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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)

 H0B6K6_9ACTN            Unreviewed;       749 AA.
H0B6K6;
22-FEB-2012, integrated into UniProtKB/TrEMBL.
22-FEB-2012, sequence version 1.
28-FEB-2018, entry version 36.
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=SPW_0892 {ECO:0000313|EMBL:EHM30698.1};
Streptomyces sp. W007.
Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
Streptomyces.
NCBI_TaxID=1055352 {ECO:0000313|EMBL:EHM30698.1, ECO:0000313|Proteomes:UP000004626};
[1] {ECO:0000313|EMBL:EHM30698.1, ECO:0000313|Proteomes:UP000004626}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=W007 {ECO:0000313|EMBL:EHM30698.1,
ECO:0000313|Proteomes:UP000004626};
PubMed=22374958; DOI=10.1128/JB.06701-11;
Qin S., Zhang H., Li F., Zhu B., Zheng H.;
"Draft Genome Sequence of Marine Streptomyces sp. Strain W007, Which
Produces Angucyclinone Antibiotics with a Benz[a]anthracene
Skeleton.";
J. Bacteriol. 194:1628-1629(2012).
-!- 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:EHM30698.1}.
-----------------------------------------------------------------------
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EMBL; AGSW01000046; EHM30698.1; -; Genomic_DNA.
RefSeq; WP_007447457.1; NZ_AGSW01000046.1.
EnsemblBacteria; EHM30698; EHM30698; SPW_0892.
PATRIC; fig|1055352.3.peg.904; -.
UniPathway; UPA00074; UER00128.
Proteomes; UP000004626; 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; -; 4.
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:UP000004626};
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}.
DOMAIN 96 198 AIRS. {ECO:0000259|Pfam:PF00586}.
DOMAIN 211 366 AIRS_C. {ECO:0000259|Pfam:PF02769}.
DOMAIN 454 572 AIRS. {ECO:0000259|Pfam:PF00586}.
DOMAIN 585 722 AIRS_C. {ECO:0000259|Pfam:PF02769}.
REGION 103 106 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00420}.
REGION 322 324 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00420}.
ACT_SITE 55 55 {ECO:0000256|HAMAP-Rule:MF_00420}.
ACT_SITE 104 104 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 102 102 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 126 126 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 278 278 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 548 548 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 58 58 ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
BINDING 100 100 ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
BINDING 125 125 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 250 250 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 510 510 ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
BINDING 547 547 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 550 550 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00420}.
SEQUENCE 749 AA; 79543 MW; 3E7873B1B6A558D9 CRC64;
MSLDTVKHAA ETPDAEQPWK ELGLKEDEYA RIREILGRRP TGAELAMYSV MWSEHCSYKS
SKVHLKQFGE KVPANDAMLV GIGENAGVVD VGQGYAVTFK VESHNHPSYI EPYQGAATGI
GGIVRDILAM GARPIAVVDP LRFGAADHPD TKRVLPGVVA GIGGYGNCLG LPNIGGEVVF
DACYQGNPLV NAGCIGVMKH EDIHLAQASG PGNKVILYGA RTGGDGIGGV SVLASETFES
TGPAKRPAVQ VGDPFQEKLL IECTLEIFKE KLVAGIQDLG GAGLSCATSE LASAGSGGMR
VELDTVPLRD SSLSPEEILM SESQERMCAI VEPQHVDRFL EICEKWDVIA TVIGEVTDGS
QLEIFWHGEQ IVDVPPRSVA HDGPVYHRPF ARPSWQDALQ ADDAGKLARP GDAAELREQV
LKLVASPNQA SKAWITDQYD RFVQGNTVLA MPEDAGMVRI DAESNLGVAM ATDGNGRYAK
LDPYTGAQLA LAESYRNVAA SGAKPLAISD CLNFGSPEDP DVMWQFAEAT RGLADGCLEL
GTPVTGGNVS LYNQTGETAI HPTPVVAVLG VIDDVNRRTP VAFAEEGQLL YLLGDTTEEF
GGSAWSEVVH NHLGGLPPKV DLGREKLLAE ILISASRDGM IDAAHDLSDG GLIQAVTESC
LRGGKGARLV VPDGLDAFTF LFSESAGRAV VSIPRSEELR FNDMCGARGL PVARIGVVDG
EEIEIQGEFS IPLSELRTAH EATIPALLA


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