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Phosphoribosylformylglycinamidine synthase subunit PurL (FGAM synthase) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase subunit II) (FGAR amidotransferase II) (FGAR-AT II) (Glutamine amidotransferase PurL) (Phosphoribosylformylglycinamidine synthase subunit II)

 F0S4A0_DESTD            Unreviewed;       740 AA.
F0S4A0;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
03-MAY-2011, sequence version 1.
27-SEP-2017, entry version 44.
RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000256|HAMAP-Rule:MF_00420};
Short=FGAM synthase {ECO:0000256|HAMAP-Rule:MF_00420};
EC=6.3.5.3 {ECO:0000256|HAMAP-Rule:MF_00420};
AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000256|HAMAP-Rule:MF_00420};
Short=FGAR amidotransferase II {ECO:0000256|HAMAP-Rule:MF_00420};
Short=FGAR-AT II {ECO:0000256|HAMAP-Rule:MF_00420};
AltName: Full=Glutamine amidotransferase PurL {ECO:0000256|HAMAP-Rule:MF_00420};
AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000256|HAMAP-Rule:MF_00420};
Name=purL {ECO:0000256|HAMAP-Rule:MF_00420};
OrderedLocusNames=Dester_1034 {ECO:0000313|EMBL:ADY73672.1};
Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA).
Bacteria; Aquificae; Desulfurobacteriales; Desulfurobacteriaceae;
Desulfurobacterium.
NCBI_TaxID=868864 {ECO:0000313|EMBL:ADY73672.1, ECO:0000313|Proteomes:UP000007102};
[1] {ECO:0000313|Proteomes:UP000007102}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 11699 / BSA {ECO:0000313|Proteomes:UP000007102};
US DOE Joint Genome Institute (JGI-PGF);
Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Mikhailova N.,
Daligault H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
Brambilla E., Klenk H.-P., Eisen J.A.;
"The complete genome of Desulfurobacterium thermolithotrophum DSM
11699.";
Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
complex involved in the purines biosynthetic pathway. Catalyzes
the ATP-dependent conversion of formylglycinamide ribonucleotide
(FGAR) and glutamine to yield formylglycinamidine ribonucleotide
(FGAM) and glutamate. The FGAM synthase complex is composed of
three subunits. PurQ produces an ammonia molecule by converting
glutamine to glutamate. PurL transfers the ammonia molecule to
FGAR to form FGAM in an ATP-dependent manner. PurS interacts with
PurQ and PurL and is thought to assist in the transfer of the
ammonia molecule from PurQ to PurL. {ECO:0000256|HAMAP-
Rule:MF_00420}.
-!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D-
ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-
(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.
{ECO:0000256|HAMAP-Rule:MF_00420}.
-!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000256|HAMAP-
Rule:MF_00420}.
-!- SUBUNIT: Monomer. Part of the FGAM synthase complex composed of 1
PurL, 1 PurQ and 2 PurS subunits. {ECO:0000256|HAMAP-
Rule:MF_00420}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420}.
-!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000256|HAMAP-
Rule:MF_00420}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00420}.
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EMBL; CP002543; ADY73672.1; -; Genomic_DNA.
RefSeq; WP_013638624.1; NC_015185.1.
STRING; 868864.Dester_1034; -.
EnsemblBacteria; ADY73672; ADY73672; Dester_1034.
KEGG; dte:Dester_1034; -.
eggNOG; ENOG4107QIK; Bacteria.
eggNOG; COG0046; LUCA.
KO; K01952; -.
OMA; FIEPYQG; -.
OrthoDB; POG091H009J; -.
UniPathway; UPA00074; UER00128.
Proteomes; UP000007102; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule.
GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
Gene3D; 3.30.1330.10; -; 2.
Gene3D; 3.90.650.10; -; 2.
HAMAP; MF_00420; PurL_2; 1.
InterPro; IPR010918; AIR_synth_C_dom.
InterPro; IPR010074; PRibForGlyAmidine_synth_PurL.
InterPro; IPR016188; PurM-like_N.
PANTHER; PTHR43555; PTHR43555; 1.
Pfam; PF00586; AIRS; 2.
Pfam; PF02769; AIRS_C; 2.
PIRSF; PIRSF001587; FGAM_synthase_II; 1.
SUPFAM; SSF55326; SSF55326; 2.
SUPFAM; SSF56042; SSF56042; 2.
TIGRFAMs; TIGR01736; FGAM_synth_II; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00420};
Complete proteome {ECO:0000313|Proteomes:UP000007102};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420};
Ligase {ECO:0000256|HAMAP-Rule:MF_00420, ECO:0000313|EMBL:ADY73672.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00420};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00420};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00420};
Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00420};
Reference proteome {ECO:0000313|Proteomes:UP000007102}.
DOMAIN 81 183 AIRS. {ECO:0000259|Pfam:PF00586}.
DOMAIN 196 349 AIRS_C. {ECO:0000259|Pfam:PF02769}.
DOMAIN 436 556 AIRS. {ECO:0000259|Pfam:PF00586}.
DOMAIN 571 712 AIRS_C. {ECO:0000259|Pfam:PF02769}.
REGION 88 91 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00420}.
REGION 307 309 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00420}.
ACT_SITE 41 41 {ECO:0000256|HAMAP-Rule:MF_00420}.
ACT_SITE 89 89 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 87 87 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 111 111 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 263 263 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 529 529 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 44 44 ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
BINDING 85 85 ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
BINDING 110 110 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 235 235 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 491 491 ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
BINDING 528 528 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 531 531 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00420}.
SEQUENCE 740 AA; 82110 MW; 210B69DA39C4ED1B CRC64;
MDREIIEQHV TWEEYQKILK ILGREPNLVE LGIFSAMWSE HCSYKSSRPH LKKFPTKAPW
VVQGPGENAG IIMVDEEKEI CAAFKVESHN HPSFIEPFHG AATGVGGILR DVFTMGARPI
ACMDSLRFGE LNDPKMKYVT KGVVSGISHY GNCVGVPTVG GEVYFDSCYQ TNPLVNAFAL
GIVKKDKIFY ARAAGVGNPV IYVGSKTGRD GIHGATMASE EFSSEEEVEK KVNVQVGDPF
MEKLLIEACL EAMKKEGIVA IQDMGAAGLT SSSVEMAARG GVGVRLELDK VPTREEGMTP
YEIMLSESQE RMLVVCEKGK EEEIMEVFRK WNLDACIIGE VIEEPVIRLF WHGEKVAELP
IKALTDEAPV YYRPFKVPKY IKENRSYDQN KIPEPKDYNQ IVKELLNSPT IASKRWIYRQ
YDHMVQVNTV VYPGSDAAVL RVKESKKGIA ISSDCNSRYC YLNPYEGGKI AVAEAARNVA
CSGAIPRAIT DCLNFGSPED PEIMWQFVKA TDGMADACKV LETPVVSGNV SFYNETTTEN
GKRAVFPTPT VVCVGVLEDV EKRMTSFFKD EGDVIVLLGE NIGNVSGSEY QKLIEGEFKG
QGQTIDLAFE KALQKAVIEA IEKGLIKSAH DVSEGGIAIN LFESAFEKEL GFEVELEDDL
RTDFLLFGED QSRIVVTTSE DKLKELLPFF EKKVVPAKKI GIVTSSGRGI IRHKGKEVVN
LSVKECKEIY ENSLERKLLS


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