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Database: UniProt/SWISS-PROT
Entry: PURL_BACWK
LinkDB: PURL_BACWK
Original site: PURL_BACWK 
ID   PURL_BACWK              Reviewed;         739 AA.
AC   A9VRF1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-SEP-2014, entry version 48.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL;
DE            Short=FGAM synthase;
DE            EC=6.3.5.3;
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II;
DE            Short=FGAR amidotransferase II;
DE            Short=FGAR-AT II;
DE   AltName: Full=Glutamine amidotransferase PurL;
DE   AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II;
GN   Name=purL; OrderedLocusNames=BcerKBAB4_0275;
OS   Bacillus weihenstephanensis (strain KBAB4).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B.,
RA   Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H.,
RA   Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P.,
RA   Weissenbach J., Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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 (By similarity).
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   -!- 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.
CC   -!- SUBUNIT: Monomer. Part of the FGAM synthase complex composed of 1
CC       PurL, 1 PurQ and 2 PurS subunits (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: In Gram-negative bacteria and most eukaryotes, FGAM
CC       synthase is only formed by PurL, a single polypeptide of 140 kDa
CC       (large PurL). However in Gram-positive bacteria and
CC       archaebacteria, phosphoribosylformylglycinamidine synthase is
CC       composed of three separate proteins: PurL (small PurL), PurQ and
CC       PurS (By similarity).
CC   -!- SIMILARITY: Belongs to the FGAMS family.
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DR   EMBL; CP000903; ABY41541.1; -; Genomic_DNA.
DR   RefSeq; YP_001643169.1; NC_010184.1.
DR   ProteinModelPortal; A9VRF1; -.
DR   STRING; 315730.BcerKBAB4_0275; -.
DR   EnsemblBacteria; ABY41541; ABY41541; BcerKBAB4_0275.
DR   GeneID; 5840445; -.
DR   KEGG; bwe:BcerKBAB4_0275; -.
DR   PATRIC; 19004950; VBIBacWei55973_0839.
DR   eggNOG; COG0046; -.
DR   HOGENOM; HOG000238227; -.
DR   KO; K01952; -.
DR   OMA; QAVVFKI; -.
DR   OrthoDB; EOG6FNHHR; -.
DR   BioCyc; BWEI315730:GHRU-348-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:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
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; Complete proteome; Cytoplasm; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN         1    739       Phosphoribosylformylglycinamidine
FT                                synthase subunit PurL.
FT                                /FTId=PRO_1000194822.
FT   REGION       99    102       Substrate binding (By similarity).
FT   REGION      317    319       Substrate binding (By similarity).
FT   ACT_SITE     54     54       By similarity.
FT   ACT_SITE    100    100       Proton acceptor (By similarity).
FT   METAL        98     98       Magnesium 1 (By similarity).
FT   METAL       122    122       Magnesium 2 (By similarity).
FT   METAL       273    273       Magnesium 2 (By similarity).
FT   METAL       538    538       Magnesium 1 (By similarity).
FT   BINDING      57     57       ATP (By similarity).
FT   BINDING      96     96       ATP (By similarity).
FT   BINDING     121    121       Substrate (By similarity).
FT   BINDING     245    245       Substrate (By similarity).
FT   BINDING     500    500       ATP (By similarity).
FT   BINDING     537    537       ATP; via carbonyl oxygen and amide
FT                                nitrogen (By similarity).
FT   BINDING     540    540       Substrate (By similarity).
SQ   SEQUENCE   739 AA;  80338 MW;  51E4D6552E30EA1B 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
     HKDEMVAEVP ADALAEEAPI YHKPSKEAAY FAEFQQMKME TPKVEDYKET LLALLQQPTI
     ASKEWVYDQY DYQVRTSTIV TPGSDAAVIR VRGTEKGLAM TTDCNSRYIY LDPEVGGKIA
     VAEAARNIVC SGGEPLAITD CLNFGNPEKP EIFWQIEKSV DGMSEACRKL QTPVIGGNVS
     MYNERSGEAV YPTPTVGMVG LVHDLKHVTT QEFKQAGDLV YVIGETKAEF GGSELQKMIY
     GKIFGQSPSI DLDVELKRQK QVLAAIQAGL VQSAHDVAEG GLAVAITESA IGAKGLGATV
     KLDGEATAVL FAESQSRFVI TVKRENKEAF EKAVEAIQVG EVTNTNEVTI HNEENEVLLT
     ANVDEMRKAW KGAIPCLLK
//
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