PUR4_VIBCH
ID PUR4_VIBCH Reviewed; 1297 AA.
AC Q9KTN2;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
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=VC_0869;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF94031.1; -; Genomic_DNA.
DR PIR; A82272; A82272.
DR RefSeq; NP_230516.1; NC_002505.1.
DR RefSeq; WP_001221777.1; NC_002505.1.
DR AlphaFoldDB; Q9KTN2; -.
DR SMR; Q9KTN2; -.
DR STRING; 243277.VC_0869; -.
DR MEROPS; C56.972; -.
DR PRIDE; Q9KTN2; -.
DR DNASU; 2614536; -.
DR EnsemblBacteria; AAF94031; AAF94031; VC_0869.
DR GeneID; 57739565; -.
DR KEGG; vch:VC_0869; -.
DR PATRIC; fig|243277.26.peg.829; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR BioCyc; VCHO:VC0869-MON; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000000584; 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; Reference proteome.
FT CHAIN 1..1297
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100420"
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; 141421 MW; D24DA2875D392696 CRC64;
MRILRGSPAL SEFRVNKLLT ACREQQLPVT GIYAEFMHFA DLKAELNPQE LEKLEKLLTY
GPTIQEHEPQ GLLLLVTPRP GTISPWSSKA TDIAHNCGLH GIKRLERGTA YYVEAETALT
AAQIATLEAL LHDRMMEVVF AELTDAQQLF SVAEPAPMSQ VDVLAGGRRA LEEANVSLGL
ALAEDEIDYL VESFTKLGRN PNDIELMMFA QANSEHCRHK IFNADWTIDG VKQDKSLFKM
IKNTFEQTPD YVLSAYKDNA AVMTGSTVGR FFPDPESRQY TYHHEDAHIL MKVETHNHPT
AISPWPGAST GSGGEIRDEG ATGIGGKPKA GLVGFTTSNL RIPGFEQPWE SDFGKPSRIV
NALDIMLEGP LGGAAFNNEF GRPNLLGYFR TYEEKVTSHA GEEVRGYHKP IMIAGGMGNI
RAEHIQKKEI PVGAKLIVLG GPAMNIGLGG GAASSMASGQ SAEDLDFASV QRENPEMERR
CQEVIDRCWQ LGDKNPIAFI HDVGAGGISN ALPELVNDGD RGGKFQLRNV PNDEPGMSPL
EIWCNESQER YVLAVAAEDM PLFDAICQRE RAPYAVVGEA TEERHLTLED SHFANTPIDM
PMDILLGKPP KMHREASTLK VSSPALERSG IELNEAVDRV LRLPAVAEKT FLITIGDRSV
TGLVARDQMV GPWQVPVANC AVTAASFDSY HGEAMSMGER TPVALLDFGA SARLAVGEAI
TNIAATDIGE LKRIKLSANW MSPAGHPGED AGLYEAVKAV GEELCPALGI TIPVGKDSMS
MKTKWQENGE QKEVTSPLSL IITAFARVED IRKTVTPQLR TDLGETSLIL IDLGNGQNRL
GATALAQVYK QLGDKPADVD NAAQLKGFFD AVQTLVRNDK LVAYHDKGDG GLLVTLAEMA
FAGHCGIKAN IETLGDDALA ALFNEELGAV VQVKNDELNA VLATLAAHGL EACAHVIGEV
EASDRLLITC GEEVLIERSR TELRTIWAEM THKMQALRDN SACADQEFAA KQDNRDPGLN
AKLTYDVQAD VAAPYIAKGV RPKMAILREQ GVNSHVEMAA AFDRAGFDAV DVHMSDILTG
QTVLDAYQGL VACGGFSYGD VLGAGEGWAK SILFNAQARE QFEQFFQRKD TFSLGVCNGC
QMLSNLRDLI PGAELWPRFV RNESDRFEAR FSLVEVQKSP SLFFSEMAGS RMPIAVSHGE
GRVEVRDAQH LAAIEQSGTV AIRFVDNFGQ PTQAYPSNPN GSPNAITGLT TQDGRVTIMM
PHPERVFRTV ANSWHPDNWG ENGAWMRMFQ NARKYFG
