PUR4_SHESR
ID PUR4_SHESR Reviewed; 1293 AA.
AC Q0HX47;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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};
GN OrderedLocusNames=Shewmr7_1309;
OS Shewanella sp. (strain MR-7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-7;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL Submitted (AUG-2006) 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: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; CP000444; ABI42308.1; -; Genomic_DNA.
DR RefSeq; WP_011625661.1; NC_008322.1.
DR AlphaFoldDB; Q0HX47; -.
DR SMR; Q0HX47; -.
DR MEROPS; C56.972; -.
DR EnsemblBacteria; ABI42308; ABI42308; Shewmr7_1309.
DR KEGG; shm:Shewmr7_1309; -.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 26038at2; -.
DR UniPathway; UPA00074; UER00128.
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..1293
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264596"
FT DOMAIN 1040..1293
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 305..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1133
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1258
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1260
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 305..316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 677
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 716
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 720
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"
FT BINDING 886
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1293 AA; 140417 MW; 76DD4E9195567E59 CRC64;
MEIIRGAPAL STFRVQKLME ACVNAALPVR QIYAEYVHLA DLSELLETNE REQLEKILTY
GPAIEAHTPQ GLLLFVTPRP GTISPWSSKA TDIAHNCGLG KVKRLERGVA YYVESDTLTV
EQQQTLKGLL HDRMVEVVLD DFAKADVLFK RTEPAPFKSV NVLAEGRRAL EVANVEMGLA
LAEDEIDYLV ENFVRLNRNP NDIELMMFAQ ANSEHCRHKI FNADWTIDGE AQPKSLFKMI
KNTFETTPDH VLSAYKDNAA VMEGSVAGRF FPDPNGVYSY HTEPMHVLMK VETHNHPTAI
SPYPGAATGS GGEIRDEGAT GRGSKPKAGL TGFSVSNLKI PGFVQPWEGS YGKPDRIVSA
LEIMTEGPLG GAAFNNEFGR PALLGYFRTY EQEVSSHNGV EVRGYHKPIM LAGGLGNIRE
EHVQKGEITV GAKLIVLGGP AMNIGLGGGA ASSMASGQSS EDLDFASVQR ENPEMERRCQ
EVIDRCWQLG DKNPIQFIHD VGAGGLSNAF PELVNDGGRG GIFNLRNVPS DEPGMSPLEI
WCNESQERYV LSVAAEDLPL FTAICERERA PFAVVGEATQ EQHLTLADSH FDNNPIDLPL
EVLLGKAPKM SRNVVSAKAV SPALEQSNID VKEAVKRILS LPTVADKTFL ITIGDRTVTG
LVNRDQMVGP WQVPVADCAV TAASFDTYAG EAMSMGERTP LALLDFGASA RMAVAESIMN
IAGADIGSFK RIKLSANWMS AAGHPGEDAG LYEAVKAVGE ELCPELSLTI PVGKDSMSMK
TAWQQDGANK TVTAPMSLVI SAFGVVQDIR NTVTPELRSD KGETSLLLVD LGAGKNRLGG
SCLAQVYGEL GDIAPDLDDA ALLRGFFETM QKLVAKKSVI AYHDRSDGGL FTTLVEMAFA
GNTGLAIDLS ALQGTDVERL FNEELGGVLQ VSRADAELIA AQFAQAGVPC HMIGSLANDQ
RVTIKDGARE VFSETRVALR TLWSETTYRM QALRDNPACA LEEFKLKQDK TDLGLTVNLS
FDPSEDVAAP YILKGAAPKM AILREQGVNS HVEMAAAFDR AGFESRDVHM SDILSGRISL
EEFQGLVACG GFSYGDVLGA GEGWAKSILF NERARDEFSR FFERDSSFAL GVCNGCQMLS
NLKEIIPGSE HWPRFVRNRS ERFEARFSLV EVQQSPSLFF QGMAGSRMPI AVSHGEGHAE
FASAQALALA EASGTIALRF VNGNGEIATQ YPQNPNGSPN GLTGICTTDG RVTLMMPHPE
RVFRTVANSW HPDNWGEDSP WMRMFRNARV NLG
