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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)

 A0A1Q5ZWV7_9SPHI        Unreviewed;       741 AA.
A0A1Q5ZWV7;
12-APR-2017, integrated into UniProtKB/TrEMBL.
12-APR-2017, sequence version 1.
25-OCT-2017, entry version 5.
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};
ORFNames=RG47T_1687 {ECO:0000313|EMBL:OKS86236.1};
Mucilaginibacter polytrichastri.
Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
Sphingobacteriaceae; Mucilaginibacter.
NCBI_TaxID=1302689 {ECO:0000313|EMBL:OKS86236.1, ECO:0000313|Proteomes:UP000186720};
[1] {ECO:0000313|EMBL:OKS86236.1, ECO:0000313|Proteomes:UP000186720}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=RG4-7 {ECO:0000313|EMBL:OKS86236.1,
ECO:0000313|Proteomes:UP000186720};
Li Y.;
"Whole Genome Sequencing of Mucilaginibacter polytrichastri RG4-7(T)
isolated from the moss sample.";
Submitted (NOV-2016) 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}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:OKS86236.1}.
-----------------------------------------------------------------------
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EMBL; MPPL01000001; OKS86236.1; -; Genomic_DNA.
UniPathway; UPA00074; UER00128.
Proteomes; UP000186720; Unassembled WGS sequence.
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; IPR010074; PRibForGlyAmidine_synth_PurL.
InterPro; IPR010918; PurM-like_C_dom.
InterPro; IPR036676; PurM-like_C_sf.
InterPro; IPR016188; PurM-like_N.
InterPro; IPR036921; PurM-like_N_sf.
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:UP000186720};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420};
Ligase {ECO:0000256|HAMAP-Rule:MF_00420};
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:UP000186720}.
DOMAIN 88 189 AIRS. {ECO:0000259|Pfam:PF00586}.
DOMAIN 202 353 AIRS_C. {ECO:0000259|Pfam:PF02769}.
DOMAIN 444 561 AIRS. {ECO:0000259|Pfam:PF00586}.
DOMAIN 575 714 AIRS_C. {ECO:0000259|Pfam:PF02769}.
REGION 94 97 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00420}.
REGION 312 314 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00420}.
ACT_SITE 48 48 {ECO:0000256|HAMAP-Rule:MF_00420}.
ACT_SITE 95 95 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 93 93 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 117 117 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 268 268 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 537 537 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 51 51 ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
BINDING 91 91 ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
BINDING 116 116 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 240 240 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 499 499 ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
BINDING 536 536 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 539 539 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00420}.
SEQUENCE 741 AA; 80606 MW; E274DC417D22F024 CRC64;
MEQQELTTVE TAKELGLLPQ EYDRIKEILG RVPNFTELSI FSVMWSEHCS YKNSIKWLKT
LPRDGARMLA KAGEENAGLV DLGDGIGCAF KIESHNHPSA LEPYQGAATG VGGINRDIFT
MGARPIAQLN SLRFGDLSLD RTKWLVKGVV KGISHYGNAF GIPTVGGELY FDESFNVNPL
VNAMSAGIVK AGETVSATSY GVGNPVYIVG SATGKDGIHG AAFASKDITE DSVNDLPAVQ
VGDPFQEKLL LEATLEVIKT GAVIGMQDMG AAGIICSNSE MSAKGEHGMK IWLDKVPTRQ
ENMKPFEILL SESQERMLIV VEKGKEALVQ AVFDKWDLNC AIIGEVTDTQ RLEYYMNGEL
VADVPADDLV LGGGAPVYDR EYREPAYYQE YQKFKIDDVA EPEDLKAVAE HLIGHPNIAS
KRWVTNQYDS MVGTATMTTN RMSDAAVVAV KGTTKAIALT TDCNSRYVNA DPQKGTSIAV
AEAARNIVCA GGEPVAITNC LNFGNPYIPE VFWQFVSAIK GMGEACTKFG TPVTGGNVSF
YNQSSDDGPV FPTPTIGMLG VLDNIDNMMT ADFKQPDDLI YLIGESVNDI ASSQYLSSFH
KVKKSPAPYF DIDKEYEMHQ IVKELILHKV IQSAHDVADG GLYINLLESS LPNGLGFNIE
SDSDIRKDAF LFGEAQGRVV VSVAPADEER FVEMMATSET PFSLLGTVAH HGNLFVDDEL
YGNITDIRMV YDNVLHAILG E


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