PUR4_PSEA6
ID PUR4_PSEA6 Reviewed; 1295 AA.
AC Q15R69;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=Patl_3113;
OS Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=342610;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6c / ATCC BAA-1087;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C.,
RA Bartlett D., Higgins B.P., Richardson P.;
RT "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL Submitted (JUN-2006) 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; CP000388; ABG41619.1; -; Genomic_DNA.
DR RefSeq; WP_011575857.1; NC_008228.1.
DR AlphaFoldDB; Q15R69; -.
DR SMR; Q15R69; -.
DR STRING; 342610.Patl_3113; -.
DR EnsemblBacteria; ABG41619; ABG41619; Patl_3113.
DR KEGG; pat:Patl_3113; -.
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; UP000001981; 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..1295
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264585"
FT DOMAIN 1042..1295
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 302..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1135
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1260
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1262
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 306..317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 677
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 678
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 717
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 721
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 884
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 886
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1295 AA; 140706 MW; ADA7B6143201C924 CRC64;
MLVLRGAPAL SEFRTKKLMQ SIEALNLPVH ALFAEFVHFA QVSAQLEAND QQVLDKLLTY
GPKIQEKQHK GLLLLVIPRA GTISPWSSKA TDIAHNCGLN NVERLERGCA FYIDADPLND
TQLIQLKNVL HDRMTQSVVS DLQDASILFK HEAPKPLTSI DVLGGGREEL VSANVRLGLA
LAEDEVDYLV SSFEKLGRNP NDIELYMFAQ ANSEHCRHKI FNADWTIDGQ TQPKSLFKMI
KNTYEKCPDY VHSAYADNAA VMEGSFAGRF FPQADNNQYR YHHEDIDILM KVETHNHPTA
IAPFSGAATG SGGEIRDEGA TGRGSKPKAG LVGFSVSNLR IPGFEQPWEN DYGKPERIVT
AFDIMLNGPL GGAAFNNEFG RPNILGYFRT YEQKVTSFNG EEVRGYHKPI MLAGGLGNIR
KQHTQKGEIT VGAKLIALGG PAMNIGLGGG AASSMASGES NEDLDFASVQ RDNPEMERRC
QEVIDKCWQL GENNPIQFIH DVGAGGLSNA FPELVNDGGR GAVFSLRNVP NDEPGMTPLE
VWCNESQERY VMSVAPENLA TFTDICARER APFAVVGEAT QARHLTLDDS HFNNKPIDMP
LDVLLGKAPK MHRDVQSKAL TGNAFDVSNI DLDEAALRLL HLPAVAEKTF LITIGDRSVT
GLVNRDQMVG PWQIPVADVA VTAAAFDTYQ GEAMSLGERT PAALLNYGAS ARLAVGEALT
NIAAADIGDL KRIKLSANWM AAAGHPGEDA GLYEAVKAVG EELCPALGLT IPVGKDSMSM
KTQWQDAQGD KAVTSPMSLV ITAFGAVKDV RKTLTPELTT KGDTCLMLID LGAGQNRMGA
SCLAQVYQQL GDKTPDVDSP ELLKGFFLAI QQLVNEKALH AYHDRSDGGL FTTLVEMAFA
GNTGLDIKLD ALTGDNASAL FNEELGAVIQ FDADKLNQVD AILAANGLSG VSHVIGTLSD
DDQIRFSREG EPVLQNSRGV YRNAWAQTTH HMQRLRDNPE CAEQELASKN DLNNPGLHAA
LSFDVTEDVA APYIAKGIAP KMAILREQGV NSHVEMAAAF DRAGFASVDV HMSDILAGRV
SLSEFQGLVA CGGFSYGDVL GAGEGWAKSI LFNAMARDEF SAFFERNETF SLGVCNGCQM
LSNLKSLIPG AEHWPHFVTN QSERFEARVA MLEVKDSPSI FFKGMQGSKM PIAVSHGEGR
AEFAQTTGLE AALDSNTIAL QYVDNYGKVT EQYPANPNGS PAGISGLTSK DGRATIMMPH
PERVFRTVAN SWHPDDWQED SPWMRMFRNA RVYLG
