PURL_BACSU
ID PURL_BACSU Reviewed; 742 AA.
AC P12042;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000255|HAMAP-Rule:MF_00420};
DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00420};
DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00420};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000255|HAMAP-Rule:MF_00420};
DE Short=FGAR amidotransferase II {ECO:0000255|HAMAP-Rule:MF_00420};
DE Short=FGAR-AT II {ECO:0000255|HAMAP-Rule:MF_00420};
DE AltName: Full=Glutamine amidotransferase PurL {ECO:0000255|HAMAP-Rule:MF_00420};
DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000255|HAMAP-Rule:MF_00420};
GN Name=purL {ECO:0000255|HAMAP-Rule:MF_00420}; OrderedLocusNames=BSU06480;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3036807; DOI=10.1016/s0021-9258(18)47560-6;
RA Ebbole D.J., Zalkin H.;
RT "Cloning and characterization of a 12-gene cluster from Bacillus subtilis
RT encoding nine enzymes for de novo purine nucleotide synthesis.";
RL J. Biol. Chem. 262:8274-8287(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, MASS
RP SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=15301530; DOI=10.1021/bi049127h;
RA Hoskins A.A., Anand R., Ealick S.E., Stubbe J.;
RT "The formylglycinamide ribonucleotide amidotransferase complex from
RT Bacillus subtilis: metabolite-mediated complex formation.";
RL Biochemistry 43:10314-10327(2004).
RN [4]
RP SEQUENCE REVISION TO 513.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
CC -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase
CC complex involved in the purines biosynthetic pathway. Catalyzes the
CC ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and
CC glutamine to yield formylglycinamidine ribonucleotide (FGAM) and
CC glutamate. The FGAM synthase complex is composed of three subunits.
CC PurQ produces an ammonia molecule by converting glutamine to glutamate.
CC PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-
CC dependent manner. PurS interacts with PurQ and PurL and is thought to
CC assist in the transfer of the ammonia molecule from PurQ to PurL.
CC {ECO:0000255|HAMAP-Rule:MF_00420, ECO:0000269|PubMed:15301530}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC ChEBI:CHEBI:456216; EC=6.3.5.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00420, ECO:0000269|PubMed:15301530};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000269|PubMed:15301530};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=181 uM for ATP (FGAM synthase activity at pH 7.2 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:15301530};
CC KM=398 uM for ATP (Glutamine amidotransferase activity at pH 7.2 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:15301530};
CC KM=507 uM for FGAR (FGAM synthase activity at pH 7.2 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:15301530};
CC KM=1.3 mM for glutamine (FGAM synthase activity at pH 7.2 and 37
CC degrees Celsius) {ECO:0000269|PubMed:15301530};
CC KM=2.5 mM for FGAR (Glutamine amidotransferase activity at pH 7.2 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:15301530};
CC KM=3.5 mM for NH3 (Glutamine amidotransferase activity at pH 7.2 and
CC 37 degrees Celsius) {ECO:0000269|PubMed:15301530};
CC Note=kcat is 2.49 sec(-1) for FGAM synthase activity with FGAR as
CC substrate (at pH 7.2 and 37 degrees Celsius). kcat is 0.044 sec(-1)
CC for glutamine amidotransferase activity with NH3 as substrate (at pH
CC 7.2 and 37 degrees Celsius).;
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP-
CC Rule:MF_00420}.
CC -!- SUBUNIT: Monomer. Part of the FGAM synthase complex composed of 1 PurL,
CC 1 PurQ and 2 PurS subunits. {ECO:0000255|HAMAP-Rule:MF_00420,
CC ECO:0000269|PubMed:15301530}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00420}.
CC -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000255|HAMAP-
CC Rule:MF_00420}.
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DR EMBL; J02732; AAA22679.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12468.2; -; Genomic_DNA.
DR PIR; G29326; SYBS2G.
DR RefSeq; NP_388530.2; NC_000964.3.
DR RefSeq; WP_003244429.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; P12042; -.
DR SMR; P12042; -.
DR IntAct; P12042; 1.
DR MINT; P12042; -.
DR STRING; 224308.BSU06480; -.
DR PaxDb; P12042; -.
DR PRIDE; P12042; -.
DR EnsemblBacteria; CAB12468; CAB12468; BSU_06480.
DR GeneID; 939233; -.
DR KEGG; bsu:BSU06480; -.
DR PATRIC; fig|224308.179.peg.704; -.
DR eggNOG; COG0046; Bacteria.
DR InParanoid; P12042; -.
DR OMA; FIEPYQG; -.
DR PhylomeDB; P12042; -.
DR BioCyc; BSUB:BSU06480-MON; -.
DR BioCyc; MetaCyc:BSU06480-MON; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004359; F:glutaminase activity; IEA:RHEA.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IDA:UniProtKB.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.30.1330.10; -; 2.
DR Gene3D; 3.90.650.10; -; 2.
DR HAMAP; MF_00420; PurL_2; 1.
DR InterPro; IPR010074; PRibForGlyAmidine_synth_PurL.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR PANTHER; PTHR43555; PTHR43555; 1.
DR Pfam; PF00586; AIRS; 2.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..742
FT /note="Phosphoribosylformylglycinamidine synthase subunit
FT PurL"
FT /id="PRO_0000100440"
FT ACT_SITE 54
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT ACT_SITE 100
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 99..102
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 317..319
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 537
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT BINDING 540
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT CONFLICT 513
FT /note="F -> L (in Ref. 1; AAA22679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 742 AA; 80325 MW; 58F527FD16271557 CRC64;
MSLLLEPSKE QIKEEKLYQQ MGVSDDEFAL IESILGRLPN YTEIGIFSVM WSEHCSYKNS
KPILRKFPTS GERVLQGPGE GAGIVDIGDN QAVVFKIESH NHPSALEPYQ GAATGVGGII
RDVFSMGARP IAVLNSLRFG ELTSPRVKYL FEEVVAGIAG YGNCIGIPTV GGEVQFDSSY
EGNPLVNAMC VGLINHEDIK KGQAKGVGNT VMYVGAKTGR DGIHGATFAS EEMSDSSEEK
RSAVQVGDPF MEKLLLEACL EVIQCDALVG IQDMGAAGLT SSSAEMASKA GSGIEMNLDL
IPQRETGMTA YEMMLSESQE RMLLVIERGR EQEIIDIFDK YDLEAVSVGH VTDDKMLRLT
HKGEVVCELP VDALAEEAPV YHKPSQEPAY YREFLETDVP APQIEDANEM LKALLQQPTI
ASKEWVYDQY DYMVRTNTVV APGSDAGVLR IRGTKKALAM TTDCNARYLY LDPEVGGKIA
VAEAARNIIC SGAEPLAVTD NLNFGNPEKP EIFWQIEKAA DGISEACNVL STPVIGGNVS
LYNESNGTAI YPTPVIGMVG LIEDTAHITT QHFKQAGDLV YVIGETKPEF AGSELQKMTE
GRIYGKAPQI DLDVELSRQK ALLDAIKKGF VQSAHDVSEG GLGVAIAESV MTTENLGANV
TVEGEAALLF SESQSRFVVS VKKEHQAAFE ATVKDAVHIG EVTADGILAI QNQDGQQMIH
AQTKELERVW KGAIPCLLKS KA
