ID A0A1F6XLG7_9BACT Unreviewed; 964 AA.
AC A0A1F6XLG7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000256|HAMAP-Rule:MF_00420};
DE Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00420};
DE EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00420};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000256|HAMAP-Rule:MF_00420};
DE Short=FGAR amidotransferase II {ECO:0000256|HAMAP-Rule:MF_00420};
DE Short=FGAR-AT II {ECO:0000256|HAMAP-Rule:MF_00420};
DE AltName: Full=Glutamine amidotransferase PurL {ECO:0000256|HAMAP-Rule:MF_00420};
DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000256|HAMAP-Rule:MF_00420};
GN Name=purL {ECO:0000256|HAMAP-Rule:MF_00420};
GN ORFNames=A2917_01215 {ECO:0000313|EMBL:OGI94985.1};
OS Candidatus Nomurabacteria bacterium RIFCSPLOWO2_01_FULL_42_17.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1801780 {ECO:0000313|EMBL:OGI94985.1, ECO:0000313|Proteomes:UP000178104};
RN [1] {ECO:0000313|EMBL:OGI94985.1, ECO:0000313|Proteomes:UP000178104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
CC complex involved in the purines biosynthetic pathway. Catalyzes the
CC ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and
CC glutamine to yield formylglycinamidine ribonucleotide (FGAM) and
CC glutamate. The FGAM synthase complex is composed of three subunits.
CC PurQ produces an ammonia molecule by converting glutamine to glutamate.
CC PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-
CC dependent manner. PurS interacts with PurQ and PurL and is thought to
CC assist in the transfer of the ammonia molecule from PurQ to PurL.
CC {ECO:0000256|HAMAP-Rule:MF_00420}.
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_00420};
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. {ECO:0000256|HAMAP-
CC Rule:MF_00420}.
CC -!- SUBUNIT: Monomer. Part of the FGAM synthase complex composed of 1 PurL,
CC 1 PurQ and 2 PurS subunits. {ECO:0000256|HAMAP-Rule:MF_00420}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420}.
CC -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000256|HAMAP-
CC Rule:MF_00420}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00420}.
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:OGI94985.1}.
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DR EMBL; MFVE01000008; OGI94985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6XLG7; -.
DR STRING; 1801780.A2917_01215; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000178104; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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 CDD; cd02203; PurL_repeat1; 1.
DR CDD; cd02204; PurL_repeat2; 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_00420; PurL_2; 1.
DR InterPro; IPR010074; PRibForGlyAmidine_synth_PurL.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR PANTHER; PTHR43555; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 1.
DR PANTHER; PTHR43555:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 1.
DR Pfam; PF00586; AIRS; 2.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00420};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_00420};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00420};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00420}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_00420}.
FT DOMAIN 181..222
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 267..397
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 418..571
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 667..766
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 821..938
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 593..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 455
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 484
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 527..529
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 725
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 762
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 765
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
SQ SEQUENCE 964 AA; 105714 MW; B73987C45B58F798 CRC64;
MILRIYVMGK AGNTKADSYL IDSKLSKKEL TKLAEALSNP ILENYYINES PKISGFSHAI
EIGFLPGVTD NIGHTVKEMA TDMFHFGKNA DFHVYTSKIF FLKENKKEEV EKIALTLYNP
LIERAYISPI KSKKINLPNK IQKVILKKNV PVTEVTLSVS EEELIKISRE GIKDEKGLRR
GPLALDLSSM LAIKDYFSKL KRNPTDIELE SLAQTWSEHC KHTIFANPID NIKDGLYKTY
IKGATNLIRK QKQERGEEDF CISVFSDNAG GIIFDDDYLI THKVETHNSP SALDPFGGAV
TGIVGVNRDT IGFGLGAKPV ANTYGFCFGQ PEDTRALFRD KEMKQKMLPP KRIMDGVIKG
INVGGNCSGI PTLSGFVKYD DRYRGKPLVF AGTVGLISRN LPASGGIRKK LSHEKSAKIG
DYIVMVGGRV GLDGIHGATF SSVTLDSNSP ATAVQIGDPI TQKKLSDAIV KEARDLNLYN
SITDDGAGGL SCSVAEMAKE CGGAKVYLEK VPLKYPGLAP WEIWISESQE RMTLAVPKTK
WKTFKKLMER RGVEATVIGE FTNSGKIVVM YKDKKIMDLD MEFLHNGLPK HHLKTEATSP
QPSPERRGSS FPFQGKAGDE VYTKVLENFL ADKNISGFSF ISEQYDHEVQ ASSVLKPLSG
PGRINTDAQV FRPVLNSNKG VVVSSATYPS YGDISAYHMA ACALDTAIRN IISVGGTLSH
LAILDNFCWC SSNDKTRLYQ LVEAVKACYD YAVGYGTPFI SGKDSMFNDF KGYDDKGNPI
AISIPPTLLI SAISVMPDLN KTVSPEFKNS GDVIYLLGET NDELGVPKVN LEKNLKTYLA
LEKVIQKELV ASSLSVTSGG LGIALAKACV GGMLGCKVSL SQICRSLASA DLKMFSESQG
RILISVSPKN VKEFEKICAG IFCVKLGTVS KNNKIIITDG KNKVVETTVK KLHDIYHKFS
NSQK
//
