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Database: UniProt
Entry: A0A1T5FDU2_9GAMM
LinkDB: A0A1T5FDU2_9GAMM
Original site: A0A1T5FDU2_9GAMM 
ID   A0A1T5FDU2_9GAMM        Unreviewed;      1287 AA.
AC   A0A1T5FDU2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=SAMN05660880_03362 {ECO:0000313|EMBL:SKB94302.1};
OS   Luteibacter sp. 22Crub2.1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=1283288 {ECO:0000313|EMBL:SKB94302.1, ECO:0000313|Proteomes:UP000191150};
RN   [1] {ECO:0000313|EMBL:SKB94302.1, ECO:0000313|Proteomes:UP000191150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22Crub2.1 {ECO:0000313|EMBL:SKB94302.1,
RC   ECO:0000313|Proteomes:UP000191150};
RA   Peterson S.W.;
RL   Submitted (FEB-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}.
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DR   EMBL; FUYT01000016; SKB94302.1; -; Genomic_DNA.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000191150; 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          36..145
FT                   /note="Phosphoribosylformylglycinamidine synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18076"
FT   DOMAIN          166..215
FT                   /note="Phosphoribosylformylglycinamidine synthase linker"
FT                   /evidence="ECO:0000259|Pfam:PF18072"
FT   DOMAIN          424..582
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   DOMAIN          829..944
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   REGION          297..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1131
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1252
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        1254
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   BINDING         302..313
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         672
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         673
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT   BINDING         712
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         880
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
SQ   SEQUENCE   1287 AA;  138880 MW;  DCB9CB825A046654 CRC64;
     MIALDGQSAL SPFRLERLNA HLDALHHGTR VQAAWFTYFV DGSAAPEGEA RARLLAVLEA
     KTTAPENATF WVVPRLGTIS PWSSKATDIL HGAGFDVRRV ERGTAWQVTG MPAAGDPAYA
     SVMAAFCDPM VQSPLTRLDD AAGLFLAGEP GPLGHVELGS DASAALAAAN KELGLALADD
     EIAYLADRYA EMGRPPTDAE LMMFAQANSE HCRHKVFNAS WTLDGKPQDI SLFGMIKNTH
     QKSPAHTLSA YHDNAAVIEG YEGQRLFVDP ADGVFRTVAE SAPYAIKVET HNHPTAIAPW
     PGAATGAGGE IRDEGATGRG GKPKAGLTGF SVSHLRIPGL PRPWEKDRPL PPRMASAFEI
     MRDGPLGAAA FNNEFGRPAL GGYFRTFEQE TGEKGVRRGY DKPIMIAGGL AAIRPDHVQK
     RAVRPGDKVI VLGGPAMLIG LGGGAASSVS SGTSSAELDF ASVQRDNPEM ERRCQQVIDA
     CWARGEHNPI VSIHDVGAGG VSNAIPEILN DAGVGGIIDL SKLPCDDPTL SPMQVWSNES
     QERYVLAIGP DELPEFEAYC ARERCPYAVV GDATEEARLI VRDTRRDITV IDLGMDVLFG
     KPPRMHRDAV TVKPRVDLVA DLSGMGMDEA LLRVLRLPAV GSKSFLITIG DRTVGGLNAR
     DPMVGPWQVP VADVAVTMTD FDGYTGEAMA MAERAPIALL SSADAARMAV GEAITNLAAA
     SMKLDEVRLS ANWMAAVNHP GEDAALFDAV KAVGMELCPA LDISVPVGKD SLSMQTVWTD
     EAGKAQKTVS PVSLVITGFA RVDDVRRTLT PQLKLDRGDT ELWLIDLGAG RDRLGGSALT
     QVFNRGGGVP PDLDDPKRLR AMFELIQEAN RSGLLLAYHD RADGGAIVTL LEMAFAGHCG
     LEIRLDGWAE ATLRALFNEE LGAVVQVASA NREAFEALLV KYGLASMTHM VGRPKEKLGI
     KLHLNGETAF KWNWTELFRA WNETSHAMQR LRDNPHSADQ ESEWRLDDAD PGISPKLTFD
     PADDIAAPYI QSGKRPRVAI LREQGVNGQV EMAAAFDRAG FDAVDVHMTD LVSGRHHLKD
     FVGLAACGGF SYGDVLGAGR GWATSILYND ALREQFARFF EDGSKFALGV CNGCQMLSQL
     KDIIPDAKHW PQFLRNQSEQ YEARVATLEI LDTSSVFFRG MAGSRIPVAV AHGEGRVYFP
     NVCSPSKSHG AARFVDNRGR PTESYPLNPN GSPGGLAAFT AADGRVTIMM PHPERVFRSA
     QLSWHPENWG EDSPWMRMFR NARAWVG
//
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