PUR4_NEIG1
ID PUR4_NEIG1 Reviewed; 1314 AA.
AC Q5F7J4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 106.
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=NGO1183;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW89843.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004969; AAW89843.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_208255.1; NC_002946.2.
DR AlphaFoldDB; Q5F7J4; -.
DR SMR; Q5F7J4; -.
DR STRING; 242231.NGO_1183; -.
DR MEROPS; C56.972; -.
DR PRIDE; Q5F7J4; -.
DR EnsemblBacteria; AAW89843; AAW89843; NGO_1183.
DR KEGG; ngo:NGO_1183; -.
DR PATRIC; fig|242231.10.peg.1390; -.
DR HOGENOM; CLU_001031_0_2_4; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000000535; 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..1314
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264582"
FT DOMAIN 1063..1314
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1156
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1279
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1281
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 307..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 674
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 675
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 714
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 718
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 880
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 882
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1314 AA; 142972 MW; B9DD36708873144D CRC64;
MPLRGVTALS DFRVEKLLQK AAALGLPEVK LSSEFWYFAG SEKALDAATV EKLQALLAAQ
SVEQTPEARE GLHLFLVTPR LGTISPWASK ATNIAENCGL AGIERIERGM AVWLEGALTD
EQKQQWAALL HDRMTESVLP DFQTASKLFH HLKSETFSTV DVLGGGKEAL VKANTETGLA
LSADEIDYLV ENYQALQRNP SDVELMMFAQ ANSEHCRHKI FNADFILNGE KQPKSLFGMI
RDTHNAHPEG TVVAYKDNSS VIKGAKIERF YPNAAENQGY RFHEEDTHII MKVETHNHPT
AIAPFAGAAT GAGGEIRDEG ATGKGSRPKA GLTGFTVSNL NIPDLKQPWE QDYGKPEHIS
SPLDIMIEGP IGGAAFNNEF GRPNLLGYFR TFEEKFDGQV RGYHKPIMIA GGLGSIQAQQ
THKDEIPEGA LLIQLGGPGM LIGLGGGAAS SMDTGTNDAS LDFNSVQRGN PEIERRAQEV
IDRCWQLGDQ NPIISIHDVG AGGLSNAFPE LVNDAGRGAV FELREVPLEE HGLTPLQIWC
NESQERYVLS ILEKDLDTFR AICERERCPF AVVGTATDDG HLKVRDDLFS NNPVDLPLNV
LLGKPPKTTR TDKTVTPSKK PFHAGDIDIT EAAYRVLRLP AVAAKNFLIT IGDRSVGGMT
HRDQMVGKYQ TPVADCAVTM MGFNTYRGEA MSMGEKPAVA LFDAPASGRM CVGEAITNIA
AVNIGDIGNI KLSANWMAAC GNEGEDEKLY RTVEAVSKAC QALDLSIPVG KDSLSMKTVW
QDGEEKKSVV SPLSLIISAF APVKDVRKTV TPELKNVEGS VLLFIDLGFG KARMGGSAFG
QVYNNMSGDA PDLDDAGRLK AFYSVIQQLV AEDKLLAYHD RSDGGLFATL AEMAFAARCG
ISADIDCLMD KFLPIHLPDF QGDPAEDLSD ELYNHAAIKI LFNEELGAVI QIRQKDRDYV
DAAFETAGLT DAVSRIGSPD FDNEFISFFG YGYFLEQNRA DLQRAWQETS HAIQRLRDNP
ACADSEFALI GDNERSALFA DVKFDVNEDI AAPFINSGAK PKIAILREQG VNGQIEMAAA
FTRAGFDAYD VHMSDLMAGR FRLADFKMLA ACGGFSYGDV LGAGEGWAKS ILFHPALRDQ
FAAFFADPNT LTLGVCNGCQ MVSNLAEIIP GAETWPKFKR NLSEQFEARL NMVHVPKSAS
LILNEMQDSS LPVVVSHGEG RADFALHGGN ISADLGIALQ YVDGQNQVTQ TYPLNPNGSP
QGIAGITNAD GRVTIMMPHP ERVYRAAQMS RKPEGWTELS GWYRLFAGAR KALG
