ID J0RLD1_9FLAO Unreviewed; 1217 AA.
AC J0RLD1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
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=FF52_20280 {ECO:0000313|EMBL:EJF99841.1};
OS Flavobacterium sp. F52.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1202532 {ECO:0000313|EMBL:EJF99841.1, ECO:0000313|Proteomes:UP000002690};
RN [1] {ECO:0000313|EMBL:EJF99841.1, ECO:0000313|Proteomes:UP000002690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F52 {ECO:0000313|EMBL:EJF99841.1,
RC ECO:0000313|Proteomes:UP000002690};
RX PubMed=22965088; DOI=10.1128/JB.01249-12;
RA Kolton M., Green S.J., Harel Y.M., Sela N., Elad Y., Cytryn E.;
RT "Draft Genome Sequence of Flavobacterium sp. Strain F52, Isolated from the
RT Rhizosphere of Bell Pepper (Capsicum annuum L. cv. Maccabi).";
RL J. Bacteriol. 194:5462-5463(2012).
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:EJF99841.1}.
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DR EMBL; AKZQ01000037; EJF99841.1; -; Genomic_DNA.
DR RefSeq; WP_008468559.1; NZ_AKZQ01000037.1.
DR AlphaFoldDB; J0RLD1; -.
DR PATRIC; fig|1202532.3.peg.4163; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR OrthoDB; 9804441at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000002690; 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; 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 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 11..80
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 122..171
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 380..535
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 764..904
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1066
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1179
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1181
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 260..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 664
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 668
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
FT BINDING 826
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1217 AA; 134391 MW; 404EAE21CEE94A2C CRC64;
MIHFFENQSK TVFAVQTQNE ISAQDISKLN WLFADANKIE KSALTGFFVG PRATMITPWS
TNAVEITQNM GISGIIRIEE FHPATEDFTD FDPMLSQKFN ELDQEIFTIN IQPEPILEID
DIAAYNKVEG LALSEEEVDY LNNLSTKLGR KLTDSEIFAF SQANSEHCRH KIFNGTFVIN
GEEKETSLFK LIKKTSQENP NDIVSAYKDN VAFVKGPKVQ QFAPKSADKP DFYEIKEFDS
VISLKAETHN FPTTVEPFNG AATGSGGEIR DRLAGGQGSL PLAGTAVYMT SYSRLKEDRK
WENAVEERKW LYQTPMDILI KASNGASDFG NKFGQPLITG SVLTFEHEEE NRKIGYDKVI
MQAGGIGYGK LDQSIKNKPK EGDKIVILGG ENYRIGMGGA AVSSADTGAF GSGIELNAIQ
RSNPEMQKRA ANAIRGLVES DNNPIVSIHD HGAGGHLNCL SELVEETGGL IDLDKLPVGD
PTLSAKEIIG NESQERMGLV IGQKDIDTLQ RIADRERSPM YQVGDVTGDH RFTFQSKTNG
SKPMDYALED FFGSSPKTVM TDTTVDRKYA DVAYNAADFE TYLKDVLRLE AVASKDWLTN
KVDRCVGGKV AKQQNAGPLQ LPLNNVGVMA LDYLGKEGIA TSIGHAPIAA LIDPVAGSRN
AIAESLSNII WAPIKDQLKG VSLSANWMWA CKNEGEDARL YEAVQGCSDF AIELGINIPT
GKDSLSMKQK YPNDEVIAPG TVIISAAGNC TNIRKVVEPV LQKNGDSIYY INLSQDDFKL
GGSSFAQIRN AIGNETCTIK DASFFKNAFN TVQELIGESQ ILAGHDIGSG GLITTLLELC
FADVNLGAKI DFSAFAEKDL LKILFAENIG IVFQAKSDAT VEAKLKANNI EFFKIGSVTS
TATLEVGNWK LDIPTYRDVW FETSYLLDQK QSKNGRAQAR FENYKNQVLN YTFPTHFTGK
KPEIDNSKPR PKAAIIREKG SNSEREMANA MYLAGFDVKD VHMTDLISGR ETLEDIQFIG
AVGGFSNSDV LGSAKGWAGA FLYNEKAKTA LDNFFKREDT LSVGICNGCQ LFMELEVINP
EHEVHGKMLH NESQKHESIF TSVTVQENNS VMLSTLAGST LGVWVSHGEG KFKLPLAEEN
YNIVSKYAYE GYPANPNGSD YNTAMMCDKT GRHLVMMPHI ERSTFQWNWA HYPKDRNDEV
TPWHEAFVNA RKWIEKN
//
