ID A1T0N3_PSYIN Unreviewed; 194 AA.
AC A1T0N3;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Aminodeoxychorismate synthase, glutamine amidotransferase subunit {ECO:0000313|EMBL:ABM05298.1};
DE EC=2.6.1.85 {ECO:0000313|EMBL:ABM05298.1};
GN OrderedLocusNames=Ping_3615 {ECO:0000313|EMBL:ABM05298.1};
OS Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM05298.1, ECO:0000313|Proteomes:UP000000639};
RN [1] {ECO:0000313|EMBL:ABM05298.1, ECO:0000313|Proteomes:UP000000639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=37 {ECO:0000313|EMBL:ABM05298.1,
RC ECO:0000313|Proteomes:UP000000639};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA Richardson P.;
RT "Complete sequence of Psychromonas ingrahamii 37.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000510; ABM05298.1; -; Genomic_DNA.
DR RefSeq; WP_011771846.1; NC_008709.1.
DR AlphaFoldDB; A1T0N3; -.
DR STRING; 357804.Ping_3615; -.
DR MEROPS; C26.955; -.
DR KEGG; pin:Ping_3615; -.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_014340_1_2_6; -.
DR OrthoDB; 9786812at2; -.
DR Proteomes; UP000000639; 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; PR00099; CPSGATASE.
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:ABM05298.1};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605,
KW ECO:0000313|EMBL:ABM05298.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000639};
KW Transferase {ECO:0000313|EMBL:ABM05298.1}.
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 169
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 171
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 194 AA; 21430 MW; EB6E3E04232D74A4 CRC64;
MLLMIDNYDS FTYNLVQYFG QLKQEVIVKR NDQVSLQEIT DLNPDQIVIS PGPCTPDAAG
ISLKTIERFA GQIPLLGVCL GHQSIGQVFG AKVVRASKVM HGKNSLIEHD TKGVFRGLNN
PLNITRYHSL ILDPGSLPSC LEVTATVLNS NEIMAIRHKT LALEGVQFHP ESIMSEQGLK
LLNNFIDQSL GFKK
//
