PUR4_SHESM
ID PUR4_SHESM Reviewed; 1293 AA.
AC Q0HKU9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Shewmr4_1238;
OS Shewanella sp. (strain MR-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60480;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-4;
RG US DOE Joint Genome Institute;
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 Shewanella sp. MR-4.";
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; CP000446; ABI38318.1; -; Genomic_DNA.
DR RefSeq; WP_011622026.1; NC_008321.1.
DR AlphaFoldDB; Q0HKU9; -.
DR SMR; Q0HKU9; -.
DR MEROPS; C56.972; -.
DR KEGG; she:Shewmr4_1238; -.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
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_0000264595"
FT DOMAIN 1040..1293
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 305..327
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; 140365 MW; A2B08AE29B90ECAE CRC64;
MEIIRGAPAL STFRVQKLME ACVNAALPVR QIYAEYVHLA DLSELLETNE REQLEKILTY
GPAIEAHTPQ GSLLFVTPRP 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
LDIMTEGPLG 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
GNTGLSIDLS ALQGTDVERL FNEELGGVLQ VSRADAELIA AQFAQAGVPC HMIGTLANDQ
RVTIKDGARE VFSETRVALR TLWSETTYRM QALRDNPACA LEEFKLKQDE TDLGLTVNLS
FDPSEDVAAP YILKGAAPKM AILREQGVNS HVEMAAAFDR AGFESLDVHM SDILSGRISL
EEFQGLVACG GFSYGDVLGA GEGWAKSILF NERARDEFSR FFERDSSFAL GVCNGCQMLS
NLKEIIPGSE HWPRFVRNRS ERFEARFSLV EVQQSPSLFF QGMAGSRMPI AVSHGEGHAE
FASAQALALA EASGTIALRF VNGNGEIATQ YPQNPNGSPN GLTGICTTDG RVTLMMPHPE
RVFRTVANSW HPDNWGEDSP WMRMFRNARV NLG
