ID U6ZXT1_9PSED Unreviewed; 1298 AA.
AC U6ZXT1; A0A7X1PHW4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 58.
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 ECO:0000313|EMBL:MQA52430.1};
GN Synonyms=purI {ECO:0000313|EMBL:MQA52430.1};
GN ORFNames=GDH07_03715 {ECO:0000313|EMBL:MQA52430.1};
OS Pseudomonas piscis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2614538 {ECO:0000313|EMBL:MQA52430.1, ECO:0000313|Proteomes:UP000486534};
RN [1] {ECO:0000313|EMBL:MQA52430.1, ECO:0000313|Proteomes:UP000486534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC042 {ECO:0000313|EMBL:MQA52430.1,
RC ECO:0000313|Proteomes:UP000486534};
RA Liu Y.;
RT "Pseudomonas dajingensis sp. nov., isolated from the profound head ulcers
RT of farmed Murray cod (Maccullochella peelii peelii).";
RL Submitted (OCT-2019) 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: 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:MQA52430.1}.
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DR EMBL; WHUV01000001; MQA52430.1; -; Genomic_DNA.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000486534; 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}.
FT DOMAIN 35..148
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 169..218
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 430..587
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 838..970
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1138
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT ACT_SITE 1263
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT ACT_SITE 1265
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 305..316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 384..386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 677
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 716
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 720
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 884
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 886
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1298 AA; 140327 MW; C4F89CA900826780 CRC64;
MLILRGAPAL SAFRHSKLLE QLSQKVPAVS GLYAEFAHFA EVTGVLTGDE QQVLARLLKY
GPSVPVQEPS GRLFLVLPRF GTISPWSSKA SDIARNCGLA KVQRLERGIA FYVAGEFSEA
DAQLIGDALH DRMTQVVMAN LEQAGGLFSH AEPKPLTAVD ILGGGRAALE KANSELGLAL
AEDEIDYLMT AFQGLARNPH DIELMMFAQA NSEHCRHKIF NASWDIDGQA QEKSLFGMIK
NTYQMHNEGV LSAYKDNAAV IVGSVAGRFF PNPETRQYGA VQEPVHILMK VETHNHPTAI
APFPGASTGS GGEIRDEGAT GRGAKPKAGL TGFTVSNLQI PGFEQPWEVP YGKPERIVDA
LDIMIEGPLG GAAFNNEFGR PALTGYFRTF EQSITTPRGE EVRGYHKPIM LAGGMGNIRD
EHVQKGEITV GSKLIVLGGP AMLIGLGGGA ASSMATGTSS ADLDFASVQR ENPEMERRCQ
EVIDRCWQLG DKNPISFIHD VGAGGLSNAF PELVNDGGRG GRFELRNIPN DEPGMAPHEI
WSNESQERYV LAVGAEDFER FKAICERERC PFAVVGEATA EPQLTVTDSH FGNSPVDMPL
EVLLGKAPRM HRSAVREAEL GDDFDPSTLD VAESIERVLH HPAVASKSFL ITIGDRTITG
LVARDQMVGP WQVPVADVAV TATSFDVYTG EAMAMGERTP LALLDAPASG RMAIGETLTN
LAASRIGKIS DIKLSANWMS AAGHPGEDAR LYDTVKAVGM ELCPELGITI PVGKDSMSMA
TRWSEEGVDK SVTAPLSLIV TGFAPVTDIR QTLTPQLRMD KGTTDLVLID LGRGQNRMGA
SILAQTHGKI GKQAPDVDDA EDLKAFFAVI QGLNADGHLL AYHDRSDGGL LTSAVEMAFA
GHCGLNLNLD ALAASAADIP AILFNEELGA LIQVRQDATP SVLAQFSAAG LGDCVAVIGQ
PVNNGHINIT FNGENVFAGE RRLLQRQWAE TSYQIQRLRD NADCAEQEFD VVLEEDNPGL
SVKLSFDVNQ DIAAPYIKKG VRPQVAVLRE QGVNGQVEMA AAFDRAGFNA IDVHMSDILA
GRVDLNEFKG MVACGGFSYG DVLGAGEGWA KSALFNSRAR DAFQGFFERN DTFTLGVCNG
CQMMSNLHEL VPGSEFWPHF VRNRSEQFEG RVAMVQVQES NSIFLQGMAG SRMPIAIAHG
EGHAEFESEE ALLEADLSGC VALRFVDNHG KVTERYPANP NGSPRGITGL TSRDGRVTIM
MPHPERVFRA VQNSWRPDDW NEDAGWMRMF RNARVWVN
//
