ID Y0KFB5_9PROT Unreviewed; 1311 AA.
AC Y0KFB5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=Meth11DRAFT_0767 {ECO:0000313|EMBL:EUJ09963.1};
OS Methylophilaceae bacterium 11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae.
OX NCBI_TaxID=1101195 {ECO:0000313|EMBL:EUJ09963.1, ECO:0000313|Proteomes:UP000022668};
RN [1] {ECO:0000313|EMBL:EUJ09963.1, ECO:0000313|Proteomes:UP000022668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11 {ECO:0000313|EMBL:EUJ09963.1,
RC ECO:0000313|Proteomes:UP000022668};
RG DOE Joint Genome Institute;
RA Chistoserdova L., Huntemann M., Han J., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Palaniappan K., Ivanova N., Schaumberg A.,
RA Pati A., Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JUL-2013) 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:EUJ09963.1}.
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DR EMBL; JCKJ01000001; EUJ09963.1; -; Genomic_DNA.
DR STRING; 1101195.Meth11DRAFT_0767; -.
DR PATRIC; fig|1101195.3.peg.749; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000022668; 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:UP000022668}.
FT DOMAIN 44..161
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 182..231
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 443..600
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 851..981
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1151
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1276
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1278
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 317..328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 689
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 690
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 729
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 733
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 902
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 904
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1311 AA; 142066 MW; 13383770A24FD11E CRC64;
MSSTQSSTSC LSLRGSAALS QFRLEKLYAT LKQSVPSIQH LYTEFVHFAF SDNALSASDQ
STLKEILTYG PATTTETPAG ELFLVIPRIG TISPWASRAT DIANNCGLDN ILRLERGIAY
YVTTQNGQPL SDAEKAAFKA AIHDRMTETV VSQLQDAEKL YHHAAPKPLN TIDILHGGKP
ALEAANNEMG LALSPDEVDY LLENYQKMGR NPTDVELMMF AQANSEHCRH KIFNADWVID
GVQQEISLFG MIRNTHKLNP GSTVVAYSDN SSIVAGQKTQ RFYPNKSGEY RFVEDDMHYL
MKVETHNHPT AISPFAGAAT GAGGEIRDEG ATGIGSKPKA GLTGFSVSNL NLPDLKQPWE
KPYGKPSRIA TPLQIMIDGP LGGAAYNNEF GRPNIAGYFR TFELEAQDAQ GNAEVRGYHK
PIMLAGGVGN ISDQHAFKDA IPPGAALIQL GGPAMLIGLG GGAASSMDTG ANTENLDFDS
VQRGNPELQR RAQEVIDRCW QLGDQNPIVS IHDVGAGGIS NAFPELVNDA KVGAVFQLRN
VNNEEPGMSP RELWSNEAQE RYVMAVAKEN LALFEDICAR ERCPFAIVGI ATEARHLTVE
DSHFANKPVD MELSVLLGKP PKMTRDVKST PKQLTAFDTS KIDLKEAAAR VLRLPGVADK
TFLITIGDRS VTGLIARDQM VGPWQVPVAD VAVTLAGYQT NVGEAFAIGE KAPIALINAP
ASGRMAIGEA ITNIAASWIS DIGNLKLSAN WMAPAGHAGE DAALFNTVKA VGMELCPALG
ISIPVGKDSM SMKTVWEEDG AKKAVTSPIS LVISAFANTQ DVRKTLTPQL RTSVDNKQLG
DTSLILIDLG NGKNRMGGSS LAQVYSQLGD QAPDVDNPAQ LKQLFTQIQA LNTDNKLLAY
HDRSDGGLFA TLTEMAFAGH CGIDVDLNTL QGDAISALFN EELGAVLQVR ASDASAILAQ
LNNALGHCAH LIGTVNNGHQ IHISKDQVQF ADSRVNLHRA WSETTYHMQS LRDNPACAQQ
EYDRILNEAD AGMHAHLTFN MQEDIAAPYI NTGARPNMAV LREQGVNGQT EMAAAFDRAG
FNSIDVHMSD VIAGRVSLKD FAGLVACGGF SYGDVLGAGE GWAKSILFNT RARDEFSAFF
NRSDSFALGV CNGCQMMSNL HSIIPGSAHW PHFVRNKSEQ FEARFAMVEV LESPSMFFNG
MAGSRMPIAV AHGEGFTEFS DKSAVTTVLN EKLATMRFID HASTPTEVYP FNPNGSPQGL
TGFTTTDGRF SIMMPHPERV FRAVQHSWRP DDWQEDGPWM RMFRNARKFI A
//
