ID A0A098G6F8_9GAMM Unreviewed; 420 AA.
AC A0A098G6F8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase I (FGAM synthase I) {ECO:0000313|EMBL:CEG57095.1};
GN Name=purQ {ECO:0000313|EMBL:CEG57095.1};
GN ORFNames=LFA_1690 {ECO:0000313|EMBL:CEG57095.1};
OS Legionella fallonii LLAP-10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1212491 {ECO:0000313|EMBL:CEG57095.1, ECO:0000313|Proteomes:UP000032430};
RN [1] {ECO:0000313|Proteomes:UP000032430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC700992 {ECO:0000313|Proteomes:UP000032430};
RA Gomez-Valero L.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LN614827; CEG57095.1; -; Genomic_DNA.
DR RefSeq; WP_045095658.1; NZ_LN614827.1.
DR AlphaFoldDB; A0A098G6F8; -.
DR STRING; 1212491.LFA_1690; -.
DR KEGG; lfa:LFA_1690; -.
DR HOGENOM; CLU_655210_0_0_6; -.
DR OrthoDB; 9804441at2; -.
DR Proteomes; UP000032430; Chromosome.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:InterPro.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR010075; PRibForGlyAmidine_synth_PurQ.
DR NCBIfam; TIGR01737; FGAM_synth_I; 1.
DR PANTHER; PTHR47552; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURQ; 1.
DR PANTHER; PTHR47552:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURQ; 1.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000032430}.
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 224
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 420 AA; 47174 MW; D8D3AECFE93931A5 CRC64;
MNIAIVQFPG SNCERETILA VKRAGMIPVE FLWNESPSKL REMDGYIIVG GFSYEDRSRA
GIIAALDPVM QEIKAQSELG KPVLGICNGA QILVETGLVP GLKNHQLGMA LTENKRIVDG
KILGTGFYNS WIHMRSCSTN KSNAFTRRLN HDSILSVPAA HAEGRFVMPV TLLKEIEQED
LHVFQYCDEQ GTIIDNFPIN PNGSMLNIAA VMNKSGNVMA MMPHPERTGS GDAIFLSMRD
YIEEAKPFTP SVLSYTPEIL PRKLYKKEVN KHECVVQLII TDNYALTVQN TLRQLGIPVQ
VGRMVHWQID CPSPKIIQQI KQTGVLYNER KEYLVDPQSI ANASSKAYLV RPMDDLLGQQ
KKQMLEDHFA VKGVEQIHHG ILWIFKSEKA TPLDDLTKAI LNTHIIFNPN SHVCYEYENS
//
