ID   PUR4_VIBVU              Reviewed;        1297 AA.
AC   Q8DF81;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Phosphoribosylformylglycinamidine synthase {ECO:0000255|HAMAP-Rule:MF_00419};
DE            Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00419};
DE            Short=FGAMS {ECO:0000255|HAMAP-Rule:MF_00419};
DE            EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00419};
DE   AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419};
DE            Short=FGAR amidotransferase {ECO:0000255|HAMAP-Rule:MF_00419};
DE            Short=FGAR-AT {ECO:0000255|HAMAP-Rule:MF_00419};
GN   Name=purL {ECO:0000255|HAMAP-Rule:MF_00419}; OrderedLocusNames=VV1_0340;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the
CC       purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of
CC       formylglycinamide ribonucleotide (FGAR) and glutamine to yield
CC       formylglycinamidine ribonucleotide (FGAM) and glutamate.
CC       {ECO:0000255|HAMAP-Rule:MF_00419}.
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_00419};
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_00419}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00419}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00419}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC       {ECO:0000255|HAMAP-Rule:MF_00419}.
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DR   EMBL; AE016795; AAO08867.1; -; Genomic_DNA.
DR   RefSeq; WP_011078440.1; NC_004459.3.
DR   AlphaFoldDB; Q8DF81; -.
DR   SMR; Q8DF81; -.
DR   EnsemblBacteria; AAO08867; AAO08867; VV1_0340.
DR   KEGG; vvu:VV1_0340; -.
DR   HOGENOM; CLU_001031_0_2_6; -.
DR   OMA; LSANWMW; -.
DR   UniPathway; UPA00074; UER00128.
DR   Proteomes; UP000002275; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1330.10; -; 2.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.90.650.10; -; 2.
DR   HAMAP; MF_00419; PurL_1; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR040707; FGAR-AT_N.
DR   InterPro; IPR010073; PurL_large.
DR   InterPro; IPR041609; PurL_linker.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   InterPro; IPR036604; PurS-like_sf.
DR   Pfam; PF02769; AIRS_C; 2.
DR   Pfam; PF18072; FGAR-AT_linker; 1.
DR   Pfam; PF18076; FGAR-AT_N; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF55326; SSF55326; 2.
DR   SUPFAM; SSF56042; SSF56042; 2.
DR   SUPFAM; SSF82697; SSF82697; 1.
DR   TIGRFAMs; TIGR01735; FGAM_synt; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glutamine amidotransferase; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           1..1297
FT                   /note="Phosphoribosylformylglycinamidine synthase"
FT                   /id="PRO_0000100422"
FT   DOMAIN          1044..1297
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   ACT_SITE        1137
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   ACT_SITE        1262
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   ACT_SITE        1264
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         307..318
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         678
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         718
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         722
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT   BINDING         886
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ   SEQUENCE   1297 AA;  140847 MW;  C8FBA0BC243CEF32 CRC64;
     MRILRGSPAL SEFRVNKLLE LCREQDLPVT GIYAEFMHFA DLTSELDAEA LEKLEKLLTY
     GPTIEEHEPQ GLLLLVTPRP GTISPWSSKA TDIAQNCGLN AVKRLERGTA YYVESSSELS
     SVQIDIVKSI IHDRMMEAVF GDLEAAAALF SVAQPAPMTQ VDILSGGRLA LEEANVSLGL
     ALAEDEIDYL VENFTKLGRN PNDIELMMFA QANSEHCRHK IFNADWTIDG VEQPKSLFKM
     IKNTFETTPD HVLSAYKDNA AVMTGSKVGR FFPDPETRQY NYHHEDAHIL MKVETHNHPT
     AISPWPGAST GSGGEIRDEG ATGIGGKPKA GLVGFTTSNL RIPGFEQPWE TDFGKPGRIV
     NALDIMLEGP LGGAAFNNEF GRPNLLGYFR TYEEKVTSHA GEEVRGYHKP IMIAGGMGNI
     RDEHVQKKEI PVGASLIVLG GPAMNIGLGG GAASSMASGQ SAEDLDFASV QRENPEMERR
     CQEVIDRCWQ LGDNNPIAFI HDVGAGGISN ALPELVNDGE RGGKFQLRDV PNDEPGMSPL
     EIWCNESQER YVLAVAPENM AAFDAICKRE RAPYAVVGVA TEERHLTLED AHFDNTPIDM
     PMDILLGKPP KMHREATTLK VDSPAMTRDG IELNEAVDRV LRLPTVAEKT FLITIGDRTV
     TGLVARDQMV GPWQVPVANC AVTAASYDTY HGEAMSMGER TPVALLDFGA SARLAVGESL
     TNIAATDIGD IKRIKLSANW MSPAGHPGED AGLYEAVKAV GEELCPALGL TIPVGKDSMS
     MKTKWNENGE EKEVTSPLSL IITAFARVED VRKTITPQLR TDKGETSLVL VDLGNGKNRL
     GATALAQVYK QLGDKPADVD NAEQLKGFFD AMQALVRQDK LLAYHDKGDG GLLVTLAEMA
     FAGHCGVNAN IAALGDDVLA ALFNEELGAV VQVKNDELDS VLSTLAANGL EACSHVIGAI
     DASDNFVIRS GDAVILERSR TDLRVIWAET THKMQALRDN PACADQEFEA KKDNSDPGLN
     VSLSFDVNED IAAPYIAKGA KPKMAILREQ GVNSHVEMAA AFDRAGFEAT DIHMSDILTG
     QAVLDEYHGL VACGGFSYGD VLGAGEGWAK SVLFNAQARE QFQAFFNREN TFSLGVCNGC
     QMLSNLKELI PGADLWPRFV RNESERFEAR FSLVEVQKSD SVFFDGMAGS RMPIAVSHGE
     GRVEVRDAQH LAAIEASGTV AVRFVDNLGN PTQQYPNNPN GSPNAITGLT TKDGRVTIMM
     PHPERVFRTV ANSWAPEGWG ENGAWMRMFQ NARKNLG