ID A0A2I0PXI8_9EURY Unreviewed; 266 AA.
AC A0A2I0PXI8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000313|EMBL:PKL70972.1};
GN ORFNames=CVV30_05170 {ECO:0000313|EMBL:PKL70972.1};
OS Methanomicrobiales archaeon HGW-Methanomicrobiales-1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales.
OX NCBI_TaxID=2013817 {ECO:0000313|EMBL:PKL70972.1, ECO:0000313|Proteomes:UP000233367};
RN [1] {ECO:0000313|EMBL:PKL70972.1, ECO:0000313|Proteomes:UP000233367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGW-Methanomicrobiales-1 {ECO:0000313|EMBL:PKL70972.1};
RX PubMed=28350393; DOI=10.1038/ismej.2017.39;
RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K.,
RA Probst A., Burstein D., Thomas B.C., Banfield J.F.;
RT "Potential for microbial H2 and metal transformations associated with novel
RT bacteria and archaea in deep terrestrial subsurface sediments.";
RL ISME J. 11:1915-1929(2017).
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:PKL70972.1}.
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DR EMBL; PGYM01000001; PKL70972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0PXI8; -.
DR Proteomes; UP000233367; Unassembled WGS sequence.
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 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}.
FT ACT_SITE 96
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 266 AA; 29770 MW; 48FB0E4A33C28879 CRC64;
MIDEKALIMS GFGINSEMET KEVLARAGMD ADIVHINDLI AGRNRLSDYR LLVFPGGFSY
GDDTGAGNAY ANRVRNNIWD DLLEFLDGDN LVLGICNGFQ ILANLGLVPA FDKHYARDIA
LMPNRGGRLE CRFVSLKPAA DNLWTKGIER LYCPVAHGEG NLSCSPETLL RLKRQKQIAF
TYCHEDLTPA YGEYPWNPNG SVEDIAGITS ADGKVLGLMP HPERAMEFVN LYDWPLRKEE
MRRKGVALPA ESLNMHLFRN AVGYFR
//
