVLSTSPE RFLRIDRHGV MESKPIKGTR PRGADPREDE
     RLARDLAANE KDRAENLMIV DLVRHDLGRC AQVGSVVADP VFQVETYATV HQLVSTVRAR
     LRPGLSPVAA VRAAFPGGSM TGAPKIRTMQ IIDRLEGGPR GVYSGAIGYF SLTGAVDLSI
     VIRTVVLSGN RLRYGVGGAV IALSDPAAEF EETAVKAAPL LRLLGAAFPG REELAGEAVS
     DVTPAGP
//
DBGET integrated database retrieval system