ID A0A430JNX8_9ACTO Unreviewed; 831 AA.
AC A0A430JNX8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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 ECO:0000313|EMBL:RTE48550.1};
GN ORFNames=EKN07_09290 {ECO:0000313|EMBL:RTE48550.1};
OS Actinobaculum sp. 352.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=2490946 {ECO:0000313|EMBL:RTE48550.1, ECO:0000313|Proteomes:UP000273303};
RN [1] {ECO:0000313|EMBL:RTE48550.1, ECO:0000313|Proteomes:UP000273303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=352 {ECO:0000313|EMBL:RTE48550.1,
RC ECO:0000313|Proteomes:UP000273303};
RA Zhu W.;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RTE48550.1}.
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DR EMBL; RQSN01000008; RTE48550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430JNX8; -.
DR OrthoDB; 9804441at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000273303; 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; 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 NCBIfam; TIGR01736; FGAM_synth_II; 1.
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 PIRSF; PIRSF001587; FGAM_synthase_II; 2.
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, ECO:0000313|EMBL:RTE48550.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000273303}.
FT DOMAIN 41..80
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 107..222
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 235..389
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 477..575
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 647..792
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 76
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 127..130
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 346..348
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 571
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 572
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 574
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
SQ SEQUENCE 831 AA; 86717 MW; 18A76B301BA6E627 CRC64;
MAFSQIESAR SPESSGQPTV TQNYDTVDNA AATPDQQMPW RELGLKEDEY QRIRSILGRR
PTIAELSMYS VMWSEHCSYK SSKKHLGEQF GRKTTAAMRE HLLVGMGQNA GVVDIGGGWA
VTFKVESHNH PSFVEPYQGA ATGVGGIVRD IIAMGARPVA VMDQLRFGAV DHPDTARMVH
GVVAGVGGYG NCLGLPNIGG ETEFDPSYQG NPLVNALCVG VMRHGDIHLA NAEGVGNKVV
LFGARTGGDG IGGASILASE TFDGGMPSKR PSVQVGDPFM EKVLIECCLE LFSAGVVEAI
QDLGAAGISC ATSELAANGH SGMHIDLEKV LLRDPSLSAG EILMSESQER MMAIVSPEKI
ADFLAVTRKW EVETAIIGEV TSDARLRIDH NGHRIVDVDP STVAVDGPVY DRAYARPTWQ
DTLQANSARN LPTPTNTAEL REQILQVLTD PNQASKAWVT DQYDRFVRGN TALAQPDDAG
VVRVDEQTGL GIAISTDANG WYTLLDPYAG AQQAVAEAYR NVCTVGAKPL AVTDCLNFGN
PEDPAAMWQL VTAMEGMADA CQALGIPVTG GNVSLYNSSG GVGTAEDADT SGPSDPAGET
HAPSSTGPEG EVGAAARPTT SINPTPVVGV LGVMADTTTA VPSGFQEEGL AIILLGATAA
ELDGSAWARI VHGHVGGRPP RVDLAAEQAL GRVLLALHDA DTQGMGRITH AAHDLSTGGL
IQALADMTTR CGIGASIDLA SVCSQVGIDS FTALFSESQG RALVAVPEGF LPAVRAAAQA
EGVPMVRIGT TGGEILAITP AEGQGTATEA LVFDVAALRA SSEAVLPALF T
//
