ID A0A1G0ZWA6_9BACT Unreviewed; 845 AA.
AC A0A1G0ZWA6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=phosphoribosylformylglycinamidine synthase {ECO:0000256|ARBA:ARBA00012747};
DE EC=6.3.5.3 {ECO:0000256|ARBA:ARBA00012747};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000256|ARBA:ARBA00032632};
DE AltName: Full=Formylglycinamide ribotide amidotransferase {ECO:0000256|ARBA:ARBA00029823};
DE Flags: Fragment;
GN ORFNames=A2283_07465 {ECO:0000313|EMBL:OGV62493.1};
OS Lentisphaerae bacterium RIFOXYA12_FULL_48_11.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798578 {ECO:0000313|EMBL:OGV62493.1, ECO:0000313|Proteomes:UP000177651};
RN [1] {ECO:0000313|EMBL:OGV62493.1, ECO:0000313|Proteomes:UP000177651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004920}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000256|ARBA:ARBA00008608}.
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:OGV62493.1}.
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DR EMBL; MHBM01000220; OGV62493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0ZWA6; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000177651; Unassembled WGS sequence.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01740; GATase1_FGAR_AT; 1.
DR CDD; cd02204; PurL_repeat2; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR010073; PurL_large.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR NCBIfam; TIGR01735; FGAM_synt; 1.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605}.
FT DOMAIN 2..139
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 377..517
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 682
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 807
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 809
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGV62493.1"
SQ SEQUENCE 845 AA; 92525 MW; 15EF9221A5451494 CRC64;
GGGAASSMDT GSNALDLDFN SVQRDNAEMQ RRCQEVIDAC IALGKDNPIL SIHDIGAGGL
SNGCPELVSE TGGKFHLRRI HNEDKSMSPM EIWCCEAQER YVLAVAEESL EGFLKLCRRE
RCPVAVVGEV TADNHLSLED EHFKNKPIDI DIRVILGKAP KMLRDVKHSS ETHQPFDFKA
IHVKEAVERV LHLPAVANKT FLITIADRSV TGMVSRDQMV GPYQTPVADA AVTITSYKAS
TGEVMTMGER TSLAIVSPSA SGRMAVAEAI TNIAGTNIGK IGDIKLSANW MCACSEEGED
AGLFDTVRAV GMDLCPQIGV SIPVGKDSLS MRTLWDNAYG KKEKMTAPLS LVVSAFAPVK
DVRKTVTPDF KPKDSKLILV DLGHGRNRLG CSALAQVYNQ VGGGVPDVDK PLELVSFFNA
MQELVDAGLL LAYHDRSDGG LLATLSEMCF GGRIGAKIDL SALGKDPISI LFAEELGAVV
QVESHSVGKA ENILKKYGLK DIACLIGSIH KTGELEFIFE GKEFLREHVS KLNRTWSELT
YHMQARRDNP ECAKQEFDNL LDEKDPGMNF KVTDDCSQPV NISSRRPRMA ILREQGVNGH
VEMASAFDRA GFESVDVHMT DLLGGYANLS DFEGLVACGG FSYGDVLGAG SGWARCVLYN
ERLKEMFAKF FSREETFTLG VCNGCQMVSQ LKDIIPGAEH WPAFTKNKSQ QFEARYVTVE
VISSPSIFFK GMEGSRLGIP VAHGEGYANF EVTGSFNKVL DNKLLALRFV DNYGKPTERY
PFNPNGSCQG LTGVTTTDGR VTIMMPHPER GFRSLQMSYR PEKLFDGEAG PWLRMFQNAR
KFARS
//
