PUR4_MYXXD
ID PUR4_MYXXD Reviewed; 1299 AA.
AC Q1D9V4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 111.
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=MXAN_2349;
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622;
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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=ABF92728.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000113; ABF92728.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q1D9V4; -.
DR SMR; Q1D9V4; -.
DR STRING; 246197.MXAN_2349; -.
DR MEROPS; C56.972; -.
DR EnsemblBacteria; ABF92728; ABF92728; MXAN_2349.
DR KEGG; mxa:MXAN_2349; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_7; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000002402; 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..1299
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264581"
FT DOMAIN 1046..1299
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1139
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1264
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1266
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 310..321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 389..391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 680
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 681
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 724
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 888
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 890
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1299 AA; 139228 MW; F9410F740D48DF96 CRC64;
MHTLRGAPAL SDFRLAKLLA QCRERVPSVS SIYAEFVHLI DAPAPLSEAD LATLGRLLDY
GPRVATGARI GSLLLVLPRP GTISPWSSKA TDIVHNCGLG ERVRRMERGT AFFIAGPDGQ
ALQDAELERL KPVLHDRMTQ AVVGRLEDAA ILFAGHTPRP FTTVDVLGGG RAALVTANRE
LGLALADDEM DYLVARFTEL KRNPTDVELM MFAQANSEHC RHKIFNASWT IDGKPQERSL
FQAIKNTYVQ HKEGVLGAYK DNAAVIEGFE VDRFFPSPES GEWGSVREPA HIMIKVETHN
HPTAISPYPG AATGAGGEIR DEGATGRGAR PKAGLTGFSV SHLRIPGFEQ PWEQPYGKPD
RIVSALDIMV DGPLGGAAFN NEFGRPNLTG YFRSYEVQVP TPGGVEVRGY HKPIMIAGGL
GNIRASHVQK GRLQPGDKLI VLGGPAMLIG LGGGAASSMA QGASAADLDF ASVQRDNAEM
ERRCQEVIDS CWALGDKNPI RSIHDVGAGG LSNAVPELAH DNDLGGRLEL RAVPNAEPGM
SPVEIWCNEA QERYVLGVAP EDLARFAALC ERERAPFSVL GDATAEQTLK LGDTQFGNAP
IDLPMDVLFG KPPRMHRDVT SRPVSFAPLT LDGSLALLAE RVLSHPTVAD KSFLITIGDR
TVSGLSSRDQ MVGPWQVPVA DCAVTLSTVT STTGEAMAMG ERTPLALIDA AASARMAVGE
ALTNIAAARI GKLSDVKLSA NWMAAAGSPG EDASLYAAVH AVGMELCPAL GLTIPVGKDS
MSMRTVWEEG GARKAVTSPV SLIISAFAPV LDVRKSLTPQ LVDVADDTRL LFIDLARGKQ
RLGGSVVAHV HGQVGPESPD VEDPALLRGF FAAVQALSES GSLLAYHDRS DGGLWATLCE
MAFAGRCGLD VDLAPLGGDV TAALFNEELG AVVQVRASDV ARVREVLAQH GLSRDVHELG
RPVTALQVRV RHGGDTLMAE DTLALRRTWS RVSYEMQKLR DNPICADQES AARSDASDPG
LSPKLTFDPA QDVAAPFIAK GARPRVAVLR EQGVNSQQEM AAAFTRAGFA AVDVHMSDIL
SGRVSLEGFK GVLACGGFSY GDVLGAGGGW AKSILFNPRA RDAFAAFFAR PDSFGLGVCN
GCQMMSQLKD IIPGAEHFPR FVRNASEQYE ARLSLVEVSK TPSLFYQGME GSRMLIVTSH
GEGRAEFPSV EDAARVNGLG LVTTRWVDNH GRVAESYPAN PNGSPHGIAG LTTRDGRFTI
TMPHPERVHR SVQHSWRPRE WGDDGPWMRM FRNARVWLG
