PUR4_PHOLL
ID PUR4_PHOLL Reviewed; 1295 AA.
AC Q7N1Z4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 117.
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=plu3317;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571870; CAE15691.1; -; Genomic_DNA.
DR RefSeq; WP_041381011.1; NC_005126.1.
DR AlphaFoldDB; Q7N1Z4; -.
DR SMR; Q7N1Z4; -.
DR STRING; 243265.plu3317; -.
DR MEROPS; C56.972; -.
DR EnsemblBacteria; CAE15691; CAE15691; plu3317.
DR GeneID; 24169869; -.
DR KEGG; plu:plu3317; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OrthoDB; 26038at2; -.
DR BioCyc; PLUM243265:PLU_RS16495-MON; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000002514; 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..1295
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264584"
FT DOMAIN 1042..1295
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 302..327
FT /note="Disordered"
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 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"
FT BINDING 886
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1295 AA; 142784 MW; D768C7E94B790CC7 CRC64;
MKILRGSPAL SAFRITKLLS VCQEQQLPVN DIYAEYVHFA EINASLSDVD SAKLQQLLKY
GPSLAEHEPQ GTLLLVTPRP GTISPWSSKA TDIAHNCGLS QVVRLERGVA YYIQSGEMSD
TQWQILSSLL HDRMMETVFT QLEQAEKLFS RQQPVPLKRI DILQAGRSAL ETANIELGLA
LASDEIDYLM DAFQKLGRNP TDVELYMFAQ ANSEHCRHKI FNADWIIDSQ AQPKSLFKMI
KNTYEQTPDY VLSAYKDNAA VMEGSAVGRF FASAENGSYD YHQEQAHILM KVETHNHPTA
ISPWPGASTG SGGEIRDEGA TGRGAKPKAG LVGFSVSNLR IPGFEQPWEE DFGKPERIVS
ALDIMMEGPL GGAAFNNEFG RPALLGYFRT YEEKVNSHNG SELRGYHKPI MLAGGIGNIR
DEHVKKGEIS VGAKLIVLGG PSMNIGLGGG AASSMASGQS DADLDFASVQ RDNPEMERRC
QEVIDRCWQL GENNPILFIH DVGAGGLSNA MPELVSDGGR GGRFELRKIL NDEPGMSPLE
VWCNESQERY VLAVAPEQLP LFEEICRRER APYAIIGEAT EERHLLLNDE HFDNQPIDMP
LDVLLGKTPK MLRDVTTLKA SGESLERRDI DLAEAVKRIM HLPAVAEKTF LITIGDRSVT
GMVSRDQMVG PWQIPVADCA VTTASLDSYY GEAMSMGERA PVALLDFAAS ARMAVGEALT
NIASAYIQDL KRIKLSANWM SAAGHPGEDA GLYAAVKAVG EELCPALGLT IPVGKDSMSM
KTRWHDQGEE REMTAPLSLV ITAFARVEDV RRTVTPELST DEDNALLLID LGQGKNTLGG
TALAQVYRLL GNKTADVRSA EQLAGFFNAI QQLIAEQKLL AYHDRSDGGL LVTLAEMAFA
GHCGIEADIS VFDEDILAGL FTEELGAVVQ IRASDRGFVE SILAEHGLAD CVHYLGKAQA
GDDFVIFSGN TEVYRQNRST LRLWWAETTW QMQRLRDNPA CADQEHQAKQ DNQDPGLNVK
LTFDISEDIA APYILQQVRP KVAVLREQGV NSHVEMAAAF HRAGFEAIDV HMSDLLSGRI
GLSQFQTLVA CGGFSYGDVL GAGEGWAKSI LFNERVRDQF AVFFARPDTL ALGVCNGCQM
MSNLRELIPG AEHWPRFVRN RSERFEARFS LVEITDSPSL FLQDMVGSRI PIAVSHGEGQ
VEFRNRQHLE MLESNQLVAL RYVNNYGQVT ENYPANPNGS VNGITAVTSL DGRATVMMPH
PERVSRTVNN SWHPDEWRED GPWMRIFRNA RKQLG
