PUR4_SODGM
ID PUR4_SODGM Reviewed; 1295 AA.
AC Q2NS22;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAMS {ECO:0000255|HAMAP-Rule:MF_00419};
DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00419};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAR amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419};
DE Short=FGAR-AT {ECO:0000255|HAMAP-Rule:MF_00419};
GN Name=purL {ECO:0000255|HAMAP-Rule:MF_00419}; OrderedLocusNames=SG1778;
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans;
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(2006).
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:0000255|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:0000255|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. {ECO:0000255|HAMAP-
CC Rule:MF_00419}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00419}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00419}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000255|HAMAP-Rule:MF_00419}.
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DR EMBL; AP008232; BAE75053.1; -; Genomic_DNA.
DR RefSeq; WP_011411602.1; NZ_LN854557.1.
DR AlphaFoldDB; Q2NS22; -.
DR SMR; Q2NS22; -.
DR STRING; 343509.SG1778; -.
DR EnsemblBacteria; BAE75053; BAE75053; SG1778.
DR KEGG; sgl:SG1778; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 26038at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000001932; Chromosome.
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-KW.
DR Gene3D; 3.30.1330.10; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.650.10; -; 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 Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF55326; SSF55326; 2.
DR SUPFAM; SSF56042; SSF56042; 2.
DR SUPFAM; SSF82697; SSF82697; 1.
DR TIGRFAMs; TIGR01735; FGAM_synt; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glutamine amidotransferase; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..1295
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264600"
FT DOMAIN 1042..1295
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 304..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1135
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1260
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1262
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 306..317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 385..387
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 677
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 678
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 717
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 721
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 884
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1295 AA; 141057 MW; 9A0E14C09C612DF8 CRC64;
MEILRGSPAL SAFRINKLLV RCRDARLAVD DIYAEYIHFA DVSAALDEDA LSRLQRLLKY
GPSLAEHQPQ GRLLLVTPRP GTRSPWSSKA TDIAHNCGLP QIKRLERGLA YYIQAPQLSE
PQWGYLAALL HDRMMETVFT RLEEAAALFA QHAPAPVTLV DVLGEGRGAL EAANLALGLA
LAQDEIDYLF AAFTRLGRNP SDVELYMFAQ ANSEHCRHKI FNADWVIDGQ PQAKSLFKMI
KNTFEQTPEY VLSAYKDNAS VMEGSAVGRF FPDAQAGRYD YHQEATHILM KVETHNHPTA
ISPWPGAATG SGGEIRDEGA TGRGAKPKAG LVGFSVSNLR IPGFEQPWEE DFGRPERIVS
ALDIMTDGPL GGAAFNNEFG RPALTGYFRT YEERVDSHNG VELRGYHKPV MLAGGIGNIR
ASHVQKGEIS VGAKLIVLGG PAMNIGLGGG AASSMASGQS DADLDFASVQ RDNPEMERRC
QEVIDRCWQR GEENPILFIH DVGAGGLSNA MPELVSDGGR GGRFQLREIP NDEPGMSPLE
VWCNESQERY VMAVAPERLA EFDAICRREC APYAVIGEAT DALHLSLDDA HYDNRPIDLP
LDVLLGKTPK MQREAVSLQA AGFPLNRDGI KLAEAINRVL HLPAVAEKTF LITIGDRSVT
GMVARDQMVG PWQVPVADCA VTTASLDSYY GEAMSLGERA PVALLNFAAS ARLAVGEALT
NLAATHIGDI KRVKLSANWM AAAGHPGEDA GLYQAVKAVG EELCPALGLT IPVGKDSMSM
KTRWQHGAES REMTAPLSLV ITAFARVEDV RATVTPQLQP ARDNVLLLID LGAGHHALGA
TALAQVYRQL GDETSDVRDA GQLAAFFRVM QQLVAQGWLL AYHDRADGGL LVTLAEMAFA
GHCGIDADIG PLGDDALAAL FNEELGAVIQ IDEADRDAIT ALFHQEGLAD CLHYLGTAQP
GDRFILRAGE RSLYSESRTT LRTWWAETSW QMQRLRDNPE SADQEHASRQ DDNDPGLTVA
LSFDPKDDIA APFIAKGARP KVAVLREQGV NSHVEMAAAF HRAGFEAIDV HMSDLFTGVQ
TLEGFHTLVA CGGFSYGDVL GAGEGWAKSV LFNLRVRDEF EAFFHRPQTL ALGVCNGCQM
MSNLRELIPG AELWPRFVRN KSERFEARFS LVEVTQSQSL LLQGMVGSRL PIAVSHGEGR
VEVRDAAHLA AIEHAGLVAL RYVDNYGKVT ENYPANPNGS PNGITAVTNA SGRVTLTMPH
PERVFRTVSH SWHPAEWGED GPWMRLFRNA RKQLG
