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   02-SEP-2026, entry version 171.
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};
GN   OrderedLocusNames=BSU06480;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   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=N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + L-
CC         glutamine + ATP + H2O = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC         ribosyl)acetamidine + L-glutamate + ADP + phosphate + H(+);
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=L-glutamine + H2O = 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; NC_000964.3.
DR   AlphaFoldDB; P12042; -.
DR   SMR; P12042; -.
DR   FunCoup; P12042; 610.
DR   IntAct; P12042; 1.
DR   MINT; P12042; -.
DR   STRING; 224308.BSU06480; -.
DR   PaxDb; 224308-BSU06480; -.
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   OrthoDB; 9804441at2; -.
DR   PhylomeDB; P12042; -.
DR   BioCyc; BSUB:BSU06480-MONOMER; -.
DR   BioCyc; MetaCyc:BSU06480-MONOMER; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P12042; -.
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   CDD; cd02203; PurL_repeat1; 1.
DR   CDD; cd02204; PurL_repeat2; 1.
DR   FunFam; 3.30.1330.10:FF:000004; Phosphoribosylformylglycinamidine synthase subunit PurL; 1.
DR   FunFam; 3.30.1330.10:FF:000011; Phosphoribosylformylglycinamidine synthase subunit PurL; 1.
DR   FunFam; 3.90.650.10:FF:000009; Phosphoribosylformylglycinamidine synthase subunit PurL; 1.
DR   FunFam; 3.90.650.10:FF:000013; Phosphoribosylformylglycinamidine synthase subunit PurL; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 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   NCBIfam; TIGR01736; FGAM_synth_II; 1.
DR   NCBIfam; NF002290; PRK01213.1; 1.
DR   PANTHER; PTHR43555; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 1.
DR   PANTHER; PTHR43555:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL; 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; SSF56042; PurM C-terminal domain-like; 2.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
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
//