ID A6DQM6_9BACT Unreviewed; 997 AA.
AC A6DQM6;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 75.
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=LNTAR_04636 {ECO:0000313|EMBL:EDM26107.1};
OS Lentisphaera araneosa HTCC2155.
OC Bacteria; Lentisphaerota; Lentisphaeria; Lentisphaerales; Lentisphaeraceae;
OC Lentisphaera.
OX NCBI_TaxID=313628 {ECO:0000313|EMBL:EDM26107.1, ECO:0000313|Proteomes:UP000004947};
RN [1] {ECO:0000313|EMBL:EDM26107.1, ECO:0000313|Proteomes:UP000004947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2155 {ECO:0000313|EMBL:EDM26107.1,
RC ECO:0000313|Proteomes:UP000004947};
RX PubMed=20363947; DOI=10.1128/JB.00208-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Morris R.M., Giovannoni S.J.;
RT "Genome sequence of Lentisphaera araneosa HTCC2155T, the type species of
RT the order Lentisphaerales in the phylum Lentisphaerae.";
RL J. Bacteriol. 192:2938-2939(2010).
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:EDM26107.1}.
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DR EMBL; ABCK01000020; EDM26107.1; -; Genomic_DNA.
DR AlphaFoldDB; A6DQM6; -.
DR STRING; 313628.LNTAR_04636; -.
DR eggNOG; COG0046; Bacteria.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000004947; 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; 3.30.1280.10; Phosphoribosylformylglycinamidine synthase subunit PurS; 2.
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 InterPro; IPR003850; PurS.
DR InterPro; IPR036604; PurS-like_sf.
DR PANTHER; PTHR43555; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 1.
DR PANTHER; PTHR43555:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF02700; PurS; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00420};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00420};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00420};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_00420}; Reference proteome {ECO:0000313|Proteomes:UP000004947}.
FT DOMAIN 202..259
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 305..429
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 445..597
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 829..970
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 255
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT ACT_SITE 325
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 323
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 482
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 510
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 743
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 787
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
FT BINDING 790
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00420"
SQ SEQUENCE 997 AA; 109206 MW; 48177753E587DE06 CRC64;
MLKPIIKGNK MIYRLEISPR KGMDDPAGHT VQRKAKSILS YELNKVDTAE VLTIDANVER
KSAEEILKEI VNPVLQQGLI GAVEQRSFDW FIAVGFLAGV TDNVSRTARE AIRDIIGRQL
TDEEKVYSSR EYFISSKNLK KEDVEHIAKD LLANELIQSL TIMSFDEWKH NGSPANTPEF
VAIQEPKVDF INIDVSDEEL MGISNSKTLA LQLDEMQAIR DYAINNNDAQ REELGLIGKL
TDAELECLAQ SWSEHCSHKI FAADIEYTDA DGNVETINSL YKSYIKKSTF EIGDQVDWLV
SVFHDNAGVI TFNEKYDLAF KLETHNSPSA LDPYGGAMTG IVGVNRDIMG TGTGAEMLVN
VWGYCLGSPF VDESEVPEGL LHPRRIRDGV HQGVIEGGNQ SGIPYGLGWE YFDARYIGKP
LVYCGTVGIL PHKQHGKSAS LKTIEPGDVI VMVGGRIGKD GIHGATFSSE ELHKDSPVAA
VQIGDPITQK KAADFLYEAR DADLYRFVTD NGAGGLSSSI GEMATECNGC FVDLAKAPLK
YAGLQPWEIF VSEAQERMSF AVPVEKVEAF LTLAQERDVE ATVLGEFNDS GKCHLIYNDL
TVAFLDLDFM HGGNPKLQLK AKWEAPVFEE IPEELDSEIS DDIHELLASL NLCSSEYKAR
QYDHEVKALS VVKPYVGVEA DVDSDASVFM AEPMTKEGFV LANGVAPSYS DIDTYHMTAS
IIDMCLRRTV AVGGSIDKVA GLDNFCWPDP VESAKTPDGQ YKLAQLVRSN QALYDYCKAF
TLPCISGKDS MKNDSTRGGK KISIPPTLLF STIAPMMDVS KSVTLSSKRA GDYVYVIGET
LAELGGSQYA AQKGYVGNKV PQVDAEKAKK IYKQVHQATD AEVVHSLHAP AFGGLAAAFA
RKSIAGRLGM EIDINLIPAD DLSETELLFS ESNSRLVATV APDKAEEFEA LLEGVAFAKV
GTVTLDDELV IRQGKHIVAA LNLENLVKSY KKTLDGV
//
