ID Q3YRH1_EHRCJ Unreviewed; 264 AA.
AC Q3YRH1;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase subunit I {ECO:0000313|EMBL:AAZ68684.1};
DE EC=6.3.5.3 {ECO:0000313|EMBL:AAZ68684.1};
GN OrderedLocusNames=Ecaj_0652 {ECO:0000313|EMBL:AAZ68684.1};
OS Ehrlichia canis (strain Jake).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=269484 {ECO:0000313|EMBL:AAZ68684.1, ECO:0000313|Proteomes:UP000000435};
RN [1] {ECO:0000313|Proteomes:UP000000435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jake {ECO:0000313|Proteomes:UP000000435};
RX PubMed=16707693; DOI=10.1128/JB.01837-05;
RA Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT "The genome of the obligately intracellular bacterium Ehrlichia canis
RT reveals themes of complex membrane structure and immune evasion
RT strategies.";
RL J. Bacteriol. 188:4015-4023(2006).
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DR EMBL; CP000107; AAZ68684.1; -; Genomic_DNA.
DR RefSeq; WP_011304761.1; NC_007354.1.
DR AlphaFoldDB; Q3YRH1; -.
DR STRING; 269484.Ecaj_0652; -.
DR KEGG; ecn:Ecaj_0652; -.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_3_0_5; -.
DR InParanoid; Q3YRH1; -.
DR Proteomes; UP000000435; Chromosome.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01740; GATase1_FGAR_AT; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR010075; PRibForGlyAmidine_synth_PurQ.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF13507; GATase_5; 1.
DR PIRSF; PIRSF001586; FGAM_synth_I; 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 Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000313|EMBL:AAZ68684.1}.
FT ACT_SITE 99
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 220
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 264 AA; 29643 MW; BB2FEA2EA77AFAA3 CRC64;
MKVVVLSGYG LNCEEETLFA FIKAGELLSC DVQGKIVHIN DMILNTKLLV DYNVLVIPGG
FSYGDDTGAG NAFALRVFNN LKEEISEFLV GDKLVIGICN GCQILMRLIS DFSNITLLNN
TVRQYQCRWV KVKVNPSNNS VWLKGLDELY IPVAHGEGRF FVENDSVITS IRNNIALRYI
TNIGNYANQE FPYNPNGSVD DIAALSDSSG RVLVMMPHPE RAMFFTQQDN WTQVKEQCLR
DNIAYPTYGD GMKVFCNAVE YFCK
//
