PUR4_METFK
ID PUR4_METFK Reviewed; 1293 AA.
AC Q1H2I8;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 101.
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}; Synonyms=purL1;
GN OrderedLocusNames=Mfla_0887;
GN and
GN Name=purL2 {ECO:0000255|HAMAP-Rule:MF_00419}; OrderedLocusNames=Mfla_1031;
OS Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylobacillus.
OX NCBI_TaxID=265072;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT / ATCC 51484 / DSM 6875;
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 Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT "Complete sequence of Methylobacillus flagellatus KT.";
RL Submitted (MAR-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABE49155.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABE49299.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000284; ABE49299.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000284; ABE49155.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q1H2I8; -.
DR SMR; Q1H2I8; -.
DR STRING; 265072.Mfla_0887; -.
DR EnsemblBacteria; ABE49155; ABE49155; Mfla_0887.
DR EnsemblBacteria; ABE49299; ABE49299; Mfla_1031.
DR KEGG; mfa:Mfla_0887; -.
DR KEGG; mfa:Mfla_1031; -.
DR eggNOG; COG0046; Bacteria.
DR eggNOG; COG0047; Bacteria.
DR HOGENOM; CLU_001031_0_2_4; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000002440; 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..1293
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000264580"
FT DOMAIN 1040..1293
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1133
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1258
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT ACT_SITE 1260
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 308..319
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 676
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 883
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
FT BINDING 885
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00419"
SQ SEQUENCE 1293 AA; 140059 MW; ED2FEE4AC3F4EDB2 CRC64;
MISLRGSAAL SPFRIEKILA ALKGSAPRIT HLYAEFWHFA WSDQPLSEAQ QEVLKQILTY
GPRMSEEAPA GELFLVIPRP GTISPWSSRA TDIARHCGIE AIQRLERGIA FYAATADGSP
LTDAEKAALR PLIHDRMTEA VFASLTDAQK LYHTAEPAPL STVDILSGGK AALEAANAEM
GLALSPDEVD YLIENFQRMG RNPTDVELMM FAQANSEHCR HKIFNADWVI DGVAQAQSLF
GMIRNTHKLN PGKTVVAYAD NASIVEGGKT KRFYPLADGQ YGFVEEDMHF LMKVETHNHP
TAISPFAGAA TGAGGEIRDE GATGSGSKPK AGLTGFSVSN LHIPGFKQPW EHNNGKPDRI
ASALQIMVDG PLGGAAYNNE FGRPNIAGYF RTLEIESAGE IRGYHKPIML AGGVGNISAR
HAKKNPIPPG AALIQLGGPA MLIGLGGGAA SSMDTGANTE NLDFDSVQRG NPELERRAQE
VIDRCWQLGD KNPILSIHDV GAGGISNAFP ELVNDAGVGA RFQLRDVHNE EPGMSPREIW
SNEAQERYVM AVRKEDLPLF AEICERERCP FAVVGEATEE KRLVVSDRHF GNTPVDMDLS
VLLGKPPKMT RDVQHVAREL PAFDHSRIDL KEAAQRVLRL PGVADKTFLI TIGDRSVTGM
IARDQMVGPW QVPVADVAVT LDGFETYRGE AFAIGEKAPL ALIDAPASGR MAIGEAITNI
AASLIEDIAD LKLSANWMAP AGHPGEDAAL FDTVKAVGME LCPQLGISIP VGKDSMSMKT
VWEERNEKKA VTAPISLVVT AFAPTADARK TLTPQLRTDL GDTRLLLIDL GAGRNRLGGS
ALAQVYGSVG NVAPDVEDAD SLKHFFNAVQ KLNREGRLLA YHDRSDGGLF ATVVEMAFAG
RTGLELDIAS LGEDAVAVLY NEELGAVLQV RAADLDAITA ELETTLRGKV HVIGAPASHG
DIVIRQGTKL VFAESRVALH RAWSETTYQM QKLRDNPVCA QQEYDRLLDE RDAGLHAKLT
FDINENIAAP YIASGARPKM AILREQGVNG QVEMAAAFDR AGFNAFDVHM SDIISGRVSL
KDFAGFVACG GFSYGDVLGA GEGWAKSILF NPRARDEFTA FFNRTDSFAL GVCNGCQMMS
NLHSIIPGAG HWPHFVRNRS EQFEARVAMV EVLDSPSLFF NGMAGSRMPI AVAHGEGYAE
FADAAAQQRA QDARLVTLRY VDNSGLPTEV YPFNPNGSPQ GITGLTTADG RFSIMMPHPE
RVFRTVQHSW HPDGWGEDGP WIRMFRNARK FIG
