PUR4_PSET1
ID PUR4_PSET1 Reviewed; 1296 AA.
AC Q3IHZ2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=PSHAa2330;
OS Pseudoalteromonas translucida (strain TAC 125).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=326442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAC 125;
RX PubMed=16169927; DOI=10.1101/gr.4126905;
RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT Pseudoalteromonas haloplanktis TAC125.";
RL Genome Res. 15:1325-1335(2005).
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; CR954246; CAI87386.1; -; Genomic_DNA.
DR RefSeq; WP_011328987.1; NC_007481.1.
DR AlphaFoldDB; Q3IHZ2; -.
DR SMR; Q3IHZ2; -.
DR STRING; 326442.PSHAa2330; -.
DR EnsemblBacteria; CAI87386; CAI87386; PSHAa2330.
DR KEGG; pha:PSHAa2330; -.
DR PATRIC; fig|326442.8.peg.2252; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_6; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 26038at2; -.
DR BioCyc; PHAL326442:PSHA_RS11495-MON; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000006843; 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..1296
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264586"
FT DOMAIN 1043..1296
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT REGION 300..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1136
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1261
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1263
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 304..315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 675
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 715
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 719
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 885
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 887
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1296 AA; 140882 MW; 2F7EBAF8E8FFDBFC CRC64;
MLILRGAPAL SEFRVNKILA RCQQSQLPVT NVYAEYAHFA DLTSPLSSAE QTKLEKLLTY
GPTIAEHTPA GKLVLVTPRP GTISPWASKA TDIAHNCGLK QVHRVERGIA YYVEGELNAE
QLLQVTALLH DRMTEATHSQ FEDAAQLFRS DAPRQMSSVD ILSGGREALA IANVEQGFAL
ADDEIDYLVE NFIKLGRNPN DIELFMFAQA NSEHCRHKIF NADWTIDGEE QPKSLFKMIK
NTFEKNPENV LSAYKDNAAV MKGSKAGRFF PNTQGEYAYH QEDIEILMKV ETHNHPTAIA
PFSGAATGSG GEIRDEGATG RGSKPKAGLV GFTVSNLRIP GYEQPWESDF GKPGRIVTAL
DIMTEGPLGG AAFNNEFGRP NLLGYFRTYE EQVTSHNGLE VRGYHKPIML AGGLGNIRTD
HVQKGEIPVG AKLIALGGPA MNIGLGGGAA SSMASGQSNE DLDFASVQRE NPEMERRCQE
VIDKCWQLGD ENPIAFIHDV GAGGLSNAFP ELVNDGGRGG KFQLRDIPND EPGMAPHEIW
CNESQERYVL AVGVEDFDRF EAICKRERAQ YAVIGEATAE PHLTVADSHF DNNPVDLPLD
VLLGKAPKMH RDVTSKQVVG KALDVTNINV ADAAQRLLRL PTIAEKTFLI TIGDRSVTGL
VARDQMVGPW QVPVANCAVT AATYDTYHGE AMSLGERTPA ALLNYAASAR LAVAESLTNI
ACANIGSLEN IKLSANWMAA AGHPGEDAGL YEAVKAIGEE LCPALGLTIP VGKDSMSMKT
TWKDEGDSQE KSVTSPLSLI ITAFGRVDDV RKTVTPQLRT DKGETSLILV DLGAGKNRMG
ASSLAQVYKQ LGDITPDVDS PELLKGFYNA MQVLVADSKL LAYHDRSDGG LFTTVAEMAF
AGHTGVTVDI NGLTGNDIEA LYNEELGAVI QVANSDLDAV NAVLKDHGLA TISHIIGTLN
SDDAIVFNRG KNTVLSNTRT ELRTMWAETT YQMQARRDNP ECAKQEFDAK FDVKDPGLNV
KLNFDLNEDI AAPYIATGAK PPMAILREQG VNSHLEMAAA FNRAGFAAID VHMSDILEGR
LSLEQFKGLV ACGGFSYGDV LGAGEGWAKS ILFNDMAREQ FQSFFHREDT FSLGVCNGCQ
MLSTLKELIP GTEHWPRFVT NKSERFEARF SLVEIQENPS VFFNGMAGSR MPIAVSHGEG
HAEFANDNAV KAALDSGTVA VKFVDNYGNP TTQYPANPNG SPEGITGITS TDGRATVMMP
HPERVFRAVA NSWHPDEWRE DSPWMRMFRN ARKNVG
