ID A0A0K1XCU8_9GAMM Unreviewed; 1298 AA.
AC A0A0K1XCU8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=AKN88_03255 {ECO:0000313|EMBL:AKX59064.1};
OS Thiopseudomonas alkaliphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Thiopseudomonas.
OX NCBI_TaxID=1697053 {ECO:0000313|EMBL:AKX59064.1, ECO:0000313|Proteomes:UP000063953};
RN [1] {ECO:0000313|EMBL:AKX59064.1, ECO:0000313|Proteomes:UP000063953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E5571 {ECO:0000313|EMBL:AKX59064.1,
RC ECO:0000313|Proteomes:UP000063953};
RX PubMed=26679585;
RA Lauer A.C., Nicholson A.C., Humrighouse B.W., Emery B., Drobish A.,
RA Juieng P., Loparev V., McQuiston J.R.;
RT "Genome Sequences of Oblitimonas alkaliphila gen. nov. sp. nov. (Proposed),
RT a Novel Bacterium of the Pseudomonadaceae Family.";
RL Genome Announc. 3:e01474-15(2015).
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}.
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DR EMBL; CP012365; AKX59064.1; -; Genomic_DNA.
DR RefSeq; WP_053100072.1; NZ_CP012365.1.
DR STRING; 1697053.AKN87_05295; -.
DR PATRIC; fig|1698449.3.peg.652; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000063953; Chromosome.
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:UP000063953}.
FT DOMAIN 35..148
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 170..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 839..968
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 301..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1138
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1263
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1265
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
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; 140547 MW; A2258F7E7927C8E1 CRC64;
MLILRGAPAL SPFRHGKLLE QLTQKVPAVT GLYAEFAHFV EVSSALSSEE GQTLSRLLQY
GPTVAQQEPA GRLFLVVPRF GTISPWSSKA TDIAQNCGLA KIERIERGIA YYVAGELSDA
DAQQLAASLH DRMTELVLGA MEEASALFNH AQPKPMSSVP VLTEGREALV AANISLGLAL
AEDEIDYLVE SFTKLGRNPN DVELMMFAQA NSEHCRHKIF NASWDIDGET QEKSLFAMIK
NTYQMNSEGV LSAYKDNAAV MEGFTAGRFY PNPATKEYAA IEQPVHILMK VETHNHPTAI
APFPGASTGS GGEIRDEGAT GRGAKPKAGL TGFTVSNLNI PGFEQPWEKA YGKPERIVTP
LDIMLEGPLG GAAFNNEFGR PALTGYFRTF EQSINTPRGE EVRGYHKPIM LAGGMGNIRE
DHVQKDEISV GGKLIVLGGP AMLIGLGGGA ASSMATGSSS ADLDFASVQR DNPEMERRCQ
EVIDRCWQMG ENNPIKFIHD VGAGGLSNAF PELVNDAGRG GVFNLRNIPN DEPGMSPLEI
WCNESQERYV LSVDAKDLAL FTEICERERC PFAVVGEATE ERQLTVEDSH FNNKPVDMPL
EVLLGKAPRM HRSVTREAEI GDDFSAAAAP MQEAIERVLR HPAVASKKFL ITIGDRSVTG
LVARDQFVGP WQVPVADCAV TATSFDVYTG EAMAMGERTP LAVLDAPASG RMAVGEAVTN
LAAAAIAKVS DIRLSANWMA AAGHPGEDVR LYETVKAVGM ELCPELGITI PVGKDSMSMQ
TNWQEQGEDK AVISPLSLVI TGFAPVQDVR RTLTPELRLD KGASELLLID LGRGQNRMGA
SILAQVYSQV GQSVPDVDRA ADLKGFFDSI QELNQQGKLL AYHDRSDGGL AAAAIEMAFA
GHCGLQLTLD KLCSSADDAM AALFNEELGA VIQIAQADRA EVLAVFEQNG LADCVKPIGQ
PVTGGQVRIS LAGNDLFVGE RRILQRIWTE TSYQIQRLRD NEECAEQEFD ALLDEQDPGL
SAKVTFDINQ NIAAPYINKG VRPKVAVLRE QGVNGHVEMA AAFDKAGFAA VDVHMSDILA
GRIDLASFKG LAACGGFSYG DVLGAGGGWS KSILFNNKAR DNFAAFFERA DSFTLGVCNG
CQMLSNLQEL IPGAEFWPRF VRNRSEQFEA RVAMVEVQES PSIFLQGMAG SRLPVVVAHG
EGQVEYPSQE ALLESDLSGC VGLRYVDNYG KVTEAFPANP NGSARGITGL TSRDGRATIM
MPHPERVFRA VQNSWHPEEW QEDGAWLRMF RNARVWVD
//
