ID E5WTM6_9BACE Unreviewed; 1225 AA.
AC E5WTM6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
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=HMPREF1016_00027 {ECO:0000313|EMBL:EFV31698.1};
OS Bacteroides eggerthii 1_2_48FAA.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=665953 {ECO:0000313|EMBL:EFV31698.1, ECO:0000313|Proteomes:UP000003246};
RN [1] {ECO:0000313|EMBL:EFV31698.1, ECO:0000313|Proteomes:UP000003246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_2_48FAA {ECO:0000313|EMBL:EFV31698.1,
RC ECO:0000313|Proteomes:UP000003246};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA Allen-Vercoe E., Ambrose C., Strauss J., Daigneault M., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides eggerthii strain 1_2_48FAA.";
RL Submitted (OCT-2010) 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:EFV31698.1}.
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DR EMBL; ACWG01000001; EFV31698.1; -; Genomic_DNA.
DR RefSeq; WP_004292476.1; NZ_GL622538.1.
DR AlphaFoldDB; E5WTM6; -.
DR HOGENOM; CLU_001031_0_2_10; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000003246; 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; 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 3..69
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 111..160
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 369..522
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 771..896
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1068
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1181
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1183
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 613
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 652
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 656
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 817
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 819
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1225 AA; 135811 MW; 037D3D23EB0A8183 CRC64;
MIAVECDHEL TQADSDKLCW LFGEATPESE NNLKGHFVGP RREMITPWST NAVEITQNMG
LSGITRIEEY FPVKDENADR DPMLQRMYKG LDQDVFTTNR QPEPIIHIED LEAYNEKEGL
ALSKEEMDYL KKVEKDLGRP LTDSEVFGFA QINSEHCRHK IFGGTFIIDG VEQESSLFQM
IKKTTQENPN KIISAYKDNV AFAEGPVIEQ FAPADHSKPD FFQIKDIKSV ISLKAETHNF
PTTVEPFNGA STGTGGEIRD RMGGGKGSWP IAGTAVYMTS YPRTDEDRPW EEILPVRQWL
YQTPEQILIK ASNGASDFGN KFGQPLICGS VLTFEHKEKD EVYGYDKVIM LAGGVGYGTQ
RDCLKGAPEA GNKVVVIGGD NYRIGLGGGS VSSVDTGRYS SGIELNAVQR ANAEMQKRAY
NVVRALCEED TNPVVSIHDH GSAGHVNCLS ELVEECGGLI DMSKLPIGDK TLSAKEIIAN
ESQERMGLLI QEEAIEHVRK VAERERAPMY VVGETTGDHR FAFQQADGVR PFDLAVEQMF
GSSPKTYMVD KTVERHYEMP KYELSQLHEY LTNVLQLEAV ACKDWLTNKV DRSVTGKIAR
QQCQGELQLP LSDCGVVALD YRGEKGIATS LGHAPQAALA DPAAGSILSV SEALTNLVWA
PLAEGLDSVS LSANWMWPCR SQEGEDARLY KAVKALSDFC CALQINVPTG KDSLSMTQKY
PDGSKVIAPG TVIVSAGGEV SDVKKVVSPV LVNDAKTTLY HIDFSFDKLK LGGSAFAQSL
GKVGDEVPCV QDAEYFRDAF LAVQELINKG LILAGHDISA GGLITTLLEM CFANVEGGME
INLDKMKEQD LIKILFAENP GIVIQISNKH KEEVKKILED AGVGYIKIGT PTDERHILVS
KDDATYQFGV DYMRDVWYSS SYLLDRKQSM NGCAKKRFEN YKMQPLDLVF RPEFKGKLSQ
YNLDPNRRTP TGIRAAIIRE KGTNGEREMA YSLYLAGFDV KDVTMTDLIS GRETLEDVNM
VVYCGGFSNS DVLGSAKGWA GAFLFNPKAK EALDKFYARE DTLSLGVCNG CQLMMELGLI
TPDHEKKGKM LHNDSHKFES TFIGLTIPTN RSVMFGSLSG SKLGIWVAHG EGKFSLPYDE
DRYNVVAKYT YDEYPGNPNG SDYSVAALAS ADGRHLAIMP HLERSIFPWQ NGYYPENRIH
NDEVTPWIEA FVNARKWVEE KTNKR
//
