PUR4_SHEON
ID PUR4_SHEON Reviewed; 1293 AA.
AC Q8EC57;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=SO_3287;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN56285.1; -; Genomic_DNA.
DR RefSeq; NP_718841.1; NC_004347.2.
DR RefSeq; WP_011073168.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EC57; -.
DR SMR; Q8EC57; -.
DR STRING; 211586.SO_3287; -.
DR PaxDb; Q8EC57; -.
DR KEGG; son:SO_3287; -.
DR PATRIC; fig|211586.12.peg.3192; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 26038at2; -.
DR PhylomeDB; Q8EC57; -.
DR BioCyc; SONE211586:G1GMP-3064-MON; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000008186; 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; Reference proteome.
FT CHAIN 1..1293
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100419"
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; 140598 MW; 6F4E26B7A350CB05 CRC64;
MEIIRGAPAL STFRVQKLME ACVSAALPVR QIYAEYVHLA DLSELLKPTE REQLEKILTY
GPAIEAHTPQ GSLLFVTPRP GTISPWSSKA TDIAHNCGLG KVKRLERGIA YYVESDTLTA
EQQRTLQGLL HDRMVEVVLN DFAKADVLFK RTEPAPFKSV NVLAEGRRAL EVANVEMGLA
LAEDEIDYLV ENFVRLNRNP NDIELMMFAQ ANSEHCRHKI FNADWTIDGK AQPKSLFKMI
KNTFEVTPDH VLSAYKDNAA VMEGSVAGRF FPDPNGVYSY HTEPMHVLMK VETHNHPTAI
SPYPGAATGS GGEIRDEGAT GRGSKPKAGL TGFSVSNLKI PGFVQPWEGN YGKPDRIVSA
LDIMTEGPLG GAAFNNEFGR PALLGYFRTY EQEVSSHNGV EMRGYHKPIM LAGGLGNIRE
EHVQKGEITV GAKLIVLGGP AMNIGLGGGA ASSMASGQSS EDLDFASVQR ENPEMERRCQ
EVIDRCWQLG DKNPIQFIHD VGAGGLSNAF PELVNDGDRG GIFNLRNVPS DEPGMSPLEI
WCNESQERYV LSVAAEDLPL FTAICERERA PFAVVGEAIQ EQHLTLADSH FDNNPIDLPL
EVLLGKAPKM SRNVVSAKAV SPALEQSQID VKDAVKRVLS LPTVADKTFL ITIGDRTVTG
LVNRDQMVGP WQVPVADCAV TAASFDTYAG EAMSLGERTP LALLDFGASA RMAVAESIMN
IAGADIGSFK RIKLSANWMS AAGHPGEDAG LYEAVKAVGE ELCPELSLTI PVGKDSMSMK
TAWQQDGVNK TVTSPMSLVI TAFGVVQDIR NTVTPELRSD KGETSLLLVD LGAGQNRLGG
SCLAQVYGEL GDVAPDLDDA ALLRGFFETM QKLVANKLVI AYHDRSDGGL FTTLVEMAFA
GNIGLDIDVE DLQGTDLERL FNEELGAVLQ VSRDNAAKIA AQFAIAGVPC HVIGTLADDQ
CITIKDGARE IFSDTRVALR TVWSETTYRM QAMRDNPACA LEEFKLKQDE TDLGLTVNLS
FDPSEDVAAP YILKGAAPKM AILREQGVNS HVEMAAAFDR AGFESRDVHM SDILSGRISL
EEFQGLVACG GFSYGDVLGA GEGWAKSILF NERARNEFSR FFERDSSFAL GVCNGCQMLS
NLKEIIPGSE HWPRFVRNRS ERFEARFSLV EVQQSPSLFF QGMAGSRMPI AVSHGEGHAE
FASAQALALA EASGTIALRF VNGKGEIATQ YPQNPNGSPN GLTGICTTDG RVTLMMPHPE
RVFRTVANSW HPDNWGEDSP WMRMFRNARV NLG
