PUR4_VIBVY
ID PUR4_VIBVY Reviewed; 1297 AA.
AC Q7MN70;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 125.
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=VV0847;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC93611.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000037; BAC93611.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_043877086.1; NC_005139.1.
DR AlphaFoldDB; Q7MN70; -.
DR SMR; Q7MN70; -.
DR STRING; 672.VV93_v1c07870; -.
DR EnsemblBacteria; BAC93611; BAC93611; BAC93611.
DR KEGG; vvy:VV0847; -.
DR PATRIC; fig|196600.6.peg.853; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 26038at2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000002675; Chromosome I.
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; Reference proteome.
FT CHAIN 1..1297
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100423"
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; 140905 MW; DC9035912AD88570 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 GDVVVLERSR TDLRVIWAET THKMQALRDN PACADQEFEA KKDNSDPGLN
VSLSYEVNED 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 NARKNLA
