ID A0A0T0PTQ5_9SPHN Unreviewed; 190 AA.
AC A0A0T0PTQ5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Para-aminobenzoate synthase {ECO:0000313|EMBL:KQT32242.1};
DE EC=2.6.1.85 {ECO:0000313|EMBL:KQT32242.1};
GN ORFNames=ASG29_10495 {ECO:0000313|EMBL:KQT32242.1};
OS Sphingomonas sp. Leaf412.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736370 {ECO:0000313|EMBL:KQT32242.1, ECO:0000313|Proteomes:UP000051178};
RN [1] {ECO:0000313|EMBL:KQT32242.1, ECO:0000313|Proteomes:UP000051178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT32242.1,
RC ECO:0000313|Proteomes:UP000051178};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT32242.1, ECO:0000313|Proteomes:UP000051178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf412 {ECO:0000313|EMBL:KQT32242.1,
RC ECO:0000313|Proteomes:UP000051178};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQT32242.1}.
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; LMQP01000003; KQT32242.1; -; Genomic_DNA.
DR RefSeq; WP_055983502.1; NZ_LMQP01000003.1.
DR AlphaFoldDB; A0A0T0PTQ5; -.
DR STRING; 1736370.ASG29_10495; -.
DR OrthoDB; 9803598at2; -.
DR Proteomes; UP000051178; Unassembled WGS sequence.
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:KQT32242.1};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Reference proteome {ECO:0000313|Proteomes:UP000051178};
KW Transferase {ECO:0000313|EMBL:KQT32242.1}.
FT DOMAIN 4..183
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 80
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 166
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 190 AA; 19973 MW; 3C8AF9DD2220925C CRC64;
MIFVVDNYDS FTWNLVHYLM ELGVEVRVER NDALSAGDAL ATGADAFLIS PGPCTPDDAG
ISLDLVAACA DARRPLLGVC LGHQSIGQHF GGKVVRGGLM HGKTSPIAHD GTGVFAGLPT
PFTGTRYHSL VVTDIPDALA VNATAPDGSV MGLRHRDLPI HGVQFHPESI ATQHGHDMLA
SFLTIAGIGR
//
