PUR4_HAHCH
ID PUR4_HAHCH Reviewed; 1298 AA.
AC Q2SK05;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=HCH_02192;
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396;
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(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; CP000155; ABC29019.1; -; Genomic_DNA.
DR RefSeq; WP_011396089.1; NC_007645.1.
DR AlphaFoldDB; Q2SK05; -.
DR SMR; Q2SK05; -.
DR STRING; 349521.HCH_02192; -.
DR PRIDE; Q2SK05; -.
DR EnsemblBacteria; ABC29019; ABC29019; HCH_02192.
DR KEGG; hch:HCH_02192; -.
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; UP000000238; 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..1298
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264577"
FT DOMAIN 1046..1298
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1139
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1263
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1265
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 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 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 1298 AA; 141107 MW; 06E16745026E6254 CRC64;
MFELRGAPAL SPFRREKLLK NIQEQAPEVQ SVYAEYMHFV DLEGDLSAEQ RTVLDRLLQY
GPQGQSEMPS GTLFLVVPRP GTISPWSSKA TDIAHNCGLT AIRRIERGVA YHVGSSEQLS
SERRAAIAAI LHDRMTQSVF HEIAGAELLF AHAEPKPMTT VDILADGRDA LAEANRSMGL
ALAEDEIDYL TSAFTELGRN PTDVELMMFA QANSEHCRHK IFNATWEIDG EVQSHSLFGM
IRNTYEQGGQ DVLSAYCDNA AVIKGGQGGR FFPDHRTKIY GYNVEDIHIL MKVETHNHPT
AISPFAGAST GSGGEIRDEG ATGIGAKPKA GLTGFTVSNL NIPGYKQPWE GDYGKPERIV
SALQIMLDGP IGGAAFNNEF GRPALCGYFR TYEEQVPGVN GLEWRGYHKP IMIAGGMGNI
RASHVEKKDI SVDAKLIVLG GPAMLIGLGG GAASSMDSGA GQEDLDFASV QRDNPEMERR
CQEVIDRCWQ LGDDNPILFI HDVGAGGLSN ALPELVKDGG RGGLFELRDV PNDEPGMSPL
EIWCNESQER YVMAVAEQDM ELFDQLCRRE RCPYAVVGSA TEELKIQVSD EYFANSPVDL
PMSVLFGKPP KMHRTIERKS FTKPIFDSTT LDLKEAAERI LRLPSVASKS FLITIGDRSV
TGMVSRDQMV GPWQAPVSDV AVTTASFDTY RGEAMAMGER TPIALIDPPS SGRMAVGEAI
TNLAAAKIEK LSDIKLSANW MAAAGHPGED EALFETVKAV GMELCPELGI TIPVGKDSMS
MKTVWEEGEK QKSVTAPLSL IISGFAPVED VRKTLTPQMD LSTPSKLLLI DLGSGKNRLG
GSALAQVYRS VGAVAPDLDN PEELAAFFAC IQKLNNEGKL KAYHDRSDGG VFTTLCEMAF
ASRCGMTICF DGLVKDRTHI ARELFNEELG AVVQVSEEHV DEVKTCFADA GLADHVVVLG
EPHADQSVKF QHEGQTVLGY SRGALQKIWA ETSYRMQSMR DNSECAAEEF AAIDDDNDPG
LSAKLTYDVN EDIAAPFINR GAKPKIVVLR EQGVNSQAEM AAAFDRAGFS AVDVHMSDIL
SGAVSLSQFK ALAACGGFSF GDVLGAGEGW AKSILFNARA RDQFEAFFHR KDTFALGVCN
GCQMISNLKE LIPGADAWPR FVRNRSEQYE ARVAMVEVLD SPSILLQGMA GSMMPIAVAH
GEGLAEVGPE GAAALMAQKN VALRFVDNYG RPTMSHPFNP NGSPLGITSV CNDDGRITVM
MPHPERVFRA VANSWRPSAW SEDGAWMRMF RNARVWLG
