PUR4_ALIF1
ID PUR4_ALIF1 Reviewed; 1303 AA.
AC Q5E749;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=VF_0652;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW85147.1; -; Genomic_DNA.
DR RefSeq; WP_011261382.1; NC_006840.2.
DR RefSeq; YP_204035.1; NC_006840.2.
DR AlphaFoldDB; Q5E749; -.
DR SMR; Q5E749; -.
DR STRING; 312309.VF_0652; -.
DR MEROPS; C56.972; -.
DR EnsemblBacteria; AAW85147; AAW85147; VF_0652.
DR KEGG; vfi:VF_0652; -.
DR PATRIC; fig|312309.11.peg.645; -.
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; UP000000537; Chromosome I.
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..1303
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264601"
FT DOMAIN 1050..1303
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 1003..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1022
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1143
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1268
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1270
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 308..319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 679
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 719
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 723
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 892
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1303 AA; 142181 MW; F07B7FE510D29C72 CRC64;
MRILRGSPAL SEFRVNKLLE LCRELSLPVT GIYAEFAHFA DVTAELDASE VQKLEKLLTY
GPTIEEHEPE GLLLLTTPRP GTISPWSSKS TDIAHNCGLD KIARLERGTA FYIERSEELS
ELQLIELKAI LHDRMMEVVF TDFESASALF AVSEPAPYTE VDLLTGGRKA LEDANVTLGL
ALAEDEIDYL LESFTEKLER NPTDIELMMF AQANSEHCRH KIFNADWTID GVKQEKSLFK
MIKNTFEVTP DNVLSAYKDN AAVMTGSEVG RFFPDPETRQ YNYHQEKTHI LMKVETHNHP
TAISPWPGAS TGSGGEIRDE GATGIGGKPK AGLVAFSVSN LKIPNFVQPW ETDFGKPSRI
VTALDIMLEG PLGGAAFNNE FGRPNLLGYF RTYEEKVNSH AGEEVRGYHK PIMLAGGLGN
IRDEHVQKKE IPVGASLIVL GGPAMNIGLG GGAASSMDSG SSSEDLDFAS VQRENPEMER
RCQEVIDRCW QLGDANPIAF IHDVGAGGIS NALPELVDDG ERGGIFNLRD VPNDEPGMSP
LEIWCNESQE RYVMAVADKD MATFDAICKR ERAPYAVVGK ATEERELKLE DSHFDNTPID
MPMDILLGKT PKMHRDAKTL KANNPAIDRS GIEMNEAVDR VLRLPTVAEK TFLITIGDRS
VTGLVARDQM VGPWQVPVAN CAVTAASYDS YHGEAMSLGE RTPVALLDFG ASARLAVGEA
ITNIAATNIG DIKHIKLSAN WMSPAGHPGE DAGLYEAVKA VGEELCPALG LTIPVGKDSM
SMKTKWEENG EQKEVTSPLS LVITAFARVE DVRKTITPQL RTPDNLEGLG DTSLVLIDLG
NGKNRLGATA LAQVYKQLGD KPADVDNAAQ LKGFYEGVQA LVANDQVVAY HDKGDGGLFV
TLAEMAFAGH CGVNANIEAL GEDTLAALFN EELGAVIQVR NDDLDAVLST LAANGLEACS
HVIGSVEASD ELVIKSGESV VIERNRTELR TIWAETTHKM QGLRDNPACA DQEHEAKKDN
SDPGLNVKLS FDVNEDIAAP FINTGAKPKM AILREQGVNS HVEMAAAFDR AGFEATDIHM
SDILTGQAVL EEYNGLVACG GFSYGDVLGA GEGWAKSVLF NDSTRDQFEN FFKREDTFSL
GVCNGCQMLS NLRDLIPGAE YWPRFVRNES ERFEARFSLV EVQKSDSVFF NGMEGSRMPI
AVSHGEGRVE VRDNDHLNAI ENSGTVALRY VDNHGNPTQQ YPNNPNGSPN AITGLTTTDG
RVTIMMPHPE RVFRTVANSW SPEGWGENGA WMRMFQNARK NIG
