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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)

 Q6UCP0_9PROT            Unreviewed;       732 AA.
Q6UCP0;
05-JUL-2004, integrated into UniProtKB/TrEMBL.
05-JUL-2004, sequence version 1.
27-SEP-2017, entry version 74.
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=HOT2C01.41 {ECO:0000313|EMBL:AAR05350.1};
uncultured marine alpha proteobacterium HOT2C01.
Bacteria; Proteobacteria; Alphaproteobacteria; environmental samples.
NCBI_TaxID=248049 {ECO:0000313|EMBL:AAR05350.1};
[1] {ECO:0000313|EMBL:AAR05350.1}
NUCLEOTIDE SEQUENCE.
PubMed=14566056; DOI=10.1073/pnas.2133554100;
De La Torre J.R., Christianson L.M., Beja O., Suzuki M.T., Karl D.M.,
Heidelberg J., DeLong E.F.;
"Proteorhodopsin genes are distributed among divergent marine
bacterial taxa.";
Proc. Natl. Acad. Sci. U.S.A. 100:12830-12835(2003).
[2] {ECO:0000313|EMBL:AAR05350.1}
NUCLEOTIDE SEQUENCE.
Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
Submitted (JAN-2017) 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; AY372455; AAR05350.1; -; Genomic_DNA.
ProteinModelPortal; Q6UCP0; -.
UniPathway; UPA00074; UER00128.
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};
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 88 190 AIRS. {ECO:0000259|Pfam:PF00586}.
DOMAIN 204 356 AIRS_C. {ECO:0000259|Pfam:PF02769}.
DOMAIN 441 558 AIRS. {ECO:0000259|Pfam:PF00586}.
DOMAIN 572 704 AIRS_C. {ECO:0000259|Pfam:PF02769}.
REGION 96 99 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00420}.
REGION 314 316 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00420}.
ACT_SITE 51 51 {ECO:0000256|HAMAP-Rule:MF_00420}.
ACT_SITE 97 97 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 95 95 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 119 119 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 270 270 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_00420}.
METAL 534 534 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 54 54 ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
BINDING 93 93 ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
BINDING 118 118 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 242 242 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 496 496 ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
BINDING 533 533 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00420}.
BINDING 536 536 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00420}.
SEQUENCE 732 AA; 80467 MW; 4A1EE19D8532D0C7 CRC64;
MSEINWQFQT EQSLVENHGL KLDEFAKIVE GLGREPNLTE LGIFSAMWNE HCSYKSSKFW
LKKLPTTGER VVQGPGENAG VIDIDDGDVA VFKMESHNHP SFLEPYQGAA TGVGGILRDV
FTMGARPVAN LNALRFGEPE HPKTKHLLSG VVSGIGGYGN CIGVPTVGGE VNFHPSYNGN
ILVNAMTVGI AKKDKIFYSA AAGVGNPVVY VGSKTGRDGI HGATMASAEF DEDSEDKKPT
VQVGDPFTEK LLLEACLELM KEEAIIAIQD MGAAGLTSSS IEMASKGDVG LEINLSKVPM
RAQNMSAYEL MLSESQERML MVLDPSKEDM ARNIFKKWDL EFEVIGKVTD TKKLILMMNG
KEEASIPINI LVEDAPEYQR DYVIEKPSLI KKYNPEDFNQ DDLMSDLSTM LKHPDLSSRK
WIWEQYDHMV MADTVVRPGS DAAVVRVHGT NKGLAMSTDC SPVYCKHNPY EGGKHAVVET
WRNLIASGAL PIAITDCMNF GNPEKPEIMG QFVECIRGMG DACSKLNYPV VSGNVSLYNE
TNGIGIYPTP AIGGVGLIKD LSNVKTLSLK NEGNFLCVVG KSKNHLGNSK YMTIIQKKED
GGTPEINLDE ELKNGHFVLE LINEQLIESS HDVGEGGILI AIAEMCIAGN LGLIIDTNPE
FPHGFYFGED QSRYLIEIKA ENFDQLKQIA KSKNVDFEKI GVINREIIRI NNSNEIKISE
LKKNFEQGVE NI


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