PUR4_NEIMB
ID PUR4_NEIMB Reviewed; 1320 AA.
AC Q9JXK5;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
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=NMB1996;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(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}.
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; AE002098; AAF42323.1; -; Genomic_DNA.
DR PIR; G81017; G81017.
DR RefSeq; NP_274988.1; NC_003112.2.
DR RefSeq; WP_002225870.1; NC_003112.2.
DR AlphaFoldDB; Q9JXK5; -.
DR SMR; Q9JXK5; -.
DR STRING; 122586.NMB1996; -.
DR PaxDb; Q9JXK5; -.
DR EnsemblBacteria; AAF42323; AAF42323; NMB1996.
DR KEGG; nme:NMB1996; -.
DR PATRIC; fig|122586.8.peg.2550; -.
DR HOGENOM; CLU_001031_0_2_4; -.
DR OMA; LSANWMW; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000000425; 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..1320
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100411"
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; 143853 MW; B6B873913EBB06BD CRC64;
MSVVLPLRGV TALSDFRVEK LLQKAAALGL PEVKLSSEFW YFVGSEKALD AATVEKLQAL
LAAQSVEQTP KAREGLHLFL VTPRLGTISP WASKATNIAE NCGLAGIERI ERGMAVWLEG
RLNDEQKQQW AALLHDRMTE SVLPDFQTAS KLFHHLESET FSGVDVLGGG KEALVKANTE
MGLALSADEI DYLVENYQAL QRNPSDVELM MFAQANSEHC RHKIFNADFI LNGEKQPKSL
FGMIRDTHNA HPEGTVVAYK DNSSVIEGAK IERFYPNAAE NQGYRFHEED THIIMKVETH
NHPTAIAPFA GAATGAGGEI RDEGATGKGS RPKAGLTGFT VSNLNIPDLK QPWEQDYGKP
EHISSPLDIM IEGPIGGAAF NNEFGRPNLL GYFRTFEEKF DGQVRGYHKP IMIAGGLGSI
QAQQTHKDEI PEGALLIQLG GPGMLIGLGG GAASSMDTGT NDASLDFNSV QRGNPEIERR
AQEVIDRCWQ LGGKNPIISI HDVGAGGLSN AFPELVNDAR RGAVFKLREV PLEEHGLNPL
QIWCNESQER YVLSILEKDL DAFRAICERE RCPFAVVGTA TDDGHLKVRD DLFANNPVDL
PLNVLLGKLP KTTRTDKTVA PSKKPFHAGD IDITEAAYRV LRLPAVAAKN FLITIGDRSV
GGLTHRDQMV GKYQTPVADC AVTMMGFNTY RGEAMSMGEK PTVALFDAPA SGRMCVGEAI
TNIAAVNIGD IGNIKLSANW MAACGNEGED EKLYRTVEAV SKACQALDLS IPVGKDSLSM
KTVWQDGEEK KSVVSPLSLI ISAFAPVKDV RKTVTPELKN VEDSVLLFVD LGFGKARMGG
SAFGQVYNNM SGDAPDLDDT GRLKAFYSVI QQLVAENKLL AYHDRSDGGL FAVLVEMAFA
GRCGLDIDLN LLLAQTFITN HTALSQSLRT EEVKALAEWQ ETIARTLFNE ELGAVIQVRK
QDVADIINLF YQQQLHHNVF EIGTLTDENT LIIRDGQTHL ISDNLIKLQQ TWQETSHQIQ
RLRDNPACAD SEFALIGDNE RSALFADVKF DVNEDIAAPF INSGAKPKIA ILREQGVNGQ
IEMAAAFTRA GFDAYDVHMS DLMAGRIHLA DFKMLAACGG FSYGDVLGAG EGWAKSILFH
PALRDQFAAF FADPDTLTLG VCNGCQMVSN LAEIIPGTAG WPKFKRNLSE QFEARLSMVH
VPKSASLILN EMQGSSLPVV VSHGEGRADF ALHGGNISAD LGIALQYIDG QNQVTQTYPL
NPNGSPQGIA GVTNADGRIT IMMPHPERVY RAAQMSWKPE GWTELSGWYR LFAGARKALG
