ID A0A3F2V2T7_9GAMM Unreviewed; 1294 AA.
AC A0A3F2V2T7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=D6160_12180 {ECO:0000313|EMBL:RLP54090.1};
OS Ketobacter sp.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Ketobacteraceae; Ketobacter.
OX NCBI_TaxID=2083498 {ECO:0000313|EMBL:RLP54090.1, ECO:0000313|Proteomes:UP000280615};
RN [1] {ECO:0000313|EMBL:RLP54090.1, ECO:0000313|Proteomes:UP000280615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BinD {ECO:0000313|EMBL:RLP54090.1};
RA Xu J.;
RT "Metagenomic reconstruction reveals the metabolic diversity of the novel
RT genus Ketobacter and the trajectory of genomic evolution within the
RT Alcanivoraceae family.";
RL Submitted (SEP-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}.
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:RLP54090.1}.
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DR EMBL; RAHY01000009; RLP54090.1; -; Genomic_DNA.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000280615; 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 InterPro; IPR001763; Rhodanese-like_dom.
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.
DR PROSITE; PS50206; RHODANESE_3; 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:UP000280615}.
FT DOMAIN 86..121
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT ACT_SITE 1134
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1259
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1261
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 307..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 678
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 679
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 718
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 722
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 886
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 888
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1294 AA; 140947 MW; F02919C0534C005C CRC64;
MLQLRGAPAL SAFRRNNLLS ELQEKIPAIE GVYAEFMHFA ELAEPLDEAE NRVLQSILRY
GPAVTSEQAA GQLLLVVPRP GTISPWSSKA TDIAHNCGLA KVSRLERGVA YYLQAEQPLD
ELQLQQVSAL LHDRMVEAVL PELEQAEALF RHNEPAPLAE VDVLAQGRQA LEQANQVLGL
ALAEDEIDYL LHSFNELKRN PTDVELMMFA QANSEHCRHK IFNADWVVDG KPQTHSLFKM
IKNTYQAGGE GVLSAYSDNA AVMEGFDAGR FYPDPVSKEY QFHQEPVHIL MKVETHNHPT
AIAPFPGAAT GAGGEIRDEG ATGRGSRPKA GLTGFTVSNL NIPGFTQPWE QPYGKPGRIV
SALDIMIEGP LGGAGFNNEF GRPNINGYFR TYEQQVKTVN GDEVRGYHKP IMIAGGFGNI
KEDHVDKGEI SVGAKLVVLG GPAMLIGLGG GAASSMATGA SAEDLDFASV QRDNPEIERR
CQEVIDQCWQ LGDDNPIDFI HDVGAGGLSN AMPELVKDGG RGGRFDLRAI PNDEPGMSPL
AIWCNESQER YVMAVANENL ERFEAICERE RCPYAVIGEA TNAMHLQLDD AHFENKPVDL
PMPVLFGKPP KMLREYQTQT VQQSAIDTGA LNLKEAVYRV LRLPAVASKK FLITIGDRTV
TGLVTRDQMV GPWQVPVADL AVTTSTLDSF TGEAMAMGER TPAALINAPA SGRMAIGEAI
TNIAAARIGK LADVRLSANW MCAAGYPGED QALFETVRAV GMELCPQLGI TIPVGKDSMS
MRTVWQDEDM SKSVTAPMSL IITAFAPVKD VRKTQTPQLQ TDVGDTRLLL IDLGNGENRL
GASALAQVYQ QLGDRCADLE SSAQLKGFFE VTQSLLQTDN LLAYHDRSDG GLLTSLCEMM
FASHCGVGVD ITALGDAIPA LFNEELGAVI QVRSDAAAGI IEQYKSSGVT VYDLGAPNQS
HHLEIEHGGQ LLLNESRITL EQAWAETSYR IQSLRDNSLC AEQEYEQIAK QDDPGMTPIL
TFDPQENICT PFINVGAKPK IAILREQGVN GQIEMAGAFH AAEFTPVDVH MSDILSGRVN
LRNFNALVAC GGFSYGDVLG AGEGWAKSIL FNLRAREQFE QFFARTDVFA LGVCNGCQMM
SNLHELIPGA DNWPHFVRNQ SERFEARVSM VEVMESGSIL LQGMAGSHLP IAVAHGEGRA
EFASEQQLSA AQQSNSVALR YVDSNGQATE TYPANPNGTP QGITGLTNQD GRITIMMPHP
ERVYRSVQNS WRPPGWGEDG VWLRLFRNGR QWLG
//
