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Database: UniProt
Entry: E3PSN0_ACESD
LinkDB: E3PSN0_ACESD
Original site: E3PSN0_ACESD 
ID   E3PSN0_ACESD            Unreviewed;       192 AA.
AC   E3PSN0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Aminodeoxychorismate synthase, subunit II {ECO:0000313|EMBL:CBH21884.1};
DE            EC=2.6.1.85 {ECO:0000313|EMBL:CBH21884.1};
GN   Name=pabA {ECO:0000313|EMBL:CBH21884.1};
GN   OrderedLocusNames=CLOST_1764 {ECO:0000313|EMBL:CBH21884.1};
OS   Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS   9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Acetoanaerobium.
OX   NCBI_TaxID=499177 {ECO:0000313|EMBL:CBH21884.1, ECO:0000313|Proteomes:UP000007041};
RN   [1] {ECO:0000313|Proteomes:UP000007041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF
RC   {ECO:0000313|Proteomes:UP000007041};
RX   PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA   Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA   Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA   Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT   "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT   its metabolism through its genome sequence.";
RL   BMC Genomics 11:555-555(2010).
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DR   EMBL; FP565809; CBH21884.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3PSN0; -.
DR   STRING; 1511.CLOST_1764; -.
DR   MEROPS; C26.959; -.
DR   KEGG; cst:CLOST_1764; -.
DR   eggNOG; COG0512; Bacteria.
DR   HOGENOM; CLU_014340_1_2_9; -.
DR   Proteomes; UP000007041; Chromosome.
DR   GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProt.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProt.
DR   GO; GO:0044271; P:cellular nitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   NCBIfam; TIGR00566; trpG_papA; 1.
DR   PANTHER; PTHR43418:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:CBH21884.1};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007041};
KW   Transferase {ECO:0000313|EMBL:CBH21884.1}.
FT   DOMAIN          3..186
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
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   192 AA;  21785 MW;  DA7CE091EC57C466 CRC64;
     MILMIDNFDS FCYNIYQYLR ELGEDVEVVR NDSISVKQIL AKNPEILLIS PGPCSPKEAG
     ISLEAIDYFK DKLPILGVCL GHQAIGEAFK GEIIKAKRPI HGHVHRIKHD EKGMFKNLPN
     PLGVTRYHSL VINEQNFPSE LEISAQTIDG EIMGVRHKRY PIEGVQFHPE AILTEHGHDL
     FRNFIENARG CK
//
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