ID A0A257CZJ2_9BURK Unreviewed; 1375 AA.
AC A0A257CZJ2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=CFE43_01285 {ECO:0000313|EMBL:OYT93999.1};
OS Burkholderiales bacterium PBB3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=2015565 {ECO:0000313|EMBL:OYT93999.1, ECO:0000313|Proteomes:UP000216249};
RN [1] {ECO:0000313|EMBL:OYT93999.1, ECO:0000313|Proteomes:UP000216249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBB3 {ECO:0000313|EMBL:OYT93999.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYT93999.1}.
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DR EMBL; NKIK01000001; OYT93999.1; -; Genomic_DNA.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000216249; 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:UP000216249}.
FT DOMAIN 39..158
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 179..228
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 451..608
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 876..1024
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 328..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1219
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1340
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1342
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 330..341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 696
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 697
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 736
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 740
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 917
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1375 AA; 147321 MW; 6C8999F9E39A2FDF CRC64;
MTLHITTFDG SNALSHFRTQ QLLPQLQGIH DKITGVAARF VHLVASDTAP DAVLSGKLAA
LLTYGDPYTG ADDGPTIVVS PRFGTVSPWA SKATDIAHNC GFAVKRIERL VEYRLTLKNG
LLSKTALTTE QLQQVAALLH DRMTESAMLD RGQALDLFKA LQPAPMDHVD VLGGGKDALV
KANTQFGLAL AADEIDYLVN AFTTLGRNPT DVELMMFAQA NSEHCRHKIF NAQFTIDGVA
QDKSMFGMIR NTHQLAPQYM LVAYSDNASV MEGVQVERFT AVAANHLFAK SASSADGMCG
SSYEKHSATN HILMKVETHN HPTAISPFPG ASTGAGGEIR DEGATGRGSK PKAGLTGFTV
SKLWGGMSDQ VGGKPEHIAS PLQIMVEGPL GGAAFNNEFG RPNLLGYFRE YEQTVESNVD
TVQRGYHKPI MIAGGLGIID AGQTHKIEFP AGSLLIQLGG PGMRIGMGGS AASSMATGAN
AAELDFDSVQ RGNPEIERRA QEVINQCWMQ GDQNPILAIH DVGAGGLSNA FPELTNDAGR
GARFDLRAVK LEESGMAPKE IWCNESQERY VMAIAPESLE QFQALCERER CPFAVIGVAT
EERQLKLVDE GAESPVDMPM NVLLGKPPKM HRDVKTVART FKPLDLTGVD IQKAVIDVLA
HPTVASKRFL ITIGDRTVGG LTHRDQMVGP WQVPVADCAV TLADFKGFAG EAMSMGERTP
LAALNAPASG RMAVAEAITN LLATPIELPR VKLSANWMAA CGEPGEDAAL YATVKAVGME
LCPALGISIP VGKDSLSMRT QWTEATTSPS GSAQGASGSA GVARKVTSPV SLIVTGFATL
QDVRGTLTPQ LNATDDTTLV LIDLGKGQHR MAASILAQTL GQTGDTVPDL DDAKDLINLV
NAVNALRAKG QILAYHDRGD GGLLATVAEM AFAGRVGVAL NVDMLVTEGD GISDSRMDVG
DSKNWAGQVG ARREELTLKA LFSEELGVVL QVRTSERSDV MATLREHGLS KFSHFIGKTR
PGTDAAAQDA AIANAGKGEL QIWRDAKSIF TARLADLHQV WDAVSWKIAQ QRDNPVCADA
EHAAAGAEND PGLHVFMPNS VLQLMDSAGE APKNVAPAIL KNRPRLAVLR EQGVNSHVEM
AYAFTEAGFE AYDVHMTDLQ TGRAKLSDFK GVVACGGFSY GDTLGAGIGW ARSITFNEVL
ADQFKAFFAR QDTFGLGVCN GCQMFAELAD IIPGAQDWPR FTTNQSERFE ARLSLVEVLE
SPSLFFKDLA GMRLPIAVAH GEGFANFKYR GNADKAIAAM RYVDNSGAAT EAYPFNPNGS
PGGLTAVTTL DGRFTAMMPH PERVFRNVQM SWTNLDQNAQ SPWMQLWHNA RKWVE
//
