ID A0A0U3MI43_9BURK Unreviewed; 1338 AA.
AC A0A0U3MI43;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000256|HAMAP-Rule:MF_00419};
DE Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00419};
DE Short=FGAMS {ECO:0000256|HAMAP-Rule:MF_00419};
DE EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00419};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000256|HAMAP-Rule:MF_00419};
DE Short=FGAR amidotransferase {ECO:0000256|HAMAP-Rule:MF_00419};
DE Short=FGAR-AT {ECO:0000256|HAMAP-Rule:MF_00419};
GN Name=purL {ECO:0000256|HAMAP-Rule:MF_00419};
GN ORFNames=DES44_2702 {ECO:0000313|EMBL:REG20195.1}, RD2015_2747
GN {ECO:0000313|EMBL:ALV07212.1};
OS Roseateles depolymerans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=76731 {ECO:0000313|EMBL:ALV07212.1, ECO:0000313|Proteomes:UP000060699};
RN [1] {ECO:0000313|EMBL:ALV07212.1, ECO:0000313|Proteomes:UP000060699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42856 {ECO:0000313|EMBL:ALV07212.1,
RC ECO:0000313|Proteomes:UP000060699};
RA Kim K.M.;
RT "Complete genome of Roseateles depolymerans KCTC 42856.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:REG20195.1, ECO:0000313|Proteomes:UP000256283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11813 {ECO:0000313|EMBL:REG20195.1,
RC ECO:0000313|Proteomes:UP000256283};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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.
CC {ECO:0000256|ARBA:ARBA00004920, ECO:0000256|HAMAP-Rule:MF_00419}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00419}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00419}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000256|ARBA:ARBA00008608, ECO:0000256|HAMAP-Rule:MF_00419}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00419}.
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DR EMBL; CP013729; ALV07212.1; -; Genomic_DNA.
DR EMBL; QUMT01000002; REG20195.1; -; Genomic_DNA.
DR RefSeq; WP_058935367.1; NZ_QUMT01000002.1.
DR STRING; 76731.RD2015_2747; -.
DR KEGG; rdp:RD2015_2747; -.
DR PATRIC; fig|76731.3.peg.2811; -.
DR OrthoDB; 9804441at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000060699; Chromosome.
DR Proteomes; UP000256283; Unassembled WGS sequence.
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-UniRule.
DR CDD; cd01740; GATase1_FGAR_AT; 1.
DR CDD; cd02203; PurL_repeat1; 1.
DR CDD; cd02204; PurL_repeat2; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 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 NCBIfam; TIGR01735; FGAM_synt; 1.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF109736; FGAM synthase PurL, linker domain; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR SUPFAM; SSF82697; PurS-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00419}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00419};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_00419};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00419};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00419};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00419};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00419};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_00419}; Reference proteome {ECO:0000313|Proteomes:UP000060699}.
FT DOMAIN 45..172
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 193..242
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 453..610
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 858..1014
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1182
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1303
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1305
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 331..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 699
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 700
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 739
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 743
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 904
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 906
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1338 AA; 143711 MW; 9E87357C4ED73B7A CRC64;
MSSTTSSKYL IHFEGGNALS AFRATALLAR LQAVSDRITA VHARHVHWVW TDHPLDDASQ
GKLAALLNYG DAYEGPSEGA LIVTAPRLGT LSPWASKATD IAHNCGLSIH RVERVTEYRL
TLKGGLLSTV TAGLAGGTKP LTEQELLACA ELLHDRMTES VLLRREDAVH LFDDKQAQPL
AHVDVLSRGR AALDEANGAW GLALSDDEID YLVTAFQRLG RNPSDVELMM FAQANSEHCR
HKIFNAQFTI DGEAQPLSLF GMIRNTEKLH PQHTVIAYAD NAAVMEGHTI ERWMAAGDQR
APRYEARTET AHVLMKVETH NHPTAISPHP GASTGAGGEI RDEGATGRGA KPKAGLTGFS
VSNLQLPGLS EPWEQASIGK PAHIASPLQI MTEGPLGGAA FNNEFGRPAL GGYFRVYEQE
VDGIHRGYHK PIMIAGGVGA IRSDLTKKIE FPAGTLLIQL GGPGMRIGMG GGAASSMAAG
TNTADLDFDS VQRGNPEIQR RAQEVINHCW GLAERNPILA VHDVGAGGIS NAFPELVNDA
GRGARFDLRK VPLEESGLAP KEIWCNESQE RYVLAIAPES LPLFQSMCER ERCPFAVVGV
TTEQRELVLE DGQGGERAID MPMDVLLGKP PKMHRDVKRV ARSGGPLNLD GVDLAQAVTH
VLRHPTVASK RFLITIGDRT VGGLSHRDQM VGPWQVPVAD CAVTLADFKG FAGEAMSMGE
RTPLAAVDAP ASGRMAVAEA ITNLLAAPIE LSRVKLSANW MAACGEAGED AALYDTVKAV
GMELCPALGV SIPVGKDSLS MRTRWSDNGQ TRQVTAPVSL IVSAFASLPD VRGTLTPQLQ
AGDTTLVLID LGQGRQRMGG SILAQTLNQF GPEVPDLDDP ALLNQTVAAV NALRAEGKLL
AYHDRSDGGL LAAAAEMAFA GQRGVSLNVD LLVTEGDGIT DSRADTGDSK NWASQVSGRR
EELTLKALFN EELGVVLQVA TGDRDAVLQT LRAHGLSKLS HVVGKTNDAG QVEVWRDAKK
VFAAPLQQLH QEWDQVSWRI TRDRDNPAFA DQEHALAGAP GGGLHWAPTF DVKEDVAAPF
IQSGVRPKMA ILREQGVNSH VEMAYAMSQA GFDSYDVHMS DLQAGAVDLS QFKGFVACGG
FSYGDTLGAG EGWARSILFN PRLKDAFEAF FARQDSFALG VCNGCQMLAA LSPMIPGAQH
WPKFVRNRSE QFEARLAQVE VLDSPSLFFK GMAGSRLPIA VAHGEGFADF SQRGDAGQVI
QAMRYVDGNG QPTEQYPLNP NGSPGGLTAV TTADGRFTAL MPHPERVFRN IQMSWTGGDP
SAFSPWMRMF RNARVWVG
//
