PUR4_SHEFN
ID PUR4_SHEFN Reviewed; 1293 AA.
AC Q085S1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Sfri_1141;
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400;
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 Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
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; CP000447; ABI70994.1; -; Genomic_DNA.
DR RefSeq; WP_011636615.1; NC_008345.1.
DR AlphaFoldDB; Q085S1; -.
DR SMR; Q085S1; -.
DR STRING; 318167.Sfri_1141; -.
DR PRIDE; Q085S1; -.
DR EnsemblBacteria; ABI70994; ABI70994; Sfri_1141.
DR KEGG; sfr:Sfri_1141; -.
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; UP000000684; 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_0000264594"
FT DOMAIN 1040..1293
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 307..326
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 384..386
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; 140532 MW; 47FF0BB4E625A4F7 CRC64;
MEIIRGAPAL SAFRVQKLME ACENAALPVS QIYAEYVHLA SLSEPLDDNE RLQLETILTY
GPAIESHAPQ GTLLFVTPRP GTISPWSSKA TDIAHNCGLG KVSRLERGIA YYVEASVLTA
EQQKLLQGLL HDRMVEVMLP AFEAAEVLFA RTEPAKFSSV NILAEGRRAL EVANIKLGLA
LADDEIDYLI ENFVRLKRNP NDIELMMFAQ ANSEHCRHKI FNADWTIDGE VQLKSLFKMI
KNTFEVTPDY VLSAYKDNAA VMTGSVAGRF FPDPDGIYNY HTEPMHILMK VETHNHPTAI
SPYPGAATGS GGEIRDEGAT GRGSKPKAGL SGFTVSNLKI PGFVQPWEGD YGKPDRIVTP
LEIMLEGPLG GAAFNNEFGR PAITGYFRTY EQLVSSHNGV EVRGYHKPIM IAGGLGNIRE
DHVQKGEITI GAKLIVLGGP AMNIGLGGGA ASSMASGQSS EDLDFASVQR ENPEMERRCQ
EVIDRCWQLG DTNPIQFIHD VGAGGLSNAF PELVNDADRG GVFNLRNVPS DEPGMSPLEI
WCNESQERYV LSVAPENLQQ FADICARERA PFAVVGEATA EMHLTLADSH FNNKPIDLPL
EVLLGKAPKM SRDVVTAKAV SPALDQTKIE LKDAVKRILT LPTVADKTFL ITIGDRSVTG
LVNRDQMVGP WQVPVADCAV TASSYDSYCG EAMSMGERTP LALLDFDASA RMAVAESIMN
IAGTDIGSFK RIKLSANWMS PAGHPGEDAG LYQAVKAIGE DLCPELGITI PVGKDSMSMK
TAWEDNGTQK TVTSPMSLVI TAFGVVQDIR KTVTPQLRSD KGDSALLMLD LSNGQNRLGG
SCLAQVYSEL GDIAPTLDKT ANLAGFFEVM QQLVADQAVM AYHDRSDGGL FTTLVEMAFA
GNTGLTIDLA SLSGTDLERL FNEEIGAVIQ VSAIDAKAIA AQFEAKGVTC HHIGGLQTAD
KISINDGERV IFADSRTALR TLWSETTYRM QALRDNPECA REEYELKQQA DAPGLTVKLG
FNPSEDVAAP YILKGVAPKM AILREQGVNS HVEMAAAFDR AGFESRDVHM SDILSGRISL
EEFQGLVACG GFSYGDVLGA GEGWAKSILF NDRARDEFSR FFERDSSIAL GVCNGCQMLS
NLKEIIPGSE HWPRFVRNRS ERFEARFSLV EVQQNPSVFF EGMVGSRMPI AVSHGEGLVE
FANAQALANA EASGTIALRY VDGHGQIATQ YPENPNGSAN GLTGICTTDG RVTIMMPHPE
RVFRTVANSW HPDNWGEDSP WMRMFRNARV KIG
