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Database: UniProt/TrEMBL
Entry: D8GYQ1_BACAI
LinkDB: D8GYQ1_BACAI
Original site: D8GYQ1_BACAI 
ID   D8GYQ1_BACAI            Unreviewed;       739 AA.
AC   D8GYQ1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   01-APR-2015, entry version 29.
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   ECO:0000313|EMBL:ADK03079.1};
GN   OrderedLocusNames=BACI_c03380 {ECO:0000313|EMBL:ADK03079.1};
OS   Bacillus cereus var. anthracis (strain CI).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=637380 {ECO:0000313|EMBL:ADK03079.1, ECO:0000313|Proteomes:UP000001657};
RN   [1] {ECO:0000313|EMBL:ADK03079.1, ECO:0000313|Proteomes:UP000001657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CI {ECO:0000313|EMBL:ADK03079.1,
RC   ECO:0000313|Proteomes:UP000001657};
RX   PubMed=20634886; DOI=10.1371/journal.pone.0010986;
RA   Klee S.R., Brzuszkiewicz E.B., Nattermann H., Bruggemann H., Dupke S.,
RA   Wollherr A., Franz T., Pauli G., Appel B., Liebl W., Couacy-Hymann E.,
RA   Boesch C., Meyer F.D., Leendertz F.H., Ellerbrok H., Gottschalk G.,
RA   Grunow R., Liesegang H.;
RT   "The genome of a Bacillus isolate causing anthrax in chimpanzees
RT   combines chromosomal properties of B. cereus with B. anthracis
RT   virulence plasmids.";
RL   PLoS ONE 5:E10986-E10986(2010).
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; CP001746; ADK03079.1; -; Genomic_DNA.
DR   RefSeq; WP_000055578.1; NC_014335.1.
DR   RefSeq; YP_003790217.1; NC_014335.1.
DR   EnsemblBacteria; ADK03079; ADK03079; BACI_c03380.
DR   KEGG; bal:BACI_c03380; -.
DR   PATRIC; 42175225; VBIBacCer111781_0607.
DR   HOGENOM; HOG000238227; -.
DR   KO; K01952; -.
DR   OMA; MFGVMWS; -.
DR   BioCyc; BCER637380:GHO7-328-MONOMER; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000001657; Chromosome.
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   PIRSF; PIRSF001587; FGAM_synthase_II; 1.
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:UP000001657};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00420};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00420, ECO:0000313|EMBL:ADK03079.1};
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      317    319       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       273    273       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   METAL       538    538       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     500    500       ATP. {ECO:0000256|HAMAP-Rule:MF_00420}.
FT   BINDING     537    537       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
FT   BINDING     540    540       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00420}.
SQ   SEQUENCE   739 AA;  80175 MW;  8BEB25939B943EFF CRC64;
     MSLMLEPNPT QIKEERIYAE MGLTDEEFAM VEKILGRLPN YTETGLFSVM WSEHCSYKNS
     KPVLRKFPTT GERVLQGPGE GAGIVDIGDN QAVVFKMESH NHPSAIEPYQ GAATGVGGII
     RDVFSMGARP VALLNSLRFG ELQSPRVKYL FEEVVAGIAG YGNCIGIPTV GGEVQFDPCY
     EGNPLVNAMC VGLINHEDIK KGQAHGAGNT VMYVGASTGR DGIHGATFAS EELSESSEAK
     RPAVQVGDPF MEKLLIEACL ELIQSDALVG IQDMGAAGLT SSSAEMASKA GMGIEMYLDD
     VPQRETGMTP YEMMLSESQE RMLIVVKKGR EQEIVDLFEK YGLAAVTMGK VTEDKMLRLF
     HKGEMVAEVP ADALAEEAPI YHKPSKEAAY FAEFQQMKME TPKVENYKET LFALLQQPTI
     ASKEWVYDQY DYQVRTSTVV TPGSDAAVVR VRGTEKGLAM TTDCNSRYIY LDPEVGGKIA
     VAEAARNIVC SGGEPLAITD CLNFGNPEKP EIFWQIEKSV DGMSEACRTL QTPVIGGNVS
     MYNERSGEAV YPTPTVGMVG LVHDLKHVTT QEFKQAGDLV YVIGETKAEF GGSELQKMLH
     GKIFGQSPSI DLDVELKRQK QVLAAIQAGL VQSAHDVAEG GLAVAISESA IGANGLGATV
     KLDGEATAAL FAESQSRFVI TVKRENKEAF EKAVEAIQVG EVTNTNEVTI HNEENEVLLT
     ANVDEMRQAW KGAIPCLLK
//
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