ID D2TMD0_CITRI Unreviewed; 187 AA.
AC D2TMD0;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Para-aminobenzoate synthase glutamine amidotransferase component I {ECO:0000313|EMBL:CBG91144.1};
DE EC=2.6.1.85 {ECO:0000313|EMBL:CBG91144.1};
GN Name=pabA {ECO:0000313|EMBL:CBG91144.1};
GN OrderedLocusNames=ROD_44491 {ECO:0000313|EMBL:CBG91144.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG91144.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG91144.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG91144.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
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DR EMBL; FN543502; CBG91144.1; -; Genomic_DNA.
DR RefSeq; WP_012908378.1; NC_013716.1.
DR AlphaFoldDB; D2TMD0; -.
DR STRING; 637910.ROD_44491; -.
DR MEROPS; C26.955; -.
DR KEGG; cro:ROD_44491; -.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_014340_1_2_6; -.
DR OrthoDB; 9786812at2; -.
DR Proteomes; UP000001889; 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:CBG91144.1};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605,
KW ECO:0000313|EMBL:CBG91144.1}; Transferase {ECO:0000313|EMBL:CBG91144.1}.
FT DOMAIN 3..185
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 187 AA; 20546 MW; CC137FC19CF016C7 CRC64;
MILLIDNYDS FTWNLYQYFC ELGADVLVKR NDELTLAQID ALSPQKIVIS PGPCTPDEAG
ISLAVIGRYA GRVPMLGVCL GHQAMAQAFG ASIVRAAKVM HGKTSPIRHN GQGVFQGLAN
PLTVTRYHSL IVDPATLPDC FQVTAWSESE EIMGIRHTAW DLEGVQFHPE SILSEQGHQL
LANFLNR
//
