PUR4_PASMU
ID PUR4_PASMU Reviewed; 1297 AA.
AC Q9CLW4;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=PM1085;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03169.1; -; Genomic_DNA.
DR RefSeq; WP_010907012.1; NC_002663.1.
DR AlphaFoldDB; Q9CLW4; -.
DR SMR; Q9CLW4; -.
DR STRING; 747.DR93_879; -.
DR PRIDE; Q9CLW4; -.
DR EnsemblBacteria; AAK03169; AAK03169; PM1085.
DR KEGG; pmu:PM1085; -.
DR PATRIC; fig|272843.6.peg.1099; -.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000000809; Chromosome.
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_0000100412"
FT DOMAIN 1043..1297
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 305..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 679
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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"
FT BINDING 888
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1297 AA; 143043 MW; 9362706FEFE34CB4 CRC64;
MLQIFRGSPA LSEFRLNQLA VRFQKANLPV SACYAEYIHF ADLSDRLTEE ETAKLDQLLH
YGPTLAGHDP VGHCFIVIPR IGTISSWSSK ATDIAHNCGL NKVNRLERGL AFYFEFDRTL
SSEEQQRLVS HIHDRMLEGI IHTPEEAKVL FDQQAPKPFT TVDILSGGRQ ALENANVELG
LALAEDEIDY LVENFTALGR NPNDIELYMF AQANSEHCRH KIFNADWIID GEKQEKSLFK
MIKNTFEKTP DHVLSAYKDN AAVMEGSKVG RFFPDQDGQY RYHNEDAHIL MKVETHNHPT
AISPFPGAAT GSGGEIRDEG ATGRGAKPKA GLVGFSVSNL VIPGFEQPWE NPVSKPNRIA
SALDIMIEGP LGGAAFNNEF GRPALLGYFR TYEEKVNSFA GEEVRGYHKP IMLAGGIGNI
RAEHVQKGEI PVGAKLIVLG GPAMNIGLGG GAASSMASGK SKEDLDFASV QRDNPEMERR
CQEVIDRCWQ LGEDNPILFI HDVGAGGLSN AMPELVHDGG RGGKFELRKI LSDERGMSPL
EIWCNESQER YVLAVAPEKL ELFTALCERE RAPFAVIGEA TEQEHLTLHD DHFDNNPIDL
PMNVLLGKTP KMTRDVKSKT VEGSALDHSQ IDLKEAFHRV LRLPVVAEKT FLITIGDRSV
TGMVARDQMV GPWQIPVADC AVTTASLDSY HGEAMSMGER APVALLDFAA SARLAVAESI
TNIAATNIGD IKRIKLSANW MSAAGHEGED AGLYQAVKAV GEELCPQLGL TIPVGKDSMS
MKTTWHENGE QKTVTAPLSL VISAFARVED VRKTVTPQLR TDKGHSRLLL IDLGEGKNRL
GATALAQVYK QLGDKPADVV NVESLKNFFN AMQALVAEQK LLAYHDRSDG GLIATLAEMA
FAGNCGLSIH ISALGDNDLA VLFNEELGAV IQVRESDLSY VRDVLSQHGL IHLTKELGEV
TTEDRIEISR GTKLLFSQKR SELRGIWAEL THQMQRLRDN PECADQEFAA KKDPENKGFS
AHLTYDINED IAAPYIATGK KPRIAILREQ GVNSHYEMAA AFDRAGFEAI DVHMSDLHNA
RYRLKDFNAL VACGGFSYGD VLGAGGGWAK SILFNPMLRD QFSEFFANPN TLTLGVCNGC
QMVSNLAEII PGTDAWPRFV RNKSERFEAR AALVRINETN SLWFQGMAGS HMPIAVSHGE
GRVEFKHDQQ LQMLKDQNLI VAQYIDNNLN PTEIYPANPN GSVEGITALS NQDGRVAIMM
PHPERVFRTV SNSWHPEDWS EDGAWMRLFR NARVVLE
