PUR4_PECAS
ID PUR4_PECAS Reviewed; 1294 AA.
AC Q6D238;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=ECA3258;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG76156.1; -; Genomic_DNA.
DR RefSeq; WP_011094776.1; NC_004547.2.
DR AlphaFoldDB; Q6D238; -.
DR SMR; Q6D238; -.
DR STRING; 218491.ECA3258; -.
DR EnsemblBacteria; CAG76156; CAG76156; ECA3258.
DR GeneID; 57209942; -.
DR KEGG; eca:ECA3258; -.
DR PATRIC; fig|218491.5.peg.3302; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 26038at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000007966; 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..1294
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264572"
FT DOMAIN 1041..1294
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 303..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1134
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1259
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1261
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 305..316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 384..386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 677
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 716
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 883
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 885
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1294 AA; 142126 MW; F85AF988A5F34950 CRC64;
MEILRGSPAL SAFRINKLLV RCKEHLLPVS DIYAEYVHFA DVSTPLNNDE QAKLTRLLKY
GPSLAEHEPQ GHLLLVTPRP GTISPWSSKA TDIAHNCGLS KVLRLERGLA FYIHAPTLND
EQWQQLGALL HDRMMESVFS DLKQAAALFS HHQPAPFKRI EILLQGRQAL EEANVRLGLA
LAEDEIDYLL EAFNNLGRNP TDIELYMFAQ ANSEHCRHKI FNADWVIDGV TQPKSLFKMI
KNTFEHTPDH VLSAYKDNAA VMEGSAVGRF YTDANGQYDY HQEDAHILMK VETHNHPTAI
SPWPGAATGS GGEIRDEGAT GRGSKPKAGL VGFSVSNLRI PGFIQPWEEE FGKPDRIVSA
LDIMTEGPLG GAAFNNEFGR PALTGYFRTY EERVDSHNGE ELRGYHKPIM LAGGIGNIRG
DHVKKGEIIV GAKLIVLGGP SMNIGLGGGA ASSMASGQSD ADLDFASVQR DNPEMERRCQ
EVIDRCWQLG EANPILFIHD VGAGGLSNAM PELVSDGGRG GRFELRDILN DEPGMSPLEV
WCNESQERYV LAVAPEQLAQ FDEICRRERA PYAVIGEATE ELHLTMNDRH FNNQPIDLPL
DVLLGKTPKM LRDVERKQVE GTPLQRDDIY LAEAVERVLH LPVVAEKTFL ITIGDRSVTG
MVARDQMVGP WQVPVADCAV TTASLDSYYG EAMSIGERAP VALRNFAASA RLAVGEALTN
IAATHIGPLT RVKLSANWMA AAGHPGEDAG LYDAVKAVGE ELCPALGLTI PVGKDSMSMK
TRWQEEGEDR AVTSPMSLVI SAFARVEDVR NTVTPQLRTG QDNALLLIDL GAGNKALGAT
ALAQVYRQLG RKTADVHSPE QLAGFFNAIQ ELVAAKALLA YHDRSDGGLI VTLAEMAFAG
HCGVTVDIAS QGEDTLATLF NEELGAVIQI PAARRAEVDA ILALHGLADC VHYLGQAEEG
TRFTINQGAE AVYQESRSTL RRWWAETSWQ MQRLRDNPQC ADQEHIARQD DNDPGLNVSL
TFDPKEDIAA PYIAKNVRPK VAVLREQGVN SHVEMAAAFH RAGFDAIDIH MSDLLANRRN
LQDFQALVAC GGFSYGDVLG AGEGWAKSIL FNARVRDEFA EFFLRPQTLA LGVCNGCQMM
SNLRELIPGA DLWPRFVRNK SDRFEARFSL VEVDKSPSLF MNDMAGSRMP IAVSHGEGQV
EVRDDAHLAA IEEHGLVALR YINHYGQVTE NYPANPNGSS NGITAVTSTS GRATVMMPHP
ERVFRTVSNS WHPEEWGEDG PWMRMFRNAR RQLG
