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Database: UniProt/TrEMBL
Entry: F9V9A3_LACGT
LinkDB: F9V9A3_LACGT
Original site: F9V9A3_LACGT 
ID   F9V9A3_LACGT            Unreviewed;       738 AA.
AC   F9V9A3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   26-NOV-2014, entry version 25.
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   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   OrderedLocusNames=LCGT_1181 {ECO:0000313|EMBL:BAK58694.1};
GN   ORFNames=I578_00808 {ECO:0000313|EMBL:EOT93272.1}, OO3_00423
GN   {ECO:0000313|EMBL:EOT33233.1};
OS   Lactococcus garvieae (strain ATCC 49156 / DSM 6783 / NCIMB 13208 /
OS   YT-3) (Enterococcus seriolicida).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=420889 {ECO:0000313|EMBL:BAK58694.1, ECO:0000313|Proteomes:UP000008521};
RN   [1] {ECO:0000313|EMBL:BAK58694.1, ECO:0000313|Proteomes:UP000008521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49156 {ECO:0000313|EMBL:BAK58694.1}, and ATCC 49156 / DSM
RC   6783 / NCIMB 13208 / YT-3 {ECO:0000313|Proteomes:UP000008521};
RX   PubMed=21829716; DOI=10.1371/journal.pone.0023184;
RA   Morita H., Toh H., Oshima K., Yoshizaki M., Kawanishi M., Nakaya K.,
RA   Suzuki T., Miyauchi E., Ishii Y., Tanabe S., Murakami M., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the fish
RT   pathogen Lactococcus garvieae.";
RL   PLoS ONE 6:E23184-E23184(2011).
RN   [2] {ECO:0000313|EMBL:EOT33233.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 49156 {ECO:0000313|EMBL:EOT33233.1};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lactococcus garvieae ATCC_49156 (Illumina only
RT   assembly).";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EOT93272.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 49156 {ECO:0000313|EMBL:EOT93272.1};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lactococcus garvieae ATCC_49156
RT   (PacBio/Illumina hybrid assembly).";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
CC       complex involved in the purines biosynthetic pathway. Catalyzes
CC       the ATP-dependent conversion of formylglycinamide ribonucleotide
CC       (FGAR) and glutamine to yield formylglycinamidine ribonucleotide
CC       (FGAM) and glutamate. The FGAM synthase complex is composed of
CC       three subunits. PurQ produces an ammonia molecule by converting
CC       glutamine to glutamate. PurL transfers the ammonia molecule to
CC       FGAR to form FGAM in an ATP-dependent manner. PurS interacts with
CC       PurQ and PurL and is thought to assist in the transfer of the
CC       ammonia molecule from PurQ to PurL. {ECO:0000256|HAMAP-
CC       Rule:MF_00420}.
CC   -!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D-
CC       ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-
CC       (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.
CC       {ECO:0000256|HAMAP-Rule:MF_00420}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-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
CC       PurL, 1 PurQ and 2 PurS subunits. {ECO:0000256|HAMAP-
CC       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}.
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DR   EMBL; AP009332; BAK58694.1; -; Genomic_DNA.
DR   EMBL; AHYM01000002; EOT33233.1; -; Genomic_DNA.
DR   EMBL; ASWT01000006; EOT93272.1; -; Genomic_DNA.
DR   RefSeq; YP_004779358.1; NC_015930.1.
DR   EnsemblBacteria; BAK58694; BAK58694; LCGT_1181.
DR   EnsemblBacteria; EOT33233; EOT33233; OO3_00423.
DR   EnsemblBacteria; EOT93272; EOT93272; I578_00808.
DR   GeneID; 11137279; -.
DR   KEGG; lgr:LCGT_1181; -.
DR   KO; K01952; -.
DR   OMA; QAVVFKI; -.
DR   BioCyc; LGAR420889:GH14-1201-MONOMER; -.
DR   UniPathway; UPA00074; UER00128.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.1330.10; -; 2.
DR   HAMAP; MF_00420; PurL_2; 1.
DR   InterPro; IPR010918; AIR_synth_C_dom.
DR   InterPro; IPR000728; AIR_synth_N_dom.
DR   InterPro; IPR010074; PRibForGlyAmidine_synth_II.
DR   InterPro; IPR016188; PurM_N-like.
DR   Pfam; PF00586; AIRS; 2.
DR   Pfam; PF02769; AIRS_C; 2.
DR   SUPFAM; SSF55326; SSF55326; 2.
DR   SUPFAM; SSF56042; SSF56042; 2.
DR   TIGRFAMs; TIGR01736; FGAM_synth_II; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008521};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   REGION       99    102       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00420}.
FT   REGION      319    321       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00420}.
FT   ACT_SITE     54     54       {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   ACT_SITE    100    100       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL        98     98       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       122    122       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       275    275       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       540    540       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING      57     57       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING      96     96       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING     121    121       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     245    245       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     502    502       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING     539    539       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     542    542       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
SQ   SEQUENCE   738 AA;  79586 MW;  8E087BE12723C4F6 CRC64;
     MSGEMSPEQI QASKIYREWG LTDEEYSKIK NEILGGRLPN FTETGMYAVM WSEHCCYKNS
     KPVLKKFPTE GPQVLIGPGE GAGVVDIGEG WAVVFKAESH NHPSYVEPYE GAATGSGGII
     RDIFSMGARP VALLDSLRFG QIDNAKTRHI VERVTAGIAG YGNCIGIPTV GGEVAFDESY
     AGNPLVNVMC IGLIEHKHIQ KGQAKGVGNT IMYVGAKTGR DGIHGASFAS QEFGSGSETQ
     RSAVQVGDPF MEKLLLEACL EVIHNHSDIL VGIQDMGAAG LVSSTSEMAS KAGSGLKLNL
     DLVPQRETNM TPYEMMLSES QERMVLCIKK GHEDEIVELF KKYELDAVNI GEVTDDGMYT
     LFHQGEKVAE IPVDSLAEDA PVYSREMKEP ARIAEFVKAE KFIPEIANAT EVLKDLLSQP
     TIASKRSIYE TYDGRVMTNT VVAPGSDAAV IRLRHSNKAL AMTTDCNARY LYLNPEIGGQ
     IAVAEAARNI IASGGKPLAI TDCLNFGNPE KPEQFYELSK ACDGVSESCR VLSTPVISGN
     VSLYNETNGQ AILPTPMIGM VGLIEDVTHI TTQDFKDAGD LIYIIGETAD DFSGSEIQKM
     MTGKISGTLN FDLQAEKENQ KHVLKAIQAG LVKSAHDLSE GGLAVALVES AFANNKGISV
     HFEGKVSQLF SESQGRFILS VHPKDEKNFE ALMAGKASKL GQVTDKSEIK ISAKDGEISL
     STAEAKAIYE GAIPCLMK
//
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