PUR4_YERPA
ID PUR4_YERPA Reviewed; 1296 AA.
AC Q1C5E7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 98.
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=YPA_2360;
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(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=ABG14325.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000308; ABG14325.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002211561.1; NZ_CP009906.1.
DR AlphaFoldDB; Q1C5E7; -.
DR SMR; Q1C5E7; -.
DR EnsemblBacteria; ABG14325; ABG14325; YPA_2360.
DR GeneID; 57975875; -.
DR KEGG; ypa:YPA_2360; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000001971; 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..1296
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264602"
FT DOMAIN 1043..1296
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 304..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1136
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1261
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1263
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 885
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 887
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1296 AA; 142048 MW; 338EB52821A8888A CRC64;
MEILRGSPAL SAFRITKLLS RCQDAHLLVS DIYAEYVHFA DVSAPLSADE HARLQRLLQY
GPSLPEHPPA GRLLLVTPRP GTISPWSSKA TDIAHNCGLS QILRLERGLA FSIQGPDLNE
SQWKQLAALL HDRMMEAVFT DLQQAEQLFS HHQPAPVQRV DILGQGRSAL EQANIKLGLA
LAQDEIDYLL TAFTGLGRNP TDIELYMFAQ ANSEHCRHKI FNADWVIDGV VQPKTLFKMI
KNTFEHTPDY VLSAYKDNAA VMEGSQVGRF YATAEKGIYD YHQEEAHILM KVETHNHPTA
ISPWPGAATG SGGEIRDEGA TGRGAKPKAG LVGFSVSNLR IPGFEQPWEE NFGKPDRIVT
ALDIMTEGPL GGAAFNNEFG RPALLGYFRT YEERVNSHNG IELRGYHKPI MLAGGLGNIR
ADHVQKGEIT VGAKLVVLGG PSMNIGLGGG AASSMASGQS DADLDFASVQ RDNPEMERRC
QEVIDRCWQL GEYNPILFIH DVGAGGLSNA MPELVNDGGR GGRFELRDIL NDEPGMSPLE
VWCNESQERY VLAVAPAQMA LFDEICRRER APYAVIGEAT EEKHLLLNDR HFGNQPIDMP
LDVLLGKTPK MLRDVTRLQA KGDALQRADI SLAEAVKRIM HLPAVAEKTF LITIGDRTVT
GMVTRDQMVG PWQIPVADCA VTSASLDSYY GEAMSLGERA PVALLDFAAS ARLAVGEALT
NIAATQIGEL KRIKLSANWM SAAGHPGEDA GLYDAVRAVG EELCPALEIT IPVGKDSMSM
KTRWQEGHEQ REMTSPLSLV ITAFARIEDV RRTVTPQLRT DKGDNALLLI DLGAGHNALG
ATALTQVYRQ LGDKPADVRN VQQLAGFFNA MQRLVADQHL LAYHDRSDGG LLVTLAEMAF
AGHCGVTVDI QSLGNDALAA LFNEELGAVI QVRAEQRADV EKLLADHGLA NCVHYLGRAV
AGDTFDIRSG TDVVYSEKRS TLRLWWAETS WQMQRLRDNP DCADQEHQAK QDESDPGLNV
KLTFDPAEDI AAPFILKQAR PKVAVLREQG VNSHVEMAAA FHRAGFDAVD VHMSDLLAGR
TDLQSFQTLV ACGGFSYGDV LGAGEGWAKS ILFNDRVRDE FEAFFHRPTT LALGVCNGCQ
MMSNLRELIP GAEHWPRFVR NLSDSFEARF SLVEVASSPS LFMQDMVGSR MPIAVSHGEG
QVEVRDAAHL AALEQSHLVA LRFVNNHGVV TEQYPANPNG SANGITAVTS VSGRATVMMP
HPERVFRTVS NSWHPEEWGE DSPWMRMFRN ARKQLG
