PUR4_PHOPR
ID PUR4_PHOPR Reviewed; 1322 AA.
AC Q6LU24;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=PBPRA0788;
OS Photobacterium profundum (strain SS9).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9;
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(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}.
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; CR378665; CAG19201.1; -; Genomic_DNA.
DR RefSeq; WP_011217543.1; NC_006370.1.
DR AlphaFoldDB; Q6LU24; -.
DR SMR; Q6LU24; -.
DR STRING; 298386.PBPRA0788; -.
DR PRIDE; Q6LU24; -.
DR EnsemblBacteria; CAG19201; CAG19201; PBPRA0788.
DR KEGG; ppr:PBPRA0788; -.
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; UP000000593; Chromosome 1.
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..1322
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264583"
FT DOMAIN 1069..1322
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 1287
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1289
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 307..318
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 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 886
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1322 AA; 144157 MW; B93E5AD4EB87759D CRC64;
MEILRGSPAL SEFRVNKLLE RCRELDLPVS GIYAEFMHFA DVSAPLNSDE QSKLASLLTY
GPTIAEHEPT GTMLLVTPRP GTISPWSSKS TDIAQNCALG NVKRLERGTA YYVEVTADLT
NAQLTDLKAL IHDRMMEVVF TDVDSAAALF TQAEPAPVQS VDILVGGRKA LEDANLKLGL
ALAEDEIDYL VENFTMLGRN PNDIELMMFA QANSEHCRHK IFNADWTIDG VEQEKSLFKM
IKNTYEKNHE HVLSAYKDNA AVMEGSEVGR FFPNPESRQY NYHQEAAHIL MKVETHNHPT
AISPWPGAST GSGGEIRDEG ATGLGGKPKA GLVGFTVSNL RVPGFEQPWE TDFGKPGRIV
NALEIMLEGP LGGAAFNNEF GRPNLLGYFR TYEEKVTSHN GEEIRGYHKP IMIAGGMGNI
RADHVQKKEI PVGAKLIVLG GPAMNIGLGG GAASSMASGQ SAEDLDFASV QRENPEMERR
CQEVIDRCWQ MGDANPIAFI HDVGAGGISN ALPELVDDGE RGGKFQLRNV PNDEPGMSPL
EIWCNESQER YVMAVAPENL AVFEAICKRE RAPFAVVGEA TEERHLTLED EHFDNTPIDM
PMDILLGKAP KMHRDAKTLK VEGQAIDRSG IELEAATQRV LRLPAVAEKT FLITIGDRSV
TGLVARDQMV GPWQVPVANC AVTAASYDTY HGEAMSMGER TPVALLDFGA SARLAVGEAI
TNIASADIGD MKRINLSANW MSPAGHPGED AGLYEAVKAV GEELCPALGL TIPVGKDSMS
MKTKWEQDGE QKEVTSPLSL VITAFGRVED VRKTVTPQLR TDKGESSLIL IDLGCGQNRL
GATALAQVYK QLGDKPADVD NPELLKGFFY AVQALVRDEK VLAYHDRGDG GLYVTLAEMA
FAGHTGVEVD INTSESDACD DVLAMLFNEE LGAVLQVRTE DLDTVKSVLA EHGLTACSHV
IGTVVDEDVV RIWNGNDRVL EQSRTDLRTV WAETTYQMQA MRDNPAGALQ EFEAKKDNSD
PGLSAQLTFD INEDVAAPFI AAPFITKAPK TGASVVNAPA INLGAKPQMA ILREQGVNSH
VEMAAAFDRA GFEATDVHMS DILSGNVQLE GFNGLVACGG FSYGDVLGAG EGWAKSVLFN
NIARDQFEAF FKRNDTFSLG VCNGCQMMSN LSELIPGSDL WPRFVRNESE RFEARFSLVE
VQKSDSLFFN EMAGSRMPIA VSHGEGRVEV RNGEHLNAIE QSGTVALRYL DNFGNVTQNY
PANPNGSPNG ITGLTTMDGR VTIMMPHPER VFRTVANSWH PDDWNENSPW MRMFRNARVN
LG
