ID A0A2A4WBR3_9GAMM Unreviewed; 1303 AA.
AC A0A2A4WBR3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000256|HAMAP-Rule:MF_00419};
DE Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00419};
DE Short=FGAMS {ECO:0000256|HAMAP-Rule:MF_00419};
DE EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00419};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000256|HAMAP-Rule:MF_00419};
DE Short=FGAR amidotransferase {ECO:0000256|HAMAP-Rule:MF_00419};
DE Short=FGAR-AT {ECO:0000256|HAMAP-Rule:MF_00419};
GN Name=purL {ECO:0000256|HAMAP-Rule:MF_00419};
GN ORFNames=COB33_10785 {ECO:0000313|EMBL:PCI67932.1};
OS Thiotrichaceae bacterium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae.
OX NCBI_TaxID=2030882 {ECO:0000313|EMBL:PCI67932.1, ECO:0000313|Proteomes:UP000217494};
RN [1] {ECO:0000313|Proteomes:UP000217494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the
CC purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of
CC formylglycinamide ribonucleotide (FGAR) and glutamine to yield
CC formylglycinamidine ribonucleotide (FGAM) and glutamate.
CC {ECO:0000256|HAMAP-Rule:MF_00419}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00419};
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, ECO:0000256|HAMAP-Rule:MF_00419}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00419}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00419}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000256|ARBA:ARBA00008608, ECO:0000256|HAMAP-Rule:MF_00419}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00419}.
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:PCI67932.1}.
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DR EMBL; NVTY01000030; PCI67932.1; -; Genomic_DNA.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000217494; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01740; GATase1_FGAR_AT; 1.
DR CDD; cd02203; PurL_repeat1; 1.
DR CDD; cd02204; PurL_repeat2; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR HAMAP; MF_00419; PurL_1; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR040707; FGAR-AT_N.
DR InterPro; IPR010073; PurL_large.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR036604; PurS-like_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; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF109736; FGAM synthase PurL, linker domain; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR SUPFAM; SSF82697; PurS-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00419}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00419};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_00419};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00419};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00419};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00419};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00419};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_00419}.
FT DOMAIN 35..151
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 173..221
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 438..590
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 839..977
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1143
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1268
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1270
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 388..390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 680
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 681
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 720
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 724
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 888
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 890
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1303 AA; 140913 MW; 167F4C20C2FFB020 CRC64;
MLPLRGTTAL SPFRTEKLLS AAQAVLPILQ AIHSEFVYFI ESKTALTSAD EVLLNELLHS
QSMQLNNLAG TLMLVVPRIG TISPWSSKAT DIARISGLAA VQRIERGIAY HIETCDGSML
SGEQKLALAS LLHDRMIESL LITFDEADEL FSHAAPTPLM SVDVITGGRA ALVAADSELG
LALSDDEIDY LVESFSALKR NPTDVELMMF AQANSEHCRH KIFNADWIID GEQQDIGLFS
MIRNTTKCSP DGVLSAYHDN AAVIASPTEA ARFFPDGSTG EYGRVNEVSH INIKVETHNH
PTAIAPFPGA ATGMGGEIRD EGATGRGAKP KAGLAGFSVS NLQLPDAPRP WEQDNGKPAR
IVSALDIMLD GPVGGAAFNN EFGRPNLTGY FRTYEAWVPS GSGQQLRGFH KPIMIAGGLG
AIREQHIDKN NMPPETQLIV LGGPAMLIGL GGSAASSVAS GDSREALDFA SVQRGNPEME
RRCQEVIDRC WQLGEENPIV SLHDVGAGGI SNALPELVND SERGAVFELR AVPNDEAGMS
PLQIWCNESQ ERYVLGIPRN RLAQFRALCE RERCPFAVVG EVKADCDLTV NDSHFENSPV
DIPMDLLFGK PPKMLRDVTR LQVTADELDC SEMTLEDAAV RVLQLPAVAD KKFLITIGDR
SVTGMVARDQ MVGPWQIPVA DVAVTLADYD NYHGEAMSMG ERSPVALLNP AASGRLAIGE
ALTNIAAADI AQLSDIKLSA NWMAAAGVAG EDAALYETVH AVGMALCPEL GIAIPVGKDS
LSMKTVWEED GEVREMSSPL SLVISAFSPV QDCRKTLTPQ LRSDKGETDL LLIDLGRGKN
RIGGSALAQV YKQTGRTTPD LDDAFQFKAF FNTLQQLNRD GQLLAYHDRS DGGLFSTITE
MAFAGHVGVT IAIDALAADN SQPAMLAALF NEELGAVIQV RRDSRDAVIA KFKAAGLADC
CHYIGGLNGD DRVVVEYDQQ EILASTRSGY QRIWSETSWQ IQSLRDNIDC AQQEYDLILN
ASDPGLNIDL SFDLNDNVAA PYFNQQRPRI AVLREQGVNG HVEMAAAFDR AGFTAVDVHM
SDILSGRLSL SDFRGLVACG GFSFGDVLGA GMGWASSILH NSRARDEFSA FFERSDSFGL
GVCNGCQMMS NLHTLIPGAQ RWPCFERNTS EQFEARFSLV EVMPSPSLFL DGMAGSRMPI
TVAHGEGRVE FRAGQALAQL EQASTSVLRF VDNNGAATES YPANPNGSPG GITGVTTDDG
RFTIMMPHPE RVFRSVQHSW YPDGWGEAGP WLRMFSNARK WVA
//
