ID A0A1Q7RAZ1_9BACT Unreviewed; 221 AA.
AC A0A1Q7RAZ1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phosphoribosylformylglycinamidine synthase I {ECO:0000313|EMBL:OLD61184.1};
DE Flags: Fragment;
GN ORFNames=AUI33_14845 {ECO:0000313|EMBL:OLD61184.1};
OS Ignavibacteria bacterium 13_1_40CM_2_61_4.
OC Bacteria; Ignavibacteriota; Ignavibacteria.
OX NCBI_TaxID=1805219 {ECO:0000313|EMBL:OLD61184.1, ECO:0000313|Proteomes:UP000186155};
RN [1] {ECO:0000313|EMBL:OLD61184.1, ECO:0000313|Proteomes:UP000186155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLD61184.1}.
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DR EMBL; MNHF01001548; OLD61184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7RAZ1; -.
DR Proteomes; UP000186155; 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 HAMAP; MF_00421; PurQ; 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 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 3: Inferred from homology;
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}.
FT REGION 202..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 86
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 203
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 205
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 221
FT /evidence="ECO:0000313|EMBL:OLD61184.1"
SQ SEQUENCE 221 AA; 24200 MW; 382E6762EE37AEB5 CRC64;
MKFGVVVFPG SNCDHDAYDV LKRCFGQETR FLWHKDSSLG GVDVVILPGG FSYGDYLRCG
AIARFSPIMK EVRAFAGRGG SVMGICNGFQ ILCEAGLLPG AFLRNERLNF VCEFVNLRVE
NASTRFTGAC QKSEVLRIPI AHGEGNYYAD DRTLAELEDN GQILFRYCEA DGSITASSNP
NGSRSNIAGI LNRAGNVMGL MPHPERASDP MLRNTDGRKI F
//
