ID   PURL_PROMA              Reviewed;         793 AA.
AC   Q7VEK9;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   27-MAR-2024, entry version 126.
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=Pro_0003;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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}.
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};
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00420}.
CC   -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000255|HAMAP-
CC       Rule:MF_00420}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP99049.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE017126; AAP99049.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_874397.1; NC_005042.1.
DR   AlphaFoldDB; Q7VEK9; -.
DR   SMR; Q7VEK9; -.
DR   STRING; 167539.Pro_0003; -.
DR   EnsemblBacteria; AAP99049; AAP99049; Pro_0003.
DR   KEGG; pma:Pro_0003; -.
DR   PATRIC; fig|167539.5.peg.3; -.
DR   eggNOG; COG0046; Bacteria.
DR   HOGENOM; CLU_003100_0_1_3; -.
DR   OrthoDB; 9804441at2; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000001420; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02203; PurL_repeat1; 1.
DR   CDD; cd02204; PurL_repeat2; 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   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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT   CHAIN           1..793
FT                   /note="Phosphoribosylformylglycinamidine synthase subunit
FT                   PurL"
FT                   /id="PRO_0000100477"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   ACT_SITE        99
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         95
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         98..101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         121
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         272
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         316..318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         523
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         560
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         561
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
FT   BINDING         563
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00420"
SQ   SEQUENCE   793 AA;  86331 MW;  DA470F1FED396B31 CRC64;
     MIKSKDYLVD YNVELALKKE GLTKADYIEI CNRLKRSPNR TELGMFGVMW SEHCCYRNSR
     SLLSNFPTTG KNILVGPGEN AGVVDLGEGQ RLAFKIESHN HPSAIEPFQG AATGVGGILR
     DIFTMGARPI ALLNSLRFGP LDTPINVGLL EGVVSGIAHY GNCVGVPTVG GEVAFDKSYS
     GNPLVNAMAL GIMETKEIVC SGAKGIDFPV IYVGSTTGRD GMGGASFASS ELTQASIDDR
     PAVQVGDPFL EKGLIEGCLE AFKTGYVVAA QDMGAAGLTC SCSEMAAKGG VGIELDLDLV
     PAREKNMTAY EFLLSESQER MLFVVEPGKE ELIMNKFRKW GLQAKVVGKV LEENIVRVIH
     EKQIVVNLPA DSLAEDTPVN KHELLEEPPG FIKDHWKWDE TSLPKVSIKG VHFKENNTIL
     DWNQIILRLL DDPTIASKRW IYNQYDYQVQ NNTIIAPGIG DAALIRLREI ENQNQNSNRG
     IAAVVDCPNR WVALDPERGA IAAVAEASRN ISCVGAKPLA VTDNLNFSSP EDPIGYWQLA
     KACKGLSKAC VVLETPVTGG NVSLYNETAL PNGLKQPIQP TPVVGMIGLI QDINSATRQG
     WKDQGDQIYL LGTSIDPSIL NNQNISLAAT SYLENIYGLK TGRPPLIDLE FEKLVQLFLR
     ESIANNLIKS AHDISDGGLV IGLAESCISS GLGIECNLPE IDNRLDKLLF AEGGSRVLVS
     VSPNNIHNIK NSLNNFNIAN SEQISFNYLG TVTDNKYFQI NINQTKIIDL SVNEITNKFE
     RSIPRRINST IVS
//