PUR4_NEIMA
ID PUR4_NEIMA Reviewed; 1320 AA.
AC Q9JWC5; A1IPQ9;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
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=NMA0445;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
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; AL157959; CAM07730.1; -; Genomic_DNA.
DR PIR; G81961; G81961.
DR RefSeq; WP_002247094.1; NC_003116.1.
DR AlphaFoldDB; Q9JWC5; -.
DR SMR; Q9JWC5; -.
DR PRIDE; Q9JWC5; -.
DR EnsemblBacteria; CAM07730; CAM07730; NMA0445.
DR KEGG; nma:NMA0445; -.
DR HOGENOM; CLU_001031_0_2_4; -.
DR OMA; LSANWMW; -.
DR BioCyc; NMEN122587:NMA_RS02260-MON; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000000626; 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.
FT CHAIN 1..1320
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100410"
FT DOMAIN 1069..1320
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1162
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1285
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1287
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 311..322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 678
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 679
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 722
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 1320 AA; 143791 MW; FEB32DC315CEDD50 CRC64;
MSVVLPLRGV TALSDFRVEK LLQKAAALGL PEVKLSSEFW YFVGSEKALD AATVEKLQAL
LAAQSVEQTP KAREGLHLFL VTPRLGTISP WASKATNIAE NCGLAGIERI ERGMAVWLEG
ALTDEQQQQW AALLHDRMTE SVLPDFQTAS KLFHHLESET FSTVDVLGGG KEALVKANTE
MGLALSADEI DYLVENYQAL QRNPSDVELM MFAQANSEHC RHKIFNADFI LNGEKQPKSL
FGMIRDTHNA HPEGTVVAYK DNSSVIEGAK VERFYPNAAE NQGYRFHEED THIIMKVETH
NHPTAIAPFA GAATGAGGEI RDEGATGKGS RPKAGLTGFT VSNLNIPGLK QPWEQDYGKP
EHISSPLDIM IEGPIGGAAF NNEFGRPNLL GYFRTFEEKF DGQVRGYHKP IMIAGGLGSI
QAQQTHKDEI PEGALLIQLG GPGMLIGLGG GAASSMDTGT NDASLDFNSV QRGNPEIERR
AQEVIDRCWQ LGDKNPIISI HDVGAGGLSN AFPELVNDAG RGAVFKLREV PLEEHGLNPL
QIWCNESQER YVLSILEKDL DIFRSICERE RCPFAVVGTA TDDGHLKVRD DLFSNNPVDL
PLNVLLGKPP KTTRTDKTVA PSKKPFHAGD IDITEAAYRV LRLPAVAAKN FLITIGDRSV
GGMTHRDQMV GKYQTPVADC AVTMMGFNTY RGEAMSMGEK PTVALFDAPA SGRMCVGEAI
TNIAAANIGD IGNIKLSANW MAACGNEGED EKLYRTVEAV SKACQALDLS IPVGKDSLSM
KTVWQDGEEK KSVVSPLSLI ISAFAPVQDV RKTVTPELKN VEDSVLLFVD LGFGKARMGG
SAFGQVYNNM SGDAPDLDDT SRLKAFYNVI QQLVAEDKLL AYHDRSDGGL FAVLVEMAFA
GRCGLDIDLN LLLAQTFITN HTALSQSLRT EEVKALAEWQ ETIARTLFNE ELGAVIQVRK
QDVADIINLF YQQQLHHNVF EIGTLTDENT LIIRDGQTHL ISDNLIKLQQ TWQETSHQIQ
RLRDNPACAD SEFALIGDNG RSALFANLKF DVNEDIAAPF INSGAKPKIA ILREQGVNGQ
IEMAAAFTRA GFDAYDVHMS DLMAGRVHLA DFKMLAACGG FSYGDVLGAG KGWAKSILFH
PALRDQFAAF FTDPNTLTLG VCNGCQMVSN LAEIIPGTAG WPKFKRNLSE QFEARLSMVH
VPKSASLILN EMQGSSLPVV VSHGEGRADF ALHGGNISAD LGIALQYVDG QNQITQTYPL
NPNGSPQGIA GVTNADGRVT IMMPHPERVY RAAQMSWKPE DWTELSGWYR LFAGARKALG
